Some of the medi-herbs used for herbal textiles.
\\n\\n
Released this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\\n\\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
\\n"}]',published:!0,mainMedia:null},components:[{type:"htmlEditorComponent",content:'IntechOpen is proud to announce that 179 of our authors have made the Clarivate™ Highly Cited Researchers List for 2020, ranking them among the top 1% most-cited.
\n\nThroughout the years, the list has named a total of 252 IntechOpen authors as Highly Cited. Of those researchers, 69 have been featured on the list multiple times.
\n\n\n\nReleased this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\n\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
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Venkateswarlu",coverURL:"https://cdn.intechopen.com/books/images_new/371.jpg",editedByType:"Edited by",editors:[{id:"58592",title:"Dr.",name:"Arun",surname:"Shanker",slug:"arun-shanker",fullName:"Arun Shanker"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"878",title:"Phytochemicals",subtitle:"A Global Perspective of Their Role in Nutrition and Health",isOpenForSubmission:!1,hash:"ec77671f63975ef2d16192897deb6835",slug:"phytochemicals-a-global-perspective-of-their-role-in-nutrition-and-health",bookSignature:"Venketeshwer Rao",coverURL:"https://cdn.intechopen.com/books/images_new/878.jpg",editedByType:"Edited by",editors:[{id:"82663",title:"Dr.",name:"Venketeshwer",surname:"Rao",slug:"venketeshwer-rao",fullName:"Venketeshwer Rao"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"4816",title:"Face Recognition",subtitle:null,isOpenForSubmission:!1,hash:"146063b5359146b7718ea86bad47c8eb",slug:"face_recognition",bookSignature:"Kresimir Delac and Mislav Grgic",coverURL:"https://cdn.intechopen.com/books/images_new/4816.jpg",editedByType:"Edited by",editors:[{id:"528",title:"Dr.",name:"Kresimir",surname:"Delac",slug:"kresimir-delac",fullName:"Kresimir Delac"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"65506",title:"Endoplasmic Reticulum-Associated Degradation (ERAD)",doi:"10.5772/intechopen.82043",slug:"endoplasmic-reticulum-associated-degradation-erad-",body:'The endoplasmic reticulum (ER) is an extensive network of flattened, membrane-enclosed tubes or sacs that extends throughout the cytosol [1]. ER has important roles in many biochemical processes required for cell survival and normal cellular functions. ER regulates these cellular processes through proteins that are localized in its complex network structures [1, 2, 3]. In addition to protein synthesis, significant cellular activities such as protein transport and folding, lipid and steroid synthesis, carbohydrate metabolism, calcium storage and protein quality control processes occur in the ER [1, 2, 3, 4].
Approximately one-third of all newly synthesized proteins are targeted to the ER and traffic to other organelles of secretory pathway, plasma membrane or the extracellular space [5]. Protein translocation to the ER occurs through Sec61 complex [6, 7]. As synchronized with translocation, protein is exposed to the ER’s oxidizing and calcium-rich environment, which is suitable for protein folding and co- and post-translational modifications such as glycosylation, disulfide bond formation and glycosylphosphatidylinositol (GPI) anchoring [8]. During this folding process, many proteins such as lectin-type molecular chaperones (e.g., calnexin (CNX) or calreticulin (CLR)), HSP70-like chaperone BiP) and enzymes like protein disulfide isomerases (PDI) work in association with each other [4, 9, 10]. Conformational maturation and folding of the proteins in the ER are instantly controlled through the added N-glycan groups to decide whether the proteins are directed to distant compartments via the secretory pathway or included in the refolding cycle [11, 12].
The folding process is not completely accurate. In mammals, 30% of all newly synthesized proteins are estimated to be incorrectly folded [13]. However, genetic mutations, errors in transcription and translation, toxic compounds and cellular stresses such as defects in cellular redox regulation due to hypoxia, oxidants and reducing agents that interact with disulfide bonds in the ER lumen, glucose starvation and abnormalities in calcium regulation lead to a significant increase in the ratio of incorrectly folded proteins [4, 11, 14]. Adequate removal of these unwanted proteins is crucial for protecting cells from proteotoxicity caused by the formation of protein aggregates through the re-opening of hydrophobic residues as well as by unfolded or misfolded proteins that may compete with their properly folded counterparts for substrate binding or for complex formation with partners. Even though the primary damage of these unwanted proteins is restricted to the cell they reside, the damage gets wider if it is a secretory protein [11]. Therefore, there is a robust control via “Protein Quality Control Mechanisms” for the removal of defective proteins in living cells, and thus, only properly folded proteins are allowed to exit from ER lumen to the secretory pathway [11, 15, 16, 17, 18]. When the folding process fails, the terminal mannose residues from the core glycan chain are gradually removed, allowing the proteins to be recognized by mannose-specific lectins and defective proteins are transferred to the 26S proteasome for degradation through the protein quality control mechanism called “ER-associated degradation (ERAD)” [19, 20, 21].
In addition to misfolding proteins, ERAD also targets some proteins that might fold into their native structures under the right conditions and also orphan subunits of oligomeric complexes. The chloride channel protein CFTR (cystic fibrosis transmembrane conductance regulator) is the best example, where it is targeted to ERAD as a consequence of its complex and inefficient folding pathway. The low folding efficiency is further decreased upon mutation as seen in CFTR∆F508. CFTR∆F508 is the most common mutation found in cystic fibrosis patients, can fold and function in plasma membrane; thus, degradation of CFTR via ERAD is obtrusive. ERAD also functions in supporting the correct stoichiometry of multimeric protein complexes by degrading components that are produced in excess of the limiting monomer [22]. For example, the unassembled subunits of T cell receptor-like TCRα and CD3δ are also well-known ERAD substrates [23]. These proteins contain charged residues in the intramembrane sections promoting the assembly of complexes. However, when oligomerization is not proper, these residues might initiate degradation via recruiting specific ERAD factors [23].
ERAD also functions in cell homeostasis by regulating the endogenous levels of many enzymes and signal molecules especially those localized to the ER membrane or plasma membrane under physiological conditions [24]. For instance, ERAD plays a homeostatic role in the regulation of HMG-CoA reductase (HMGR), which is the key enzyme of cholesterol metabolism; apolipoprotein B, an essential secreted protein member of triacylglycerol-rich lipoproteins responsible for the export of lipids, triglycerides and cholesterol; hepatic cytochrome P450 enzyme 3A4 metabolizing endo- and xenobiotics; IP3 receptor, an ER-localized protein allowing Ca2+ release by binding seconder messenger inositol 1,4,5-triphosphate (IP3); type II iodothyronine deiodinase, an ER-localized enzyme converting thyroxin (T4) to the biologically active hormone triiodothyronine (T3) and GABA neurotransmitter receptor responsible for the reduction of neuronal excitability and the tumor metastasis suppressor KAI1 levels [22, 25, 26, 27, 28].
Some viruses hijack the ERAD system through encoding effectors by serving as adaptors that redirect correctly folded molecules towards degradation. US2 and US11, the human cytomegalovirus gene products, induce degradation of major histocompatibility complex (MHC) class I heavy chain, which enables virus-infected cell to avoid detection by the immune system [29]. Similarly, Vpu is a glycoprotein encoded in the human immunodeficiency virus (HIV-1) genome and binds and targets newly synthesized CD4 for degradation [30], allowing them to evade immunosurveillance. Moreover, toxins like diphtheria, cholera and ricin enter the cell by endocytosis and move to the ER. They use the ERAD system to escape from the ER lumen and gain access to their enzymatic substrates in the cytoplasm [31].
ERAD is a highly complicated and regulated mechanism in which the diversity and combination of components change according to the protein to be destroyed [19, 20, 21, 32]. Maturation-defective proteins are removed from the ER lumen or lipid bilayer by retrotranslocation through the ERAD pathway and degraded by proteasome. The ubiquitin system is an integral part of the ERAD and is composed of factors necessary for the recruitment, processing and binding of ubiquitin chains to substrates [24]. In other words, ERAD is composed of steps that include substrate selection, modification with ubiquitin chain, retrotranslocation and 26S proteasomal degradation. Several key molecules such as E1, E2, and E3 enzymes responsible for ubiquitin transfer, channel components responsible for retrotranslocation, chaperones and cofactor proteins function in a synchronized manner during ERAD pathway [12, 19, 20, 21].
This critical role of ERAD in the regulation of cell homeostasis is an evident that ERAD disorders will have important effects on cell survival. Furthermore, it has been shown that aberrations in ERAD function play a role in the pathology of nearly 70 diseases such as cystic fibrosis, α1-antitrypsin (AAT) insufficiency, diabetes, neurodegenerative diseases (Parkinson, Alzheimer\'s and Huntington\'s diseases), viral infection and albinism [4, 33].
In this section, the knowledge related to the basic mechanism and regulation patterns of the ERAD will be summarized and presented.
About 30% of the total proteins and all transmembrane proteins of the cell are synthesized in the ER, which acts as a portal for entry into the secretory pathway via the Sec61 channel [7, 8]. As being translocated, the N terminal hydrophobic signal sequence of newly synthesized protein is cleaved by a peptidase complex [34]. Co- and post-translational modifications such as disulfide bond formation, initial steps of N-glycosylation, and glycophosphatidylinositol (GPI) anchorage take place in the ER.
The oxidizing environment of ER assists the formation of disulfide bonds, which stabilizes tertiary protein structure and facilitates protein assembly. During the folding process, disulfide bonds are formed through the oxidation of pairs of free thiols on cysteine residues by protein disulfide isomerases (PDIs). PDIs act as cycles, and after initial oxidation, disulfide bonds are sometimes isomerized by PDI and ERp57, which is a thiol oxidoreductase, in order to stabilize the correct folding of protein [35]. Conversely, the reduction of disulfide bonds of misfolded proteins is necessary for retrotranslocation step of ERAD. Indeed, PDI enables the retrotranslocation of the simian virüs-40 (SV-40) and cholera toxin [36, 37]. ERdj5, an ER oxidoreductase, reduces disulfide bonds and interacts with EDEM (ER-degradation enhancing mannosidase-like protein) and also accelerates the step of retrotranslocation of SV-40 [37]. ERDJ5 also regulates the degradation of disease-causing α1-antitrypsin variant (null Hong Kong) [38].
Folding is aided by molecular chaperones shepherding against misfolding and unfolding. Chaperone-like glycans bind to N-glycans playing a crucial role in protein folding and degradation. It is apparent that N-glycosylation, quality control of protein folding and ERAD are functionally linked. After entering to the ER, a large majority of the newly synthesized polypeptide chain are being N-linked glycosylated. The oligosaccharyltransferase enzyme recognizes the Asn-X-Ser/Thr consensus sequence in the most of the nascent protein molecule and covalently integrates a high mannose containing core glycan groups (Glc3Man9GlcNAc2) from dolichol localized on the ER membrane to the protein [39]. Due to the very short half-life of triglycosylated form of protein-bound oligosaccharide, glycan processing starts immediately after the transfer of precursor glycan groups through glucosidase enzymes. Following cleavage of two of three glucose residues, the nascent protein could interact with quality control lectins like CNX and CLR. This interaction is preserved until cleavage of remaining glucose residue. After releasing the glycoprotein from CNX/CLR cycle, final glucose is also trimmed creating unglycosylated substrate. This compromises the interaction of substrate with the lectin chaperones. At this stage, if protein is properly folded, it could exit the ER for their final destination. However, if glycoprotein is still unfolded, it is retained in the ER and reglucosylated by UDP-glucose:glycoprotein glucosyltransferase and rebound with CNX and CLR giving protein more time for proper folding [40, 41]. It is not yet understood the mechanisms involved in the termination of reglycosylation/deglycosylation cycles. However, it is clear that, if the polypeptide chain cannot reach its mature form after repeated folding attempts, terminal mannose residues from the core glycan chain are gradually removed by ER α1,2-mannosidase I (ERMan1). ERMan1 produces Man8GlcNAc2 isomer by removing a mannose residue from the middle branch of N-glycans. By this trimming, glycoprotein becomes poorer substrates for reglycosylation and exit from the CNX cycle [11].
The hydrophobic patches of properly folded proteins are usually buried within the interior of soluble proteins. However, those patches could be exposed in misfolded proteins. If a protein has exposed hydrophobic surfaces, BiP binds to it in order to hide these aggregation-prone surfaces for proper folding attempts by preventing aggregation. However, if folding does not succeed or delayed, extended chaperone-misfolding protein interaction serve for a sophisticated process where protein is transferred to other chaperones and/or to the ERAD process [27, 42].
It is well accepted that the first step of ERAD is selection of misfolded proteins by chaperones. As early as 1999, it was found that yeast ERAD substrates strikingly differed in their requirement for the ER-luminal Hsp70, BiP [43]. The degradation of soluble substrates such as pαF and a mutant form of the vacuolar protease carboxypeptidase Y* (CPY*) were dependent on BiP, while degradation of transmembrane proteins Pdr5*p, Ste6-166p, Sec61-2p and Hmg2p occurred in a BiP-independent manner. In 2004, it has been shown that substrates with cytosolic domain such as Ste6-166p were degraded BiP-independently, while proteins with luminal defects required BiP, suggesting that depending on the topology of misfolded lesion (ER lumen, ER membrane and cytoplasm) cytosolic or luminal chaperones function in the recognition and targeting for the degradation [44].
It is possible to study substrate recognition during ERAD using model misfolded proteins. It is clear that de-mannosylation is required for degradation of misfolded glycoproteins since inhibition of this mannose trimming stabilizes misfolded glycoproteins in the ER [45]. Overexpression of ERMan1 accelerates the degradation of N-glycosylated proteins [39, 46]. The resulting Man8-GlcNAc2 containing glycoprotein after this trimming becomes a substrate for EDEM1 (ER-degradation enhancing mannosidase-like protein 1, Htm1p in yeast)—a mannosidase-related lectin in the ER. It was further proposed that misfolded glycoproteins interact with ERManI and EDEM1 for their ERAD, and lectin-carbohydrate interaction found to be crucial for EDEM substrate recognition [47]. Although ERMan1 was suggested to be a biological timer initiating the ERAD of misfolded proteins [48], recent studies revealed that mannosidases are not solely responsible for intensive demannosylation during ERAD, especially under non-basal conditions. Under ER stress (unfolded protein response active) conditions, the transcriptional elevation of EDEM1 enhances the ERAD efficiency by suppressing proteolytic downregulation of ERMan1 [49]. It appeared that EDEMs also play an important role in demannosylation of substrates [50]. EDEM1 also prevents reglycosylation and promotes retrotranslocation and degradation of some ERAD substrates [51]. On the other hand, while mannosidase homology domain (MHD) of Htm1p is necessary for substrate binding, mammalian EDEM1 binds misfolded proteins independent of MHD domain, and therefore, EDEM1 substrate binding may not require mannose trimming or even glycosylation [52]. Thus, in addition to N-linked oligosaccharide moieties of glycoproteins, EDEM1 can recognize the folding lesions of misfolded proteins. In summary, EDEMs are directly or indirectly involved in demannosylation of glycoproteins and/or serve as receptors that bind and target mannose-trimmed proteins for ERAD (Figure 1).
Protein quality control and targeting misfolding proteins to the ERAD.
Truncation of terminal mannose from branch C exposes α terminal α1,6-bonded mannose residues functioning as a recognition signal for ERAD lectins such as OS9 (Yos9 in yeast) and XTP3-B (Figure 2). Through their mannose-6-phosphate receptor homology (MRH) domain, both proteins primarily recognize α1,6-linked mannose j. Additionally, OS-9 also recognizes α1,6-linked mannose e and c [53].
Schematic representation of ERAD using the Hrd1 complex as model.
Several reports suggest that factors (EDEMs, OS9 and XTP3-B) required for substrate recognition and targeting reside within supramolecular complexes and/or interact with important ERAD regulators [54]. For example, EDEM1 interacts with CNX, receives substrates from CNX cycle and facilitates ERAD substrate degradation such as NHK-α1-antitrypsin mutant [55, 56, 57]. EDEM1 also associates with the components of ER retrotranslocation machinery. It is suggested that EDEM1 binds misfolded proteins and uses its MHD domain to target aberrant proteins to the ER-resident glycoprotein SEL1L protein of the Hrd1-SEL1L ubiquitin ligase complex [58]. SEL1L scaffolds several luminal substrate recognition factors and links them to Hrd1. OS9 and XTP3-B also associate with Hrd1-SEL1L complex, which also includes BiP and GRP94 [59, 60]. Furthermore, XTP3-B is proposed to link BiP with Hrd1 complex [60]. According to a hypothesis, these three chaperones (EDEM1, OS9 and XTP3-B) function as oligomers, where one monomer interacts with substrate and another with Hrd1-SEL1L complex [61]. Additionally, EDEM1 also interacts with Derlins, a transmembrane protein, which is a candidate for translocon [62]; furthermore, Derlin2 is shown to enhance the interaction of EDEM1 with a cytosolic AAA-ATPase p97, which couples ATP hydrolysis to the retrotranslocation of misfolded proteins [50].
It is clear that substrate recognition step of ERAD is a complicated mechanism, in which several different enzymes and chaperones having distinct but concerted roles in the ERAD are involved. Moreover, depending on substrates, the number and features of involved proteins vary. For example, concerted roles of EDEM, ERdj5 and BiP in the degradation of misfolded proteins have been suggested [63]. After exiting CNX-CLR cycle, EDEM1 further trims the Man8-GlcNAc2 glycan structure and ERdj5 reduces disulfate bonds. Concomitantly, ERdj5 activates BiP’s ATPase activity. ADP-bound BiP binds to the misfolded protein and holds it in a retrotranslocation component form until it transfers to the retrotranslocation complex [63].
ERAD is also involved in the quality control of non-glycosylated proteins, which is independent of lectin-like proteins. Immunoglobulin light chain (Ig-K-LC), a non-glycosylated ERAD substrate, is degraded in a BiP-dependent manner. Okuda-Shimizu and Hendershot have characterized an ERAD pathway for this non-glycosylated BiP substrate [64] and different protein interaction dynamics seen to play a role in this process. Ig-K-LC has two intramolecular disulfide bonds, and its fully oxidized form does not have ability to pass from the ER to the cytoplasm. BiP interacts with only partially oxidized form of the Ig, preventing the full oxidation of Ig-K-LC and thereby facilitating its release from the ER [64]. Furthermore, a transmembrane UBL domain-containing protein, homoCys-responsive ER-resident protein (HERP), has been implicated as a receptor for non-glycosylated BiP substrates [64]. HERP interacts with Derlin1, and the partially oxidized Ig-K-LC is transferred from BiP to the HERP-Derlin1-Hrd1 complex and subsequently directed to proteasomal degradation [65]. Besides BiP, ERdj5 as disulfide reductase is also indicated to be important for ERAD of non-glycosylated proteins [63]. The non-glycosylated substrates captured by BiP are transferred to ERdj5 for the cleavage of disulfide bonds. Then, these substrates are transferred to SEL1L by the help of BiP for retrotranslocation [63]. Besides BiP, both OS9 and XTP3-B have been implicated in the ERAD of non-glycosylated proteins [12].
Ubiquitin is a 76 amino acid polypeptide encoded on multiple genes. It is ubiquitously expressed in all eukaryotic cells and highly conserved from yeast to human. Ubiquitin can be covalently conjugated to other proteins as monomers or as chains through a complex, highly regulated process called ubiquitination. Although there are reports for evidence of Ser- and Thr-linked ubiquitination, ubiquitin chain is generally attached on the Lys residue on misfolded protein. Lys-6, -11, -27, -29, 33, -48 and -63 are the residues used for ubiquitin linkage. Both the type of ubiquitination (mono/poly) and the linkages of ubiquitin chains affect the fate, localization, stability and activity of target proteins [9].
Ubiquitination has a regulatory role in almost all cellular processes by altering the fate and function of the proteins. The most well-established role of ubiquitination is targeting proteins for degradation by the 26S proteasome, and the most efficient way of targeting proteins to the proteasome is by tagging them with chains of ubiquitin [66]. This targeting requires modification of proteins with chains of four or more ubiquitins attached through lysine 48 (K48) and the specific recognition of these chains by the 19S cap of the 26S proteasome [67]. Mainly Lys-48 but rarely Lys-11-based polyubiquitin chains are reported to bind onto ERAD substrates [68].
Ubiquitination regulates several critical cellular functions, often by mediating the selective degradation of important regulatory proteins. Antigen presentation, inflammatory response induction and cell cycle progression are few examples. As expected, malfunctioning of ubiquitin-dependent proteolysis has implications for cancer and several inherited diseases, such as Angelman syndrome, Parkinson’s disease and Alzheimer’s disease [69].
The role of ubiquitination, however, is not limited to proteasomal targeting. The type of residue that the chain is built is critical for the fate of the ubiquitinated protein. Monoubiquitination has effects in protein trafficking, including endocytosis and lysosomal targeting. Polyubiquitin chains conjugated through K48 or other lysines (often K63) also have effect on proteasome-independent mechanisms, such as DNA repair, regulation of transcription factor activity and protein kinase activation [70].
Ubiquitination is a multi-enzyme process. Three enzymes are involved: E1-ubiquitin activating enzyme, E2-ubiquitin conjugating enzyme and E3-ubiquitin ligase. During ubiquitination, E1 forms a thiol-ester bond between its active cysteine and C-terminal glycine of ubiquitin in an adenosine triphosphate (ATP)-dependent manner. Ubiquitin on E1 is now activated and transferred to the active cysteine of E2 by a trans-thiolation reaction. E3 binds both to E2 and substrate and facilitates the formation of an isopeptide linkage between C-terminal glycine of ubiquitin and an internal lysine residue on substrate. Ubiquitin modification is dynamic and could be removed by deubiquitination enzymes (DUBs).
Today only 2 E1 enzymes and 35 E2 enzymes have been identified in mammals, but there are approximately 100 E3 in yeast and at least 600 in humans [71, 72]. E3s catalyzing the transfer of active ubiquitin moieties on the substrate are responsible for substrate specificity. There are two large families of E3s: (1) HECT [homologous to E6-associated protein (E6AP) C-terminus] domain E3s and (2) RING [really interesting new gene] domain E3s. HECT domain E3s share a 350-residue region harboring a strictly conserved cysteine residue that forms an essential thiol-ester intermediate during catalysis. That is why ubiquitin is transferred to the active-site cysteine of the HECT domain followed by transfer to substrate or to a substrate-bound multi-ubiquitin chain. The RING finger defines the largest family of E3s. RING fingers range from 40 to 100 amino acids and are defined by eight conserved cysteine and histidine residues that coordinate two zinc ions stabilizing a characteristic cross-braced conformation. For RING E3s, current evidence indicates that ubiquitin is transferred directly from E2 to substrate [69, 70].
Ubiquitination step marks ERAD substrates for proteasomal degradation. In yeast, Doa10p and Hrd1p ligases are mainly responsible for ubiquitination of ERAD substrates, but additional E3s shown to contribute to the ERAD under special circumstances [9]. Depending on the topology of misfolded lesion, factors required for ERAD vary. In yeast, three ERAD pathways have been proposed. ERAD-C, ERAD-L and ERAD-M target proteins with lesions in the cytoplasmic, luminal and membrane domains, respectively [44, 73, 74]. ERAD-L substrates use the Hrd1p ubiquitin ligase complex containing Hrd1p, Hrd3p, Usa1p, Der1p, and Yos9p, whereas ERAD-M substrates use Hrd1p and Hrd3p, only in some cases Usa1p [68]. Hrd3p is specifically important for structural integrity of Hrd1p complex. Hrd3p stabilizes Hrd1p, and when it is absent, Hrd1p is auto-ubiquitinated and rapidly degraded. Hrd3p and its mammalian homolog SEL1L also function as an adaptor bridging substrate recognition, ubiquitination and retrotranslocation in Hrd1-mediated ERAD. On the other hand, ERAD-C substrates interact with the Doa10p ubiquitin ligase complex. These three pathways have been identified only in yeast and mammalian has more complicated machinery. Even in yeast, some membrane proteins require both Doa10p and Hrd1p E3s; thus, these pathways could overlap [42].
Although Hrd1p and Doa10p are conserved evolutionary (mammalian homologs: Hrd1 and TEB4, respectively), the number of ERAD E3s in mammals is highly expanded. Besides Hrd1 and TEB4, gp78, RNF5/RMA1, RNF170, RNF185, Trc8, RNF103, RFP2, Fbx2, Fbx6, Parkin, CHIP and UBE4a are other characterized ERAD E3s [9, 27]. Hrd1 and gp78, both homologues to yeast Hrd1p, are the most studied ERAD E3 indicated for degradation of several substrates, some of which are associated with the quality of disease-related proteins. HMG-CoA reductase, apolipoprotein B, cytochrome P450 CYP3A4, CFTRΔF508, z-variant antitrypsin, CD3δ and KAI1 are shown to be degraded via gp78-mediated ERAD, whereas studies have been suggested that Hrd1 is important for the ERAD of GABAb receptor, Nrf2, Pael-receptor mutant tyrosinase, z-variant antitrypsin and gp78 [22, 75, 76, 77, 78]. Only a couple of substrates are known for other E3 ligases. It is also interesting that multiple E3s often function in the degradation on same substrate either in parallel or in tandem.
As Hrd1p in yeast, Hrd1 in mammals functions in a multi-protein complex. While it is complex with EDEM1, Derlins, OS9, XTP-3B and SEL1-L have been linked with degradation of glycosylated substrates (Figure 2), and another Hrd1 complex utilizing BiP, HERP and Derlin1 functions in the degradation of non-glycosylated substrates. Other ERAD factors have also been shown to interact with Hrd1 including UBXD2 and UBXD8 that interact with p97/VCP and recently identified chaperones such as ubiquilin and BAG6. Similarly, gp78, the second major mammalian ERAD E3 enzyme, functions in multiprotein complex in conjunction with E2 enzyme UBE2G2. Besides its diversity on substrate specificity, gp78 also has variety of different partners allowing its communication with proteins on both sites of ER membrane. gp78 uses a VIM (VCP-interacting motif) segment to bind p97/VCP [77] and CUE domain recruiting a multiprotein complex composed of Bag6 and its cofactors [79].
After initial E3-mediated ubiquitin attachment, ubiquitin chain extension (“polyubiquitination”) occurs by the covalent modification of additional ubiquitin monomers onto a Lys residue in a previously linked ubiquitin. This forms an extended isopeptide-linked polyubiquitin chain. In some selected cases, the cooperative extension of a polyubiquitin chain is by the E4s, ubiquitin chain extension enzymes, that facilitate ERAD [80, 81, 82].
The ERAD substrates must be retrotranslocated to the cytosol for proteasomal degradation and the cytoplasmic AAA+ ATPase p97 (VCP or Cdc48p in yeast) is the main retrotranslocation protein providing the mechanical force required for removal of proteins from the ER. It is an essential protein having many roles in diverse biological processes, such as endoplasmic reticulum-associated degradation (ERAD), homotypic membrane fusion, transcriptional control, cell cycle regulation, autophagy, endosomal sorting and regulating protein degradation at the outer mitochondrial membrane [83, 84, 85].
p97/VCP has a multidomain structure including N domain, D1 weak ATPase, D2 major ATPase and C domain [86, 87, 88]. p97/VCP functions as a homohexamer and D1 domain is responsible for oligomerization independent of nucleotide binding. The change in the conformation of hexameric ring by ATP hydrolysis is persistent with its function in retrotranslocation [88, 89].
The diversity in cellular functions of p97/VCP is dictated by the variety of its partner proteins that interact with its N domain. p97/VCP associates with several E3s like Hrd1 and gp78, DUBs like ataxin3 and YOD1 and ERAD accessory factors such as UbxD2 and VIMP. Moreover, many p97/VCP interacting proteins (Ufd1-Npl4 dimer, gp78 etc.) bind directly to ubiquitin. p97/VCP functions as a segregase using the energy from ATP hydrolysis to segregate ubiquitinated proteins from large immobile complexes of ER to the cytosol. This cytosolic protein is recruited to the ER membrane through its interaction with membrane-embedded ERAD components. There are at least seven different ERAD members that could interact with p97/VCP via certain motifs such as VIM motif (gp78 and SVIP), UBX domains (UBXD2 and UBXD8), SHP boxes (Derlin1 and Derlin2) and uncharacterized cytosolic regions of Hrd1 and VIMP that found to have p97/VCP-binding motif [12, 42, 90].
Retrotranslocation is tightly coupled with both ubiquitination and proteasomal degradation. In most cases, inhibiting ubiquitination prevents both degradation and retrotranslocation. The interaction of p97/VCP/CDC48p with its cofactor Ufd1-Npl4 dimer enhances its affinity to ubiquitin (Figure 2). However, it has been also suggested that Hrd1-mediated ERAD requires well-established retrotranslocation machinery, the p97/VCP–Ufd1–Npl4 complex, whereas the gp78 pathway needs only p97/VCP and Npl4 [75].
Many deubiquitinating enzymes (DUBs) in mammalian cells, including Ataxin3, USP13, USP25 and YOD1, are also implicated in the ERAD through physical interaction with ERAD core machinery [72, 91, 92]. Several studies revealed that p97/VCP interacts with DUBs. However, the function of DUBs in the ERAD is still not fully characterized. Otu1p (yeast homolog of YOD1) binds to CDC48p and trims the polyubiquitin chain, resulting oligoubiquitin chains with up to 10 ubiquitin molecules. It has been further suggested that releasing substrates from CDC48p requires DUBs [93]. Consistently, catalytically inactive YOD1 inhibits retrotranslocation of ERAD substrates [91]. In conclusion, many p97-associated DUBs serve as positive regulators of ERAD.
Several putative retrotranslocation channels have been proposed such as the Sec61 complex, members of Derlin family and polytopic E3s such as Hrd1 and gp78. Sec61 is one of the proposed channel protein mutants, which prevented degradation of some ERAD substrates in yeast [94, 95]. Cholera toxin also translocates from ER by utilizing Sec61 [96]. On the other hand, retrotranslocation of some other ERAD substrates has been suggested to depend on Derlins [97, 98], a family of polytopic transmembrane ER proteins linked to some ERAD substrates. Moreover, Derlin1 recruits p97/VCP [99], a key protein of retrotranslocation, which provides energy for the process. Derlin1 also interacts with some E3s like Hrd1, gp78 and RNF5 forming large complexes on the ER membrane [9]. Recently, Hrd1 ubiquitin ligase has been suggested to be the top candidate for retrotranslocation channel [9]. Auto-ubiquitination of Hrd1p in its RING finger domain triggers conformational change allowing the misfolded luminal domain of a substrate to move across the membrane. Thus, it was suggested that Hrd1 forms an ubiquitin-gated protein-conducting channel [33]. It has also been suggested that proteins might exit the ER via the formation of lipid droplets or lipid droplets serve as an intermediate step for substrates en route to the proteasome [100]. However, studies in yeast suggested that lipid droplet formation is dispensable for ERAD-L and ERAD-M [101].
Once retrotranslocated from ER to the cytosol, ERAD substrates should be rapidly targeted to the proteasome for degradation in order to avoid accumulation of aggregates in the cytosol. Consistently, proteasomal inhibition also stabilizes ERAD substrates in the ER lumen. For the coupling of retrotranslocation with degradation, ubiquitinated substrates must be recognized by cytosolic proteins functioning as ubiquitin receptors. Ubiquitin-binding domain containing proteins has ability to shuttle ubiquitinated proteins from retrotranslocation complex at the ER membrane to the proteasome since these proteins interact both with proteasome and p97/VCP. Indeed, it has been suggested that p97/VCP bridges the ER to the proteasome by forming a complex with mHR23B (homolog of yeast Rad23p)-PNGase [102] (Figure 2). In yeast, the substrates are probably transferred from CDC48p to the proteasome indirectly via ubiquitin- and proteasome-binding domains containing shuttling factors Rad23p and Dsk2p [103, 104]. Recently, Bag6/Bat3/Scythe has been characterized as a novel chaperone system with regulatory functions in protein degradation [79]. The chaperone holdase activity of this system keeps some retrotranslocated substrates in a soluble state for proteasome degradation. Bag6, also a partner protein of gp78 E3 enzyme, interacts with proteasome, and proteins like ubiquilin that known as proteasome adaptor proteins suggesting Bag6 might act between p97/VCP and proteasome to hand substrates off from retrotranslocation machinery to the proteasome.
Regulation of ERAD in normal and pathological conditions is also of great importance since hyper-ERAD may cause in loss-of-function phenotypes upon unnecessary degradation of folding intermediates as seen in CFTR and hypo-ERAD may result in gain-of-function phenotypes upon accumulation and/or aggregation of misfolded and unassembled proteins. Several studies suggested different regulation paths for ERAD activity via ubiquitin ligases and their dynamic ERAD complexes, UPR and endogenous ERAD inhibitors.
It is thought that ERAD functions at relatively low levels under basal conditions, but under proteotoxic stress its activity is enhanced. Accumulation of the unfolding or misfolding proteins in the ER lumen triggers “ER stress” by decreasing free chaperone levels [105]. In response to this cellular stress, the pathway known as the “Unfolded Protein Response (UPR)” is activated and results in specific cellular functions classified as adaptation, alarm and apoptosis [4]. Three transmembrane proteins with luminal domains that sense the changes in the ER environment function as UPR sensor proteins are inositol requiring enzyme-1 (IRE1), activating transcription factor 6 (ATF6) and protein kinase RNA-like endoplasmic reticulum kinase (PERK). PERK is a serine/threonine kinase, and IRE1 possesses both kinase and endoribonuclease domains [27, 50]. These sensors initiate signal transduction by sensing the presence of unfolded proteins in the ER lumen and thus control the UPR pathway [15, 18, 106]. All these transmembrane proteins interact with BIP under basal conditions. However, when unfolded proteins are present, BIP dissociates from the UPR sensor proteins. After dissociation of BIP, PERK and IRE1 dimerize and become activated by auto-phosphorylation, whereas ATF6 become translocated to the Golgi and proteolytically cleaved [27, 50]. Activated PERK phosphorylates translation factor eIF2α attenuating protein synthesis to limit protein load. IRE1 activates XBP-1 that enhances transcription of ERAD factors [27, 50]. On the other pathway, ATF6 upregulates many genes that encode ER-resident chaperones and folding assistants like BIP, CNX, CLR and PDI. To summarize, with the induction of UPR in the cell, the overall translation is inhibited for several hours primarily to slow down the entry of newly synthesized proteins to the ER, the amount of chaperones and ER protein folding capacity is increased for proper folding of accumulated unfolded proteins, and thus, the normal ER function and homeostasis are protected [4, 107]. UPR also enhances ERAD capacity by upregulating some of the ERAD genes to ensure that defective proteins are degraded when the folding attempts fail [21, 22, 23]. EDEM proteins, Hrd1, SVIP, OS9 and gp78, are only some of the targets of the ER stress-induced Ire1/Xbp1 pathway [62, 108, 109, 110, 111]. If the cellular stress is consistently increasing, UPR induces cell death mechanisms such as apoptosis or autophagy [4, 14, 112].
It has been suggested that large or prolonged variations such as change in Ca2+ or redox homeostasis, exposure to pathogens and large-scale accumulation of misfolded proteins may induce UPR to adapt ERAD activity. However, smaller or more transient fluctuations on ER load may be overcome rapidly by post-translational pathways that control stability, localization and assembly of ERAD components [23]. For example, reversible ADP ribosylation adapts BIP response for short-term fluctuations [113]. Reversible palmitoylation changes the sub-organelle distribution of CNX [114, 115]. Moreover, many ERAD factors/enhancers, including EDEM1, ER Man1, HERP, OS9, SEL1L and gp78, have fast turnover. This is important since when protein misfolding crisis is over, ERAD activity should rapidly turn back to the basal levels. Many ERAD factors then rapidly degraded via a process called ERAD tuning [23]. ERAD tuning does not require signal transduction from the ER to the nucleus [23]. Hrd1 was suggested to be a central regulator of ERAD tuning. It has been shown that Hrd1 ubiquitinates gp78 E3 enzyme and enhances its degradation, which in turn causes inhibition of gp78-mediated ERAD. Very recently, Hrd1 was also found to regulate the stability of OS9 [116]. Hrd1 also undergoes auto-ubiquitination to induce its own proteasomal degradation [117]. Another homeostatic control mechanism, in which ERAD activity itself is regulated post-translationally and independent of UPR, is degradation of EDEM1, OS9 and SEL1L by the E2 enzyme UBC6e, a component of Hrd1 supramolecular complex [118].
Another type of ERAD regulation occurs via substrate-specific adaptor, as reported for HMGR. The adaptor proteins, Insig1 or Insig2, bind to HMGR only in the presence of 24,25-dihydrolanosterol, an intermediate molecule in sterol biosynthesis. Under low sterol levels, HMGR is stable; however, when sterol levels are high, Insig-HMGR interaction become favored, leading delivery of HMGR to E3 complex following by its proteasomal degradation [119]. Likewise, ERAD-mediated degradations of apolipoprotein and IP3R are initiated when lipid levels are low and calcium levels are high, respectively [23].
DUBs are also proposed as factors that regulate ERAD. As explained above, several DUBs have been reported to interact with p97/VCP and function as positive regulators of retrotranslocation. Additionally, some DUBs are linked with the regulation of E3 enzyme stability. For example, USP19, an ER-anchored DUB, rescues HRD1 from proteasomal degradation and thereby regulates HRD1 stability [120]. Similarly, USP19 enhances the stability and activity of another E3 MARCH6 [121].
SVIP (small VCP interacting protein), a VCP-interaction motif (VIM) containing protein, is the first identified endogen ERAD inhibitor. SVIP interacts with p97/VCP and Derlin1 and inhibits the ubiquitination and degradation of gp78-dependent ERAD substrates [111]. Another endogen ERAD inhibitor is SAKS1. SAKS1 binds to the polyubiquitin chain of the substrate and p97/VCP and attenuates the ERAD process [122].
ERAD activity can also be controlled by hormonal regulation. Glucocorticoids have been suggested to ameliorate ER stress by promoting correct folding of secreted proteins and enhancing removal of misfolded proteins from the ER probably through induction of UPR. Recently, androgen-mediated regulation of ERAD has been reported. Androgen treatment upregulated the expression of Os9, p97/VCP, Ufd1, Npl4, Hrd1 and gp78, but downregulated ERAD inhibitor SVIP, which in turn enhanced the proteolytic activity of ERAD in androgen-sensitive prostate cancer cells [123]. Furthermore, the regulation of ERAD by androgen is mediated via AR and is partially or fully independent on the androgen-mediated induction of IRE1α branch [123].
The authors declare no conflict of interest.
Textiles are susceptible to micro-organisms and their products (e.g. toxins) known to cause infection and intoxication. Myriad textile products such as herbal textiles and clothing are available in the market to support healthy lifestyle and hygiene. Most textile products are meant to come in contact with the skin; hence, herbally treated fabrics are better choice as they do not harbor harmful chemicals and thus are ecofriendly. People of yore used to live in harmony with nature and passionately protected their environment; however, nowadays, excessive exploitation of natural resources has led to a phenomenal increase in environmental pollution. This is taking a serious toll on the lives of all living beings on the planet earth. Right kind of fabric is of paramount importance to a healthy lifestyle, and synthetic fabrics’ teeming with chemicals and dyes poses severe health threat. One would not like to eat a bowl of pesticide-drenched food. Then, why wear clothing doused in chemicals? Textile dyes obtained from natural sources are usually friendly to human skin and are biodegradable and ecofriendly. Some natural dyes have medicinal properties and impart healing qualities to the fabric. They are ecofriendly, save energy, provide rural employment, and preserve traditional craftsmanship [1].
Clothing is our second skin and plays an important role in human life. Textiles finished or dyed from extracts of various medicinal herbs are called herbal textiles. Textiles and clothing infused with medicinal herbs are becoming popular, especially in urban India. The use of such products helps in providing protection against myriad biological toxins and pathogens. Customers demand for new ranges of technology, owing to upward trend in enhancing beauty, that provide better esthetics along with improved health and a sense of relief and satisfaction during use. This trend has produced Cosmetotextiles.
Among technical textiles, medical textiles are a promising product, which plays an important role in maintaining the human health. Medical textiles consist of textiles used in operative and postoperative tasks on and around the patient and medical practitioners. They are broadly classified as nonimplantable materials, implantable materials, extracorporeal devices, hygiene products, protective, and healthcare textiles. Healthcare, disposable, and nondisposable hygiene products mainly used in hospitals to reduce the chances of contamination by biological toxins and infectious organisms.
India has good potential to produce natural dyes commercially as it is considered as 1 of the 17 mega diversity countries globally [2]. Traditional knowledge facilitates the use of plants and their products for healing the wounds and burn injuries and treating the skin infections. Herbal extracts are being used successfully for imparting antimicrobial finish to textiles [3].
Herbal products derived from plants are gaining popularity worldwide for use in textiles on account of their easy availability, green approach, low toxicity, biocompatibility, and ecofriendly nature [2, 3]. Owing to market demand for textile products having added comfort and functional properties, herbal products may be explored for their potential benefits to produce such products. This mandates scientists to devise methods and techniques to use plants containing bioactive agent in producing value added and more attractive functional textile substrates. Insect repellent, deodorizing/aroma, UV protection, antimicrobial, and flame retardant are some of the new properties, which have been imparted recently to textiles. In recent years, the growing demand for herbal products has led to the idea of developing healthcare textile products using herbal extracts.
Currently, herbal colorants are the most attractive option because of high biodegradability, low toxicity, green chemistry, and potential application in the textile dyeing and finishing industry. Natural colorants from plant sources are considered as novel agents in imparting multifunctional properties such as antimicrobial, insect repellent, deodorizing, and UV protection to textiles. Many natural colorants possess some inherent functions in addition to their coloring attribute. These inherent properties are transferred to the textile substrate dyed with an herbal colorant. Alternatively, dyeing textiles with these herbal colorants can combine dyeing with functionality finishes, an ecofriendly process using less water and energy than currently used separate wet treatments. Recently, increased interest in the use of natural dyes in textile dyeing has been observed due to enforcement of the stringent environmental regulations by many countries because of toxic effects of synthetic dyes. This review gives an overview of the herbal methods available at present for dyeing textile materials with aim to provide other useful finishes [4].
Textiles dyed exclusively with herbal extracts without using any chemicals are called herbal textiles. The herbs utilized in dyeing are different from vegetable dyes as they also have medicinal values. These herbs are applied to the fabric using natural ingredients in order to preserve medicinal properties. Further, bleaching of cloth is done by exposing it to sunlight without the use of any chemical bleach. The concept of herbal textiles has been derived from Ayurveda, the ancient Indian method of vedic healthcare. Ayurvastra is a branch of Ayurveda. In Sanskrit, ayur means health, and veda means wisdom, while vastra means clothing when it combines the meaning life cloth [5].
It is made by embedding essential oils and herbs into textiles. A wide range of herbs such as turmeric, tulsi, neem, rose, Indigo, lemon grass, castor, and ber can be used for this process providing medicinal value and aroma to the fabric. Ayurvastra (marketed as cosmetotextiles) has been used for curing several diseases such as diabetes, arthritis, skin infections, hypertension, and hay fever [5].
Herbal clothing is an ancient technique of dyeing textiles in medicinal herbs. This alternative method of treatment originated more than 5000 years ago in India. Its core principles are rooted in the Vedas, which are an ancient book of Hindus. The Vedas date back to around 3000 BC. The science of life or Ayurveda dates back to around 1000 BC. The origins of Ayurveda are also found in the Atharvaveda. It contains incantations and hymns that cure various diseases through mantra. Mythology says that Ayurveda was given to Dhanvantri by Lord Brahma. Charaka Samhita and Sushruta Samhita are the oldest known Ayurvedic texts [6]. About 100 years ago, people from different parts of India were using various forms of natural dyeing in which they repeatedly dipped clothes in herb-based preparations following each wash [7]. These herbs are used traditionally in Ayurvedic treatment and many medical applications. When this fabric is worn, the medicinal property of the fabric is then transferred to the skin. The process of herbal dyeing was developed through extensive research during the age-old dyeing methods practiced since the days of the Indus civilization. Herbs were used to create different colors and to provide various health benefits. The natural/herbal fabrics are 100% organic, completely free of synthetic chemicals, and toxic irritants and are biodegradable [8].
Herbal clothing is prepared from organic cotton fabric impregnated with special herbs and oils for health benefits. Since ancient times, herbal clothing (Ayurvastra) is believed to cure diabetes, skin infections, psoriasis, hypertension, asthma, arthritis, rheumatism, high blood pressure, eczema, and cancer. Antimicrobial property or natural dyes such as indigo, pomegranate, myrobalan, and Indian madder of against bacteria such as Escherichia coli and Klebsiella pneumoniae have been reported [9]. Herbs such as harad, rakta chandana, shweta chandana, and kumkuma are used in Ayurveda for protecting the skin from harmful rays of sun. The herbal preparations act on melanocytes present in the skin, modulate their function, and block the effect of UV rays on the skin. References in different texts of Ayurveda are replete with examples of wearing pure cotton clothes impregnated with herbs such as chandana, haridra usheera, manjista, and nimbi aragwadha to safeguard human body from inclement weather and to keep it healthy. They used herbal products such as soap nut and lime for washing cloths before soaps and detergents were discovered. Herbal textiles and dyes have great vista of applications in diverse walks of human life. These herbal dyes have been used for centuries to produce colors for fabrics, yarns, leather, food, and so on. Natural dyes exhibit better biodegradation and have a better compatibility with the environment. The application of natural dyes has the potential to earn carbon credit by consumption of fossil fuel-based synthetic dye [10].
Skin is the largest sense organ in the human body (Figure 1). It can act as a barrier as well as a medium for entry of certain substances in the body. Several toxins and chemicals present in the environment get accumulated in the conventional clothing and may enter into the body through the skin. Hence, enhancing skin’s ability to resist entry of harmful chemicals and toxins into the body will improve the health. The radiated heat activates herbal molecules of the cloth and is reflected back to the body along with the herbal molecules. Through the blood, the herbal molecules enter deep into the body, show its effects at different levels of the body, and help in curing various diseases [5]. The skin can act not only as a protective barrier but also as a medium for outside substances to enter into the body. In the same way, the skin has the ability to absorb herbs found in our natural dyes. These herbs release their medicinal qualities in the body and strengthen the skin’s ability to block and resist the harmful substances. The close contact of herbal clothing next to the skin enhances the body metabolism, which leads to effective elimination of body toxins. The herb-infused and herb-dyed organic fabrics act as healing agents after the herbs being absorbed through the skin [6].
Structure of the human skin [6].
Skin temperature helps the herbal molecules to be absorbed into the body through sweat pores to manifest the desired medicinal effect.
The cloth should be in direct contact with the skin to manifest its curative effects.
Herbs are garden plants that are grown and harvested for culinary, aromatic, medicinal, and fibrous uses. Plant herbs are placed in the garden for their unmistakable fragrances, attractive textures, appealing colors, and variety of home uses. Due to current ecoconsciousness, there has been a revival of inherent in ecofriendly natural dyes throughout the world. The application of herbal products has given a new direction toward the treatments of various diseases through textile products. The herbs also do not pollute the environment through contamination of water resources in areas close to processing units. All kinds of shades of red, yellow, brown, orange, and green can be obtained with the help of the herbs.
Functional finishes using natural dyes have been in the vogue that promotes an ecofriendly lifestyle. Natural dyes are environmental friendly, nontoxic, noncarcinogenic, nonallergic, and renewable resources. Biosphere is being gifted with more than 500 plant species that yield the natural dyes [11]. The roots, flowers, leaves, seeds, and barks of more than 200 medicinal herbs, plants, flowers, roots, and barks are used to make the dyes. In herbal textiles, the color is gained from the medicinal preparation only, and no other colorants are used. As a result, its properties will last as long as the color is there. Since the herbs make beautiful shades, herbal wears are also becoming very popular for its primordial elegance.
Only herbal preparations devoid of any chemical are used in dyeing herbal textiles, whereas chemicals such as copper sulfate and ferrous sulfate are used as catalysts when dyeing is done with vegetable dyes. Thus, herbal dyes are different from vegetable dyes as they also impart some medicinal value. Herbal clothing is believed to help restore the balance within the body’s systems and strengthen the immune system. Some of the medi-herbs used in herbal textiles give the magical healing quality to the dyed fabric or yarn (Table 1) [12, 13, 14, 15]. Table 1 shows the diseases cured by different herbs.
S. no. | Name of the herb | Medicinal properties | Diseases claimed to be cured |
---|---|---|---|
1. | Neem (Azadirachta indica) | Antibacterial and antifungal | Common skin diseases, skin allergy, controls blood sugar levels |
2. | Curry leaves (Murraya koenigii) | Medicinal value | Beneficial in curing arthritis suppresses pain and reduces inflammation |
3. | Shoe flower (Hibiscus rosa-sinensis) | Controls blood sugars | Diabetes |
4. | Fenugreek/Methi (Trigonella foenum-graecum) | Medicinal value | Controls cholesterol, hypertension |
5. | Amla (Emblica officinalis) | Antifungal, antibacterial, antiviral | Boosts immunity |
6. | Acacia (Catechu) | Antifungal, antibacterial | Used for treatment of parasitic infestation and itching |
7. | Manjistha (Rubia cordifolia) | Medicinal value | Blood purifier and diuretic, leprosy |
8. | Cuscus/Khus khus grass (Chrysopogon zizanioides) | Medicinal value | It helps in fighting asthma |
9. | Arjuna (Terminalia arjuna) | Medicinal value | Cardiovascular support, hypertension, asthma |
10. | Pomegranate (Punica granatum) | Antibacterial, antiviral, astringent | Antimicrobial treatment, hypertension |
11. | Harad/myrobalan (Terminalia chebula) | Antiseptic, anti-inflammatory, controls cholesterol | Hypertension, anemia, asthma cures, wounds, ulcers |
12. | Aloe vera (Aloe barbadensis) | Antibacterial, antifungal | Burns, wounds, common skin diseases, psoriasis, anemia |
13. | Gurhal (Hibiscus rosa-sinensis) | Controls blood sugar levels | Diabetes |
14. | Jamun (Syzygium cumini) | Controls blood sugar levels | Diabetes controls blood sugar levels |
15. | Mahuva (Madhuca longifolia) | Controls blood sugar levels | Control diabetes |
16. | Champa flower (Magnolia champaca) | Controls blood sugar levels | Diabetes, anemia |
17. | Touch-me-not (Mimosa pudica), | Medicinal value | Controls blood sugar levels, diabetes |
18. | Eucalyptus (Eucalyptus globules) | Antiseptic | Relieve congestion, prevent infection, ease muscle soreness |
19. | Tulsi/basil (Ocimum tenuiflorum) | Antibacterial, antiseptic, antispasmodic, diaphoretic, febrifuge, nervine, controls cholesterol | Respiratory disorders, viral, bacterial infections. Controls blood sugar levels, boosts immunity, hypertension, HIV/AIDS |
20. | Chitosan | Antimicrobial | Naturally occurring biopolymer having antimicrobial properties |
21. | Balloon vine (Cardiospermum halicacabum) | Antiphlogistic, analgesic, blood refrigerant, anti-infectious | Cold, fever, renal edema, urinary tract infections,·furuncle, carbuncle, eczema, sprains, external wounds |
22. | Sandalwood (Santalum album) | Alterative, antibacterial, anti-inflammatory, antiseptic, astringent, carminative, disinfectant, diuretic, expectorant, hemostatic, refrigerant, sedative, stimulant | Headache, acute dermatitis, bronchitis, cystitis, eye diseases, gonorrhea, herpes zoster, infection, palpitations, sunstroke, urethritis cools the skin, curing skin itching, burns, its mild fragrance has a soothing effect that helps in fighting stress |
23. | Onion (Allium cepa) | Antioxidant, antimicrobial | Skin diseases, control diabetes |
24. | Indian Madder (Rubia cordifolia) | Antibacterial, anti-inflammatory, antiseptic, astringent, sedative, stimulant | It removes blood impurities and cures various skin diseases, HIV/AIDS |
25. | Indian Mulberry (Morinda pubescens) | Antibacterial, anti-inflammatory | It is blood purifier and used for wound healing, control diabetes |
26. | Saffron (Crocus sativus) | Medicinal value | Controls heart disease |
27. | Indigo (Indigofera tinctoria) | Antibacterial, antiallergy, antiseptic and aromatic, anti-inflammatory properties | Controls cholesterol, helps reducing the insulin resistance, thus controls diabetes, boosts immunity, anemia, skin diseases |
28. | Turmeric (Curcuma longa) | Antihepatotoxic, antioxidant, antimicrobial antiseptic, antiallergic | Fighting skin diseases and helps fight skin disease, anemia, psoriasis, liver disorders |
29. | Henna (Lawsonia inermis) | Blood purifier, anti-irritant, deodorant, antiseptic | Skin irritations such as heat rashes and skin allergies and to cool the body. Because of this cooling property, henna used as a prophylactic against skin diseases like burns, bruises, and skin inflammations, including sores from leprosy |
30. | Brazil wood (Caesalpinia echinata) | Blood purifier, anti-irritant | Skin diseases such as burns, bruises, and skin inflammations |
31. | Castor (Ricinus communis) | Blood purifier | Skin diseases |
32. | Baheda (Terminalia bellirica) | Controls cholesterol | Hypertension, anemia |
33. | Guar (Cyamopsis tetragonoloba) | Controls cholesterol | Hypertension |
34. | Safflower (Carthamus tinctorius) | Controls cholesterol | Hypertension, HIV/AIDS |
35. | Reetha (Sapindus trifoliatus) | Medicinal value | Psoriasis, skin disease |
36. | Amaltas (Cassia fistula) | Therapeutic effect | Psoriasis |
37. | Cluster fig (Ficus racemosa) | Therapeutic effect | Psoriasis |
38. | Winter cherry (Withania somnifera) | Therapeutic effect | Psoriasis, rheumatism |
Some of the medi-herbs used for herbal textiles.
Different parts of the plants namely root, bark, leaf, fruit, wood, seed, and flower are used to extract dyes. It is estimated that over 2000 pigments are found in various parts of plants; however, only about 150 have been commercially utilized [16]. Herbal cloth production by a particular method is accomplished by utilizing extracts of selected herbs for dyeing cotton/silk/linen, yarn, and fabric. Synthetic/chemical dyes are not used at any stage, and for washing, specific products are used [17].
The process of herbal dyeing was developed through extensive research during the age-old dyeing methods practiced since the days of Indus civilization. Manufacturing herbal textile begins with 100% hand-loomed organic cotton or silk wool, linen, jute, hemp, and so on and their natural blends that are dyed exclusively in herbal infusions for both color and health purposes. No chemical process is involved while dyeing and processing the fabric. The fabrics have to pass through various stages of treatment before they are turned into finished products. Herbal textiles are extra smooth and good for transpiration that helps in recovering from various diseases. Each fabric is infused with specific herbs, which are known to cure diseases. It may help to treat a broad range of diseases and skin infections such as eczema and psoriasis; the fabric also helps with conditions such as heart ailments, rheumatism, arthritis, blood pressure, diabetes, and respiratory conditions, such as asthma and sleeping disorders. It also helps in boosting immunity. The antibacterial and anti-inflammatory properties of herbal medicated clothing extend its use as dressings and bandages. It can also relieve the general body aches, stimulate the weight loss, and strengthen the immune system. It can also be used as energy booster; mood enhancer, for overall wellbeing, calming, and blood purification; and cooling [18]. The most effective time to wear herbal cured clothing is when the body is at rest, such as during sleep, relaxation, or meditation because this is when the body is naturally healing and re-establishing balance. Hence, most of herbal clothing products are sleepwear, bed sheets, towels, meditation clothes, and cotton mats [19].
The herbal textile production begins with pure organic yarn/fabric, and each step is carefully and meticulously controlled without the use of any chemical process in dyeing and processing. The process starts with the gray cloth going through various stages of treatment before it is dyed and becomes ready to wear. Only certified organic cotton, natural cotton, silk wool, linen, jute, hemp, and their natural blends should be used for herbal dyeing. The herbal dyeing process has been developed following the extensive research and is in practice since the Indus civilization. Machines are not used to prepare herbal clothing, and all the processes namely bleaching, dyeing, and other processes are accomplished in big vessels fabricated according to need. Further, no chemicals are added during spinning, weaving, or enhancing the appearance [20].
Most common fabric used is organic cotton, the cotton that is cultivated without chemical pesticides and fertilizers. Silk, wool, coir, linen, hemp banana, nettle, and bamboo are also used to prepare herbal clothing. For handloom, the process starts with the cotton yarn and goes through a process named desizing (to remove loose particles, debris, etc.). The common processes used in manufacturing of herbal clothing are detailed in the following paragraphs.
It involves washing of the processed gray cloth with mineral-rich water and sea salt to remove sizing, gums, and oils used in the weaving.
This process is actualized with biodegradable, organic cleaning agents, and surfactants and sun dried. The bleaching of cloth is done naturally by exposing it to sunlight on a natural grass base and by using animal manure. The fabric or yarn is first bleached using cow urine, milk, honey, along with biodegradable, naturally derived, organic cleaning agents, and surfactants such as Saptala (Acacia sinuata) and Phenila (Sapindus mukorossi) [21]. Many Ayurvedic doctors consider cow’s urine highly beneficial in balancing an individual’s “doshas” or basic constituents of an individual’s physiology and psychology, strengthening the immune systems and as an elixir in giving life [22]. The process ends with exposing the fabric or yarn directly to sunlight.
To make the colors look bright and retain color fastness, natural mordants such as myroballans, rubhabs leaves, oils, alum, fruit extracts of haritaki, bark of lodhra, minerals, and iron are used. Use of heavy metallic mordants such as copper, chrome, zinc, and tin is avoided as they are not ecofriendly. Mordanting is done before dyeing the fabric or yarn to make the colors look bright and retain fastness.
The word medication is used instead of dyeing because the medicinal herbs are used to impart required color to fabric or yarn [20, 23]. The yarn or fabric is then medicated in a carefully controlled mixture of herbal medicinal preparations depending on the disease or ailment being treated. Required herbs are applied directly to the fabric with the help of natural ingredients so as to keep the medicinal value of herbs intact [7, 11]. Steps involved are as follows:
The organic cotton yarn/fabric is dyed carefully with concoction of herbal dyes indicated for the treatment of desired disease(s).
The herbal dyes are prepared by careful blending of medicinal herbs derived from plants, flowers, roots, and barks.
The temperature, duration, number of the soaks, blend of herbs, and equipment are carefully controlled.
Desired herbs with the help of natural ingredients are applied directly on fabric in order to preserve the medicinal value of herbs.
Shades of red, yellow, brown, orange, and green can be obtained with careful use of herbs.
Finally, the medicated cloth is cooled and washed several times to remove the nonabsorbed particles and always dried in shade.
The finishing process used after herbal dyeing is also organic and is given by sprinkling pure water on the cloth and then stretching under pressure, using hand rolls, Aloe vera, castor oil, and so on [7, 11].
After dyeing, residue can be recycled. Solid and liquid wastes are separated by the filtration and used for farming purposes—as biomanure and for watering the fields and also to generate the biogas [11].
Herbal textile is made by embedding essential oils and herbal extract finishes into textiles. Such textiles have their applications in providing medicinal value and aroma to the garment. Microencapsulation, sensory perception technology, liposomes, dyes, and coated textile technology are used for incorporating the herbal drugs and oils in textiles. The temperatures of the finish, the duration and concentration of plant extract, the blend of herbs, and even the equipment used are carefully controlled [24].
Spray drying, air suspension coating, solvent evaporation, sol-gel microencapsulation, and in-situ polymerization are some commonly used techniques used for textile finishing by microencapsualtion. For encapsulation of flavor, fragrance, and oils, spray drying is used in which core particles dispersed in a polymer solution and sprayed into a hot chamber leading to solidification of shell particles on core material and polynuclear or matrix-type microcapsules are obtained. Air suspension coating is done by suspending solid particles of core material in a hot or cold upward moving steam of air. Coating material may be derived from cellulose derivatives, dextrins, emulsifiers, lipids, protein derivatives, and starch derivatives, which is atomized through nozzles into the chamber and deposits as a thin layer on the surface of suspended particles. Solvent evaporation is a process in which the drug is dissolved, dispersed, or emulsified in an external aqueous or oil phase; it has been used to impart antifungal finish to textiles. Sol-gel microencapsulation is used to produce flame retardant, water/oil repellent, UV protecting, antiwrinkle, self-cleaning, flavor and odor containing, and antibacterial textiles. Sol-gel synthesis involves the hydrolysis of silicone monomer and the condensation of silica into a porous structure with a three-dimensional networked structure, which can be tailored for a wide range of useful properties.
Microencapsulation, widely used in textile finishing, is a process in which small capsules having desired properties are prepared using small particles/droplets surrounded by a coating material. The material inside the microcapsule is known as core material, whereas outer coating is called a shell. Microcapsules may have diameter ranging a few micrometers to a few millimeters. Many special and functional properties can be imparted to the fabrics by microencapsulating the core material. This core material can be any substance having a special function to perform for the fabric. Encapsulation has allowed moisturizers, therapeutic oils, and insecticides to be incorporated into fabrics. Microencapsulation of antimicrobial agents is also gaining popularity in sportswear and medical textiles [25].
For preparation of herbal textile by microencapsulation, the “core material” along with the wall material should give a durable finish. This wall material can be certain substances like gum acacia, and the core material is the desired herbal extract. The microencapsulated herbal extracts have shown antimicrobial activity and wash durability up to 20 washes [26]. Microencapsulation is a very popular technique for incorporating fragrance into fabrics. These capsules applied are unbreakable under the normal conditions, and the application of pressure on fabric releases fragrance, which causes healing in aromatherapy [27]. Microencapsulated herbal extracts such as Aloe barbadensis Mill, Bitter Gourd, Ginger, and Cuminum cyminum Linn have successful application in which the herbal extracts are used as core material and gum acacia as wall material [28]. According to the study, microencapsulated extracts of Andrographis paniculata, when applied on the fabric to impart mosquito repellency finish, gave good mosquito repellent activity up to 30 washes [29].
New textile technologies have enabled the application of cosmetic ingredients on fabric to provide its functional benefit to the end-use product, and therefore, cosmetic textiles are moving from laboratory to showrooms. Fragrance finish is one such finish that falls under this category. A fragrance is made from a pleasant smelling aroma compound. Aromachology is a science that studies the effects of fragrances on the human body and mind. It researches how scents can be used to induce relaxation and make life more pleasant. Fragrances can be used in various forms such as essential oils, perfumes, colognes, household products, and potpourri. Some areas in textiles where fragrance finish can find application include Cosmetotextiles.
The major use of microencapsulation in cosmetic textiles is in the application of vitamins, essential oils, skin moisturizing agents, skin cooling, and antiaging agents [30]. Yamato et al. studied microcapsules having active substances that can improve the physiological conditions of human skin. The microcapsule gradually released its content when the textile structure was subjected to light pressure created due to the movement of human body [31].
Aroma finish is a process by which textile material is treated with the pleasant odor producing essential oils and aromatic compounds so that the wearer gets beneficial effects. Various essential oils such as lavender, rosemary, and jasmine are used.
The fragrance compounds and the essential oils are volatile substances, and prolonging life span of their odor is most difficult task in preparation of the textiles for aromatherapy. Microencapsulation is an effective technique to achieve this task. Microcapsules are tiny spherical enclosures containing a liquid or gas and assume the shape of the enclosed particle if containing a solid [32]. With microencapsulation method, fragrance lasts for more number of washes since microencapsulation makes the finished particles more securely attached to the internal structure of the fiber and thus releasing them slowly [33].
Bacteria often cause decay of fabrics leading to loss of various useful properties of fabrics. This problem can be prevented by the use of antimicrobial finishes that can be applied with the help of microencapsulation. This finish is especially beneficial for textiles for medical and technical uses [34].
Herbal extracts prepared from Chamomile, sage, and green tea were applied to cotton fabric using pad-dry-cure method. Treated fabrics exhibited antimicrobial activity against Gram-negative, Gram-positive bacteria and yeasts. This antimicrobial activity was retained even after 10 cyclic washes [35].
Textile materials having antimicrobial activity are used in hygienic, health, personal care, and surgical products. Some products include baby and adult diapers and sanitary pads. Most of the diapers are made by synthetic materials, which are nonbiodegradable and poor antimicrobial properties, and may cause rashes and dermatitis. Natural antimicrobial coatings on diapers obtained by using curcumin, Aloe vera, tulsi, and neem have same antimicrobial effect when compared with synthetic antimicrobial coatings [36]. Curcumin or diferuloylmethane (1,7-bis(4-hydroxy-3-methoxyphenyl)-1,6-heptadiene-3,5-dione) is the main phytochemical present in turmeric. This polyphenolic compound has several biological activities including antimicrobial activity. Curcumin is suspected to affect the bacterial cytoskeleton, thus producing the antimicrobial effect [37]. The Aloe vera leaves secrete a colorless gel-like substance, which contains about 98–99% water and 1–2% active compounds such as aloesin, aloin, aloe emodin, aloe mannan, flavonoids, saponin, sterols, amino acids, and vitamins. Anthraquinones and their derivatives such as barbaloin-IO-aloe emodin-9 anthrone, isobarbaloin, and chromones, which inhibit the bacterial protein synthesis, are potent antimicrobial agents [38]. Antimicrobial property of tulsi (holy basil) may be attributed to essential oils found in leaves. These essential oils contain germacrene-A, clemene, caryophyllene, eugenol, and caryophylline oxide. Additionally, tulsi leaves also have other biologically active phytochemicals such as rosmarinic acid, oleanolic acid, and ursolic acid. These essential oils and phytochemicals have antibacterial properties owing to their damaging effect of bacterial cell membrane and thus causing leakage of cellular potassium [39]. Neem leaf, bark, and seeds have antimicrobial properties, and it is high, moderate, and low, respectively. Neem contains several bioactive constituents like azadirachtin and other compounds such as nimbolinin, nimbin, nimbidin, nimbidol, sodium nimbinate, gedunin, salannin, quercetin, nimbanene, 6-desacetylnimbinene, nimbandiol, nimbolide, ascorbic acid, n-hexacosanol and amino acid, 7-desacetyl-7-benzoylazadiradione, 7-desacetyl-7-benzoylgedunin, 17-hydroxyazadiradione gedunin, and nimbiol. Quercetin and β-sitosterol, polyphenolic flavonoids purified from leaves of neem have antifungal and antibacterial activities. Neem (Azadirachta indica) in plant parts shows antimicrobial property through bacterial cell wall breakdown [40].
Wet processing of textile substrates from its preparatory stage to dyeing and then finishing is important for enhancing its esthetic value, removal of impurities, color shade, color pattern, and requisite functionality. Some of the traditional processes used in herbal finishing involve an excessive use of water, energy, and chemicals. Recently, due to global concerns on environmental pollution, sustainability mandates the development of sustainable dyeing and finishing processes using plant waste and nonfood plant extracts [41]. Based on environmental friendly, plant-based products having biocompatibility, biodegradability, and nontoxicity along with insect repellent, deodorizing, flame retardant, UV protection, and antimicrobial activity are in great demand all around the world for producing more appealing and highly functional value-added textiles [42, 43, 44, 45]. A wide variety of finishing chemicals from plants are now available in the market that matches the expectations of consumers [46]. Various plants reported as source of natural dyes are teak, mahogany, ketapang, tamarind, mangosteen, mango, suji, pandan, indigofera, guava, banana, and onion [47]. Plant parts including roots, leaves, twigs, stems, heartwood, bark, wood shavings, flowers, fruits, rinds, hulls, husks, and the like used to produce herbal dye. Additionally, most of the herbal dyes have inherent medicinal properties [48].
Natural fibers such as cotton and wool are susceptible to microbial growth and even dust mites because they retain oxygen, water, and nutrients. Hence, antimicrobial finishes should be applied to textiles to destroy or suppress the growth of microorganisms and also to protect the textiles from strength and color loss, unpleasant odor, and quality deterioration [49]. Micro-organisms may deteriorate the clothes in a closet, curtains, carpets, bed, bath and kitchen linens, pillows, and mattresses. Several microorganisms also thrive on the skin, while dust mites live on skin cells sheded on sheets, towels, and clothing. A hospital houses an immense amount of textiles with high volumes of traffic. Because of the constant flow of people, especially those with infectious diseases, specific finish hospital uses are required. Patients, caretakers, and hospital staff are at risk of acquiring infection as inherent properties of the textile fibers susceptible to the growth of micro-organisms.
In past, natural dyes were applied to textiles for simultaneous coloration and antimicrobial finishing successfully. Finish imparted by catechu on wool was found to be effective against Escherichia coli, Staphylococcus aureus, Candida albicans, and Candida tropicalis. Observed antimicrobial characteristics and negligible cytotoxicity of catechu indicated the dye as a promising antimicrobial agent for developing bioactive textile materials and herbal clothing [50, 51]. Several natural, nonmetallic, and antimicrobial finishes exist, and one of such antimicrobial finish is chitosan, a deacetylated form of chitin, which is a main component in crustacean shells and reported to be effective against both Gram-positive and Gram-negative bacteria [52]. Many antimicrobial textiles are produced with the combinations of bioactive substances to enhance the antimicrobial efficacy of the finishes and counteract the negative aspects of the treatments. By combining finishes, the occurrence of drug-resistant strains arising from the finish is reduced.
Pure cotton woven/knitted fabrics treated with the selected medicinal 16 medicinal herb extracts such as neem, turmeric, holy basil, and sandal wood have been evaluated for curing seven different diseases such as allergic dermatitis, psoriasis, asthma, liver disorders, headache, joint pain, and sinus trouble/cold. Seven different types of curative garments have been developed. The antibacterial assessments of the medicinal herb extracts treated fabrics and clinical trials have confirmed the correlation between the curative performance and its antibacterial activity. The curative property of the garments in all the cases was found to be significant and lasted for 10–15 washes [53].
Although known since long for dyeing and medicinal value, the protective properties of herbal dyes have been noticed only recently. Several plants used for dye production are classified as medicinal, and some have recently been shown to possess significant antimicrobial activity. Several natural dyes have demonstrated to possess antimicrobial activity like curcumin from turmeric; naphthoquinones such as lawsone from Lawsonia inermis, juglone from walnut, lapachol from taigu, and catechin from Acacia catechu; and several anthraquinones from Rubia tinctorum, Rubia cordifolia, Rheum emodi, Punica granatum, and Quercus infectoria [54, 55]. These natural antimicrobial agents may significantly reduce the risk of infections especially when they are used in close contact. Natural bioactive compounds present in natural dyes/pigments have also been reported as significant antimicrobial agents for finishing in green dyeing procedures.
Ultraviolet (UV) rays, electromagnetic spectrum between visible light and X-rays, influence the physiology of living organisms. Exposure may cause tanning to skin cancers. Sunscreen lotions and clothing provide protection from dangers of UV rays. Change in construction parameters of fabrics with appropriate UV absorbers and adequate finishing methods may be used to prepare the UV protective fabrics.
Textiles, as a protective shield against solar radiation, have been since ancient times. Textile structures provide the desired characteristics such as pliability, good mechanical strength, softness, esthetics, and other engineered properties, which are required for preparing good sunscreening apparels. Textiles themselves are not able to provide effective protection against UV rays; hence, UV blocking agents should be applied over the fabric to make them UV protective. Quantum of protection required for different skin types is determined by UV radiation intensity and distribution subject to geographical location, time of day, and season. Several UV protection agents have been developed to enhance the UV protection offered by different textiles. Both organic and inorganic UV blocking agents are available. The organic blockers are also termed as UV absorbers because they absorb UV rays, whereas inorganic blockers scatter them [47].
Three yellow dyes obtained from Rheum emodi, Gardenia yellow, and curcumin have been successfully used for simultaneous dyeing and functionalization of silk to render its UV protective [56]. Wool fabric dyed with dye obtained from the eucalyptus leaves using pad-batch and pad-dry techniques showed ultraviolet protection factor (UPF) values ranging between very good and excellent [57]. UV protection properties of chlorogenic acid, the main ingredient of water extract from honeysuckle, on wool have been studied. The wool treated with honeysuckle extract showed good UV absorbance; thus, extract of honeysuckle may be developed as a natural UV-absorbing agent [58]. Natural plant colorants such as madder (Rubia tinctorum) and indigo (Indigofera tinctoria) and of insect origin cochineal (Dactylopius coccus) were applied on cotton fabrics, and indigo was found to have higher UPF values [59]. UV rays induce DNA damage, oxidative stress, and inflammatory processes in skin. Rheum emodi contains anthraquinones (rhein, emodin, aloe-emodin, chrysophanol, physcion, and rhein), stilbenoids (resveratrol and piceatannol), and flavonoids. UV protective effect of Rheum emodi is supposed to be due to flavonoids, which absorb the UV radiation [60]. Main coloring ingredient of the dye extracted from Gardenia yellow is crocin, which is a water soluble carotene, which absorbs the UV rays [61]. Curcumin alleviates the effect of UV rays by reducing the transmittance of UV light across fabric [62]. Madder roots contain anthraquinone derivatives mainly purpurin and munjistin and also small amounts of rubiadin, nordamncanthal, pseudopurpurin, and xanthopurpurin. Anthraquinones are considered to be strong UV absorbers [22].
Bacterial growth and/or waste released from human body are the main causes for odor in garments. Recent advances in textile manufacturing have improved the performance of textiles with respect to odor with antimicrobial and UV protection properties. To meet the consumer’s growing demand for hygienic clothing, extensive research has been done to deodorizing property to textiles with the application of natural colorants. The deodorizing performance of fabrics dyed with herbal colorants has been compared, and pomegranate was found to be best among gardenia, Cassia tora L., coffee sludge, and pomegranate rind [23]. Fabric dyed with gallnut recorded a better deodorizing function against ammonia, trimethyl amine, and acetaldehyde than control fabrics. Dyed fabrics also found to possess an excellent antimicrobial activity against Staphylococcus aureus and Klebsiella pneumoniae [20]. Young-Hee Lee and co-workers dyed cotton, silk, and wool fabrics with pomegranate (Punica granatum) and showed excellent deodorizing property in the dyed fabrics [21]. Cotton fabrics dyed with C.I. Direct Blue 200, a copper complex direct dye, and pre- and post-mordanted with Cu(II) sulfate for deodorization of ethyl mercaptan showed that deodorization effects increased quadratically with the copper ion uptake [63]. These studies indicate that natural and synthetic dyes can be utilized for deodorizing functionalization of textiles.
Carpets, blankets, and shawls are prepared from wool, and other similar fibers have properties such as warmth, softness, and flame retardancy protein content of the fiber, which are susceptible to attack by moth as its larvae thrive on the protein present in the wool. Cloth moth (Tineola bisselliella) and carpet beetle (Anthrenus verbasci) are common moths, which attack the wool items. Dichlorodiphenyltrichloroethane (DDT), permethrin, permethrin/hexahydro pyrimidine derivative, and cyhalothrin are some of the insecticides used to provide antimoth finish. Nano titanium oxide particles have also been utilized as an antifeeding compound on wool fabric to kill larvae of the carpet beetle, Anthrenus verbasci, which feeds on wool fibers [64]. Chemicals used for antimoth finishing are detrimental to the environment; hence, natural colorants may be good alternatives. Shakyawar et al. used saffron flower waste, onion skin, henna, myrobolan, silver oak leaf, madder, walnut, dholkanali, and yellow root natural dyes for antimoth finishing and recorded the best results for silver oak leaves, walnut husk, and pomegranate rind [65]. Natural dyes from cochineal, madder, walnut (quinines), chestnut, fustic, indigo, and logwood (flavonoids) were also applied on wool, and their antimoth properties against black carpet beetles were tested, all except indigo, which increased the insect resistance of the wool fabric. Metallic mordants were found to have no significant effect on insect resistance with all natural dyes used. The anthraquinone dyes including cochineal, madder, and walnut were found to be quite effective in protecting wool fabric against black carpet beetles [66].
Synthetic/chemical dyes are increasingly being banned for use in the textile industry, which have led to severe blow to the handloom industry. At the same time, textiles dyed with natural herbal dyes having medicinal attributes are commanding a huge market due to their inherent advantages. Nowadays, the use of herbal dyes in the textile industry is preferred owing to the advantage of dyes extracted from the medicinal plants, origin from the renewable resources, limited chemical reactions involved in their preparation, biodegradable properties, disease-curing properties, and ecofriendly in nature [18, 67].
Herbal textiles are of two kinds: one category is for curing diseases and the other is for wellbeing. The first category of cloths, which are used for curing diseases, includes sleep wear, bed sheets, towels, meditation clothes, and coir mats. Herbal textiles are mostly used in making such garments that stay close to human skin, so that all the medicinal components could be absorbed through the skin. Herbal textiles can fetch more competitive than conventional fabrics owing to low production cost. For example, a common chemical dye costs around $75 per kg, and a herbal dye costs approximately $5 per kg. Most of the herbs used in dyeing are cultivated in South Asian countries, namely India, Pakistan, and Bangladesh, India being the largest producer. The Handloom Weavers Development Society (HLWDS) of Kerala, India has exported herbal and organic textile worth Rs. 50 Lakh to the United States, Europe, and Japan. The herbal textile is gaining such popularity that the Japanese Government has accorded HLWDS a $40,218 grant. Large consignments of herbal textiles have been shipped to international markets of the United States, Canada, France, Denmark, Italy, Poland, Maldives, Mauritius, Japan, and Sri Lanka [17, 68, 69, 70].
Most effective time to wear the herbal-infused clothing is while resting, sleeping, or meditating, when the body is naturally healing and re-establishing balance, so many of the products are created with these factors in mind. The technique for producing the herbal textiles is also used for floor coverings and coir mats. For coir mats, the fibers are first soaked in herbal dyes and then woven into coir mats. Apart from medicated handloom clothes such as sarees, T-shirts, shirts, trousers, kurtas, dhods, chudidhars, nightwear, fashion wear, sportswear, and inner wears, caps for healing headaches, goosery caps for head balance, cooling caps, hair shining caps, hair strengthening caps, bandages, and mask are also prepared [68, 71].
Plant dyes are increasingly being incorporated by designers into their designs contributing to revival of Ayurvastra or herbal clothing. Ayurganic is a line of loungewear inspired from the concept of Ayurvastra. Designer duo Lecoanet and Hemant have revived the tradition of Ayurvastra in Ayurganic, their line of medicinal clothing. The multi-award winning designers who began their journey as couturiers in Paris are now refining the concept of Ayurvastra. Anjelika dreams organic produces fair trade, organic handmade clothing that follows this tradition. Gibie towels specialize in Ayurvastra towels, Ayurvastram in Ayurvastra textiles and yoga mats, and niraamaya in Ayurvastra yoga mats. The handloom weavers’ development society in India is producing a wide range of herbal fabrics including sarees, bed sheets, and dress materials using medicinal dyes and exporting them to the United States, Germany, the United Kingdom, Singapore, and Taiwan [6, 11].
“Herbalfab” ecofriendly fabric brand has developed a unique technique to dye with flowers, fruits, roots, and so on. Turmeric, myrabolams, onion, kesu and dhavadi flowers, and natural indigo are used for preparing the natural dyes. This prevents the water pollution by replacing the petrochemical dyes with herbal dyes and imparts the medicinal value to cloth. The colors obtained are unique, which can kick start a new fashion trend. Herbalfab also encompasses a range of other ecofriendly fabrics like khadi, which is handspun and handwoven, nonviolent silk, organic denim, and so on [72].
The Handloom Weavers’ Development Society, India produces a variety of home textiles using herbal fabrics in India. They also export herbal clothing such as sarees, bed sheets, and dress materials to other countries. With increasing demand for herbal clothing, companies such as Ayurvastra online have started offering the online products. Many textile industries are getting inclined toward Cosmetotextiles. The brands making herbal clothes are Aura, Cognis, Pantaloons, Quiospheres, and so on. These brands have a range of clothing namely bandee, vest, camisole, men and women’s tee, coirs, and so on [73].
It acts as a revitalizing tonic and helps in keeping the body fresh and healthy. The uses of proper herbs in the textiles have proven to cure diseases such as arthritis and fever. We breathe through our body more than we do through nose. It can improve the skin’s natural ability to block and resist the harmful chemicals and toxins from entering the body, which will be beneficial to health.
Herbal cloths have the ability to protect us from various skin diseases and provide relief from infectious diseases and mental ailments.
No synthetic/chemical dye is used at any stage of herbal cloth production. For washing and cleaning purpose, the nut or nut powder of Sapindus laurifolia is recommended [74].
Medicinal herbs treated fabrics also have a lot of therapeutic value; thus, the fabric has been found very helpful for people suffering from ailments such as skin allergies, breathing problems, sleeping disorders, and blood pressure.
The health benefits of herbal clothing and its usage depend on the theory of touch. The body loses toxins when it comes in contact with herbal clothing, and this improves the metabolism. Herbal clothing is also known to help fight against many common diseases such as diabetes, hypertension, skin allergies, asthma, and heart ailments.
The human body naturally heals itself during sleep or meditation. Thus, when the body is at rest, herbal clothing will work most effectively. The skin is known as the largest organ of the body. Not only it acts as a fence and protects the body, but it can also be the channel for outside germs and toxins to enter into the body. Herbal clothing guards against the harmful toxins trying to enter the body through the skin [75, 76].
Herbal textiles are mainly used in making sleepwear, undergarments, bed coverings, towels, meditation clothing, and so on, which remain close to the skin absorbing all the benefits it gives out. Herbal textiles are also used in home textile products such as mattresses, coir mats, door mats, bath towels, bed spreads, and carpets.
Some of herbal constituents are antiallergens and hence are safe for skin contact and are mostly nonhazardous to human beings.
Natural dyes are usually moth proof and can replace the synthetic dyes in kids’ garments.
We breathe through our skin more than we do through nose, and chemically dyed textiles having carcinogenic amines and chemicals may be allergic and dangerous to human skin. Organic clothing can help reduce the exposure to allergens and other irritants and give a comfortable feeling [77, 78, 79].
Preparation of herbal cloths is a labor-intensive industry and hence will provide the job opportunities for manpower engaged in cultivation, extraction, and application on textile, food, leather, and so on.
Use of natural dyes may earn the carbon credit as it reduces the consumption of petroleum-based synthetic dyes.
It promotes the agriculture and balances the ecological cycle.
Waste can be used as manure.
No heavy metals such as chrome and copper are used in natural/herbal Ayurvedic dyeing.
Manual farming and organic practices have a lower carbon footprint as the entire process consumes less fuel and energy and emits fewer greenhouse gases than chemical textiles.
Herbal dyes are extracted from the plants cultivated without the use of synthetic pesticides and fertilizers, and also no chemical defoliants are used.
Processing is in green environment; hence, workers’ health is not compromised, and also water and electric use and toxic runoff are reduced.
Stringent testing ensures that product is free from contaminants such as nickel, lead, formaldehyde, amines, and pesticides.
It improves the soil fertility and soil structure by increasing the soil activity, thus reducing the risk of erosion.
It is the massive saving of precious water.
It promotes the development of earthworms and other arthropods leading to improvement in the growth conditions of the crop. Furthermore, organic crops thrive on root symbioses and are better equipped to exploit the soil; hence, fields can accommodate a more number of plants, animals, and microorganisms [80, 81, 82].
Natural fibers and natural dyes used in the preparation of herbal clothing allow its natural breakdown without damaging the environment compared to the synthetic material, which takes hundreds of years to breakdown and leaves the pollutant material in soil [66, 67, 83].
Herbal textiles are ecofriendly, and also residues they produce can be further used for making the other green products.
Solid and liquid wastes from herbal dyeing are amenable to recycling producing the organic manure.
Some of the ecofriendly industries producing the herbal textiles produce organically recycled paper bags by utilizing the residual organic and herbal dyed fabrics that can reduce the pollution due to plastic bags [84].
It also promotes the cultivation of herbs required for the production of herbal textile products.
Herbal dyes add value to the cotton fabrics in ecofriendly manner.
Herbal fabrics are lightweight and so used to construct the perfect breezy clothes. The biggest advantage of cotton herbal cloth is that it is cool in summer and warm in winter [85, 86].
The color shades produced by herbal dyes are unique, hence commanding high demand in market.
Herbal fabrics and dyes are not good substitutes for synthetic dyes offering broader range and variations.
Retaining color and its herbal benefits demands utmost care in washing; herbal cloths should be washed separately, preferably hand wash or gentle machine wash with bleach-free detergents and should be shed dried. This causes inconvenience to the user.
The dyeing process is cumbersome and time taking, and each stage should be carefully controlled.
Medicinal herbs impart colors; hence, color choice for consumer is very limited as only few herbs can be used for dyeing a fabric that meant to be used in a particular disease condition.
Herbal cloths show the curative effects, but progress is slow.
Though there are no complaints on allergic reaction by the consumers, some people think that the herbal clothing shows side effects on children [87, 88, 89].
Textile industry has realized its negative contribution to the environmental pollution through the harmful chemicals used in manufacturing processes and is continuously trying to find solution for this problem. Herbal dyeing is one important step toward achieving the organic lifestyle, thus reducing the environmental pollution. Herbal textile products are devoid of pesticides, fertilizers, antibiotics, growth hormones, genetically modified organisms, additives, irradiation, or sewage sludge, hence avoiding many ailments that are common with conventional clothing.
Modern consumer’s demand for novel ecomaterials is expected to increase in future. Recently, efforts have been made toward the development of commercially viable natural colorants by making advances in aspects such as identification of new sources, formulations, extraction, purification, and stability techniques. In spite of enthusiastic studies discussing the socioeconomic viability of natural dye production and applications at commercial scale for sustainable utilization of bioresources, there is a need for investigations related to hygiene and ecosafety, which have great future for the discovery of relatively better and more stable natural pigments that may have wider industrial applications.
Herbal textiles have tremendous scope in world textile market and may become a major textile product in future. The blend of herbs and textiles to achieve the health in an ecofriendly manner is the great way of adopting the healthy life. Herbal clothing is receiving the increased awareness all over the world. Herbally treated textiles are one of the great solutions to revive and increase the share of Indian handloom industry in world textile market. Furthermore, herbal clothing is nontoxic, noncarcinogenic, biodegradable, and ecofriendly; these characteristics make them an obvious choice for modern informed costumer looking for a healthy product. Additionally, the production of biocolorants to meet the rising demand shall force entrepreneurs to take up this venture for greater profits leading to more employment generation.
As an Open Access publisher, IntechOpen is dedicated to maintaining the highest ethical standards and principles in publishing. In addition, IntechOpen promotes the highest standards of integrity and ethical behavior in scientific research and peer-review. To maintain these principles IntechOpen has developed basic guidelines to facilitate the avoidance of Conflicts of Interest.
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\\n\\nA Conflict of Interest is a situation in which a person's professional judgment may be influenced by a range of factors, including financial gain, material interest, or some other personal or professional interest. For IntechOpen as a publisher, it is essential that all possible Conflicts of Interest are avoided. Each contributor, whether an Author, Editor, or Reviewer, who suspects they may have a Conflict of Interest, is obliged to declare that concern in order to make the publisher and the readership aware of any potential influence on the work being undertaken.
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\\n\\nIntechOpen requires:
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\\n\\nAll Authors are obliged to declare every existing or potential Conflict of Interest, including financial or personal factors, as well as any relationship which could influence their scientific work. Authors must declare Conflicts of Interest at the time of manuscript submission, although they may exceptionally do so at any point during manuscript review. For jointly prepared manuscripts, the corresponding Author is obliged to declare potential Conflicts of Interest of any other Authors who have contributed to the manuscript.
\\n\\nCONFLICT OF INTEREST – ACADEMIC EDITOR
\\n\\nEditors can also have Conflicts of Interest. Editors are expected to maintain the highest standards of conduct, which are outlined in our Best Practice Guidelines (templates for Best Practice Guidelines). Among other obligations, it is essential that Editors make transparent declarations of any possible Conflicts of Interest that they might have.
\\n\\nAvoidance Measures for Academic Editors of Conflicts of Interest:
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\\n\\nIf a manuscript is submitted by an Author who is a member of an Academic Editor's family or is personally or professionally related to the Academic Editor in any way, either as a friend, colleague, student or mentor, the work will be handled by a different Academic Editor who is not in any way connected to the Author.
\\n\\nCONFLICT OF INTEREST - REVIEWER
\\n\\nAll Reviewers are required to declare possible Conflicts of Interest at the beginning of the evaluation process. If a Reviewer feels he or she might have any material, financial or any other conflict of interest with regards to the manuscript being reviewed, he or she is required to declare such concern and, if necessary, request exclusion from any further involvement in the evaluation process. A Reviewer's potential Conflicts of Interest are declared in the review report and presented to the Academic Editor, who then assesses whether or not the declared potential or actual Conflicts of Interest had, or could be perceived to have had, any significant impact on the review itself.
\\n\\nEXAMPLES OF CONFLICTS OF INTEREST:
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\\n\\nNON-FINANCIAL
\\n\\nAuthors are required to declare all potentially relevant non-financial, financial and material Conflicts of Interest that may have had an influence on their scientific work.
\\n\\nAcademic Editors and Reviewers are required to declare any non-financial, financial and material Conflicts of Interest that could influence their fair and balanced evaluation of manuscripts. If such conflict exists with regards to a submitted manuscript, Academic Editors and Reviewers should exclude themselves from handling it.
\\n\\nAll Authors, Academic Editors, and Reviewers are required to declare all possible financial and material Conflicts of Interest in the last five years, although it is advisable to declare less recent Conflicts of Interest as well.
\\n\\nEXAMPLES:
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\\n\\nAuthors should declare if they are board members of an organization that could benefit financially or materially from the publication of their work.
\\n\\nAcademic Editors should declare if they were coauthors or they have worked on the research project with the Author who has submitted a manuscript.
\\n\\nAcademic Editors should declare if the Author of a submitted manuscript is affiliated with the same department, faculty, institute, or company as they are.
\\n\\nPolicy last updated: 2016-06-09
\\n"}]'},components:[{type:"htmlEditorComponent",content:"In each instance of a possible Conflict of Interest, IntechOpen aims to disclose the situation in as transparent a way as possible in order to allow readers to judge whether a particular potential Conflict of Interest has influenced the Work of any individual Author, Editor, or Reviewer. IntechOpen takes all possible Conflicts of Interest into account during the review process and ensures maximum transparency in implementing its policies.
\n\nA Conflict of Interest is a situation in which a person's professional judgment may be influenced by a range of factors, including financial gain, material interest, or some other personal or professional interest. For IntechOpen as a publisher, it is essential that all possible Conflicts of Interest are avoided. Each contributor, whether an Author, Editor, or Reviewer, who suspects they may have a Conflict of Interest, is obliged to declare that concern in order to make the publisher and the readership aware of any potential influence on the work being undertaken.
\n\nA Conflict of Interest can be identified at different phases of the publishing process.
\n\nIntechOpen requires:
\n\nCONFLICT OF INTEREST - AUTHOR
\n\nAll Authors are obliged to declare every existing or potential Conflict of Interest, including financial or personal factors, as well as any relationship which could influence their scientific work. Authors must declare Conflicts of Interest at the time of manuscript submission, although they may exceptionally do so at any point during manuscript review. For jointly prepared manuscripts, the corresponding Author is obliged to declare potential Conflicts of Interest of any other Authors who have contributed to the manuscript.
\n\nCONFLICT OF INTEREST – ACADEMIC EDITOR
\n\nEditors can also have Conflicts of Interest. Editors are expected to maintain the highest standards of conduct, which are outlined in our Best Practice Guidelines (templates for Best Practice Guidelines). Among other obligations, it is essential that Editors make transparent declarations of any possible Conflicts of Interest that they might have.
\n\nAvoidance Measures for Academic Editors of Conflicts of Interest:
\n\nFor manuscripts submitted by the Academic Editor (or a scientific advisor), an appropriate person will be appointed to handle and evaluate the manuscript. The appointed handling Editor's identity will not be disclosed to the Author in order to maintain impartiality and anonymity of the review.
\n\nIf a manuscript is submitted by an Author who is a member of an Academic Editor's family or is personally or professionally related to the Academic Editor in any way, either as a friend, colleague, student or mentor, the work will be handled by a different Academic Editor who is not in any way connected to the Author.
\n\nCONFLICT OF INTEREST - REVIEWER
\n\nAll Reviewers are required to declare possible Conflicts of Interest at the beginning of the evaluation process. If a Reviewer feels he or she might have any material, financial or any other conflict of interest with regards to the manuscript being reviewed, he or she is required to declare such concern and, if necessary, request exclusion from any further involvement in the evaluation process. A Reviewer's potential Conflicts of Interest are declared in the review report and presented to the Academic Editor, who then assesses whether or not the declared potential or actual Conflicts of Interest had, or could be perceived to have had, any significant impact on the review itself.
\n\nEXAMPLES OF CONFLICTS OF INTEREST:
\n\nFINANCIAL AND MATERIAL
\n\nNON-FINANCIAL
\n\nAuthors are required to declare all potentially relevant non-financial, financial and material Conflicts of Interest that may have had an influence on their scientific work.
\n\nAcademic Editors and Reviewers are required to declare any non-financial, financial and material Conflicts of Interest that could influence their fair and balanced evaluation of manuscripts. If such conflict exists with regards to a submitted manuscript, Academic Editors and Reviewers should exclude themselves from handling it.
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\n\nEXAMPLES:
\n\nAuthors should declare if they were or they still are Academic Editors of the publications in which they wish to publish their work.
\n\nAuthors should declare if they are board members of an organization that could benefit financially or materially from the publication of their work.
\n\nAcademic Editors should declare if they were coauthors or they have worked on the research project with the Author who has submitted a manuscript.
\n\nAcademic Editors should declare if the Author of a submitted manuscript is affiliated with the same department, faculty, institute, or company as they are.
\n\nPolicy last updated: 2016-06-09
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