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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 ...
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.
Acute-phase serum amyloid A proteins (A-SAAs) are secreted during the acute phase of inflammation.These proteins have several roles, including the transport of cholesterol to the liver for secretion into the bile, the recruitment of immune cells to inflammatory sites, and the induction of enzymes that degrade extracellular matrix.
According to the prevailing amyloid hypothesis of Alzheimer's disease, the aggregation of amyloid-beta (a peptide normally produced in and cleared from the healthy young brain) into extracellular plaques drives the neuronal loss and brain atrophy that is the hallmark of Alzheimer's dementia.
Amyloid beta is commonly thought to be intrinsically unstructured, meaning that in solution it does not acquire a unique tertiary fold but rather populates a set of structures. As such, it cannot be crystallized and most structural knowledge on amyloid beta comes from NMR and molecular dynamics.
However, several aspects of amyloid biology are still under investigation. For example, recent evidence has suggested that amyloid plaque formation is linked to brain microvascular trauma. [49] [50] Other research implicates chronic inflammation of the brain and immune dysfunction of the nervous system. [51] [52]
However, neuronal cell bodies contain less APP as a function of their proximity to amyloid plaques. [37] The data indicate that this deficit in APP results from a decline in production rather than an increase in catalysis. Loss of a neuron's APP may affect physiological deficits that contribute to dementia.