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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 ...
Due to this resistance to degradation, when amyloid fibrils accumulate in the heart's walls, specifically the left ventricle, rigidity prevents the heart from properly relaxing and refilling with blood: this is called diastolic dysfunction which can ultimately lead to heart failure. [2]
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The transthyretin protein is a tetramer. The tetramer has to dissociate into misfolded monomers to aggregate into a variety of structures including amyloid fibrils. Because most patients are heterozygotes, they deposit both mutant and wild type TTR subnits. [citation needed] FAP is inherited in an autosomal dominant manner. [2]
Amyloid cardiomyopathy (stiff heart syndrome) [5] is a condition resulting in the death of part of the myocardium (heart muscle). It is associated with the systemic production and release of many amyloidogenic proteins , especially immunoglobulin light chain or transthyretin (TTR). [ 6 ]
Amyloid beta (Aβ, Abeta or beta-amyloid) denotes peptides of 36–43 amino acids that are the main component of the amyloid plaques found in the brains of people with Alzheimer's disease. [2] The peptides derive from the amyloid-beta precursor protein (APP), which is cleaved by beta secretase and gamma secretase to yield Aβ in a cholesterol ...
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 ]