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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]
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 ...
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 .
Amyloid, the aggregation, or clumping, of proteins, is resistant to degradation by the body. Amyloids are mostly fibrils, while also containing a P component, apolipoprotein, collagen, fibronectin, and laminin. [2] The P component, a pentameric protein, stabilizes the fibrils of the amyloid, which reduces their clearance from the body. [1]
Misfolded proteins can form protein aggregates or amyloid fibrils, get degraded, or refold back to its native structure.. In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly.
Amyloid-beta precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. It functions as a cell surface receptor [ 5 ] and has been implicated as a regulator of synapse formation , [ 6 ] neural plasticity , [ 7 ] antimicrobial activity, [ 8 ] and iron export . [ 9 ]
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.
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