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  2. Amyloid - Wikipedia

    en.wikipedia.org/wiki/Amyloid

    To date, 37 human proteins have been found to form amyloid in pathology and be associated with well-defined diseases. [2] The International Society of Amyloidosis classifies amyloid fibrils and their associated diseases based upon associated proteins (for example ATTR is the group of diseases and associated fibrils formed by TTR). [3]

  3. Amyloidosis - Wikipedia

    en.wikipedia.org/wiki/Amyloidosis

    Amyloid light chains deposition in shoulder joint causes enlarged shoulders, also known as "shoulder pad sign". [18] Amyloid light chain depositions can also cause bilateral symmetric polyarthritis. [18] The deposition of amyloid proteins in the bone marrow without causing plasma cell dyscrasias is called amyloidoma. It is commonly found in ...

  4. Serum amyloid A - Wikipedia

    en.wikipedia.org/wiki/Serum_amyloid_A

    Molecular weights of the human proteins are estimated at 11.7 kDa for SAA1 [5] and 14.8 kDa for SAA4. [6] Serum amyloid A (SAA) is also an acute phase marker that responds rapidly. Similar to CRP, levels of acute-phase SAA increase within hours after inflammatory stimulus, and the magnitude of increase may be greater than that of CRP ...

  5. Serum amyloid A1 - Wikipedia

    en.wikipedia.org/wiki/Serum_amyloid_A1

    Serum amyloid A1 (SAA1) is a protein that in humans is encoded by the SAA1 gene. [ 5 ] [ 6 ] [ 7 ] SAA1 is a major acute-phase protein mainly produced by hepatocytes in response to infection, tissue injury and malignancy. [ 8 ]

  6. AL amyloidosis - Wikipedia

    en.wikipedia.org/wiki/AL_amyloidosis

    Amyloid light-chain (AL) amyloidosis, also known as primary amyloidosis, is the most common form of systemic amyloidosis. [1] The disease is caused when a person's antibody -producing cells do not function properly and produce abnormal protein fibers made of components of antibodies called light chains .

  7. Amylin - Wikipedia

    en.wikipedia.org/wiki/Amylin

    A non-fibril forming peptide (1–19 residues of human amylin) is toxic like the full-length peptide but the respective segment of rat amylin is not. [17] [18] [19] It was also demonstrated by solid-state NMR spectroscopy that the fragment 20-29 of the human-amylin fragments membranes. [20]

  8. LECT2 amyloidosis - Wikipedia

    en.wikipedia.org/wiki/Lect2_amyloidosis

    LECT2 Amyloidosis (ALECT2) is a form of amyloidosis caused by the LECT2 protein. It was found to be the third most common (~3% of total) cause of amyloidosis in a set of more than 4,000 individuals studied at the Mayo Clinic; the first and second most common forms the disorder were AL amyloidosis and AA amyloidosis, respectively.

  9. AA amyloidosis - Wikipedia

    en.wikipedia.org/wiki/AA_amyloidosis

    There is evidence that eating amyloid fibers may lead to amyloidosis. This evidence is based on studies in cattle, chickens, mice, and cheetahs. [22] Thus, in a sense, SAA amyloidosis may be considered a contagious disease, although whether this occurs or is important in the development of naturally occurring amyloidosis remains unknown.