Amyloids are aggregations of misfolded protein, which creates fibrillary structures. Unlike normally folded proteins, misfolded fibrils are insoluble and deposited extracellularly or intracellularly. The pathologic mechanism is still unclear, but resultant toxic oligomers within the tissue are known to damage the tissue via aberrant protein interactions. This condition has been known as amyloidosis. Different kinds of amyloid protein may cause similar or different clinical signs and symptoms, largely depending on the target organ it is deposited. However, because treatments and prognoses of each type are different drastically, it is critical to distinguish them and determine the specific type of amyloidosis. The confirmation and typing of amyloid heavily depend on pathologic examination of tissue. The gold standard method for the former is a Congo red staining and birefringence under polarized microscopy. The conventional way for the latter is immunohistochemistry (IHC), where most of the amyloid types can be classified. However, electron microscopy, mass spectrometry, or other molecular methods are required for typing some amyloids that are difficult to identify through IHC. In this chapter, we will describe basic concepts of amyloidosis and pathologic findings of amyloid deposition, including atypical structural deposition. Furthermore, we will review methodologies for amyloid typing briefly.
Part of the book: Amyloid Diseases