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As a result, amyloid deposits into the body's extracellular space. [5] The process of forming amyloid fibrils is thought to have intermediate oligomeric forms. Both the oligomers and amyloid fibrils can be toxic to cells and can interfere with proper organ function. [21]
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-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 .
AA amyloidosis is a form of amyloidosis, a disease characterized by the abnormal deposition of fibers of insoluble protein in the extracellular space of various tissues and organs. In AA amyloidosis, the deposited protein is serum amyloid A protein (SAA), an acute-phase protein which is normally soluble and whose plasma concentration is highest ...
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 ]
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]