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Amyloid
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Amyloids are various types of insoluble fibrous protein aggregations sharing specific traits when examined microscopically. The name amyloid comes from the early mistaken identification of the substance as starch (amylum in Latin), based on crude iodine-staining techniques. For a period, the scientific community debated whether or not amyloid deposits were fatty deposits or carbohydrate deposits until it was finally resolved that it was neither, but rather a deposition of proteinaceous mass.
Amyloid deposits are extracellular, thioflavin-positive, and exhibit apple-green birefringence when stained with congo red when seen under a polarizing microscope. Other indicators exist, such as serum amyloid P component binding. Since these are indirect indicators, biophysicists have redefined amyloid using a canonical set of biophysical characteristics (see below), and this seems to cause a low level of conflict between histologists and biophysicists.
The phenotypes of genetically transmitted amyloid diseases are often inherited in an autosomal dominant fashion. Sometimes, the difference between aggressive amyloid diseases and senescent amyloid diseases is due to a mutation that makes the protein more prone to aggregation. Most commonly seen are point mutations, which affect the cohesiveness of the protein and promote misfolding; other mutations cause aggregation-prone pieces of the protein to be cleaved off from the rest of the protein.
Amyloids are present in some neurodegenerative diseases but play a normal productive role in processes such as melanin formation.[1
以上內容來自
the summary was check for reference of Dr Kim and Dr chen's homework as my noticed.
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Amyloids are various types of insoluble fibrous protein aggregations sharing specific traits when examined microscopically. The name amyloid comes from the early mistaken identification of the substance as starch (amylum in Latin), based on crude iodine-staining techniques. For a period, the scientific community debated whether or not amyloid deposits were fatty deposits or carbohydrate deposits until it was finally resolved that it was neither, but rather a deposition of proteinaceous mass.
Amyloid deposits are extracellular, thioflavin-positive, and exhibit apple-green birefringence when stained with congo red when seen under a polarizing microscope. Other indicators exist, such as serum amyloid P component binding. Since these are indirect indicators, biophysicists have redefined amyloid using a canonical set of biophysical characteristics (see below), and this seems to cause a low level of conflict between histologists and biophysicists.
The phenotypes of genetically transmitted amyloid diseases are often inherited in an autosomal dominant fashion. Sometimes, the difference between aggressive amyloid diseases and senescent amyloid diseases is due to a mutation that makes the protein more prone to aggregation. Most commonly seen are point mutations, which affect the cohesiveness of the protein and promote misfolding; other mutations cause aggregation-prone pieces of the protein to be cleaved off from the rest of the protein.
Amyloids are present in some neurodegenerative diseases but play a normal productive role in processes such as melanin formation.[1
以上內容來自
the summary was check for reference of Dr Kim and Dr chen's homework as my noticed.
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