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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]
The modern classification of amyloid disease tends to use an abbreviation of the protein that makes the majority of deposits, prefixed with the letter A. For example, amyloidosis caused by transthyretin is termed "ATTR". [medical citation needed] Deposition patterns vary between people but are almost always composed of just one amyloidogenic ...
Inclusion body myositis (IBM) (/ m aɪ oʊ ˈ s aɪ t ɪ s /) (sometimes called sporadic inclusion body myositis, sIBM) is the most common inflammatory muscle disease in older adults. [2] The disease is characterized by slowly progressive weakness and wasting of both proximal muscles (located on or close to the torso ) and distal muscles (close ...
Inclusion bodies have a non-unit (single) lipid membrane [citation needed].Protein inclusion bodies are classically thought to contain misfolded protein.However, this has been contested, as green fluorescent protein will sometimes fluoresce in inclusion bodies, which indicates some resemblance of the native structure and researchers have recovered folded protein from inclusion bodies.
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 .
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.
Inclusion body myopathy with early-onset Paget disease and frontotemporal dementia (IBMPFD), now more commonly referred to as multisystem proteinopathy (MSP), is an autosomal dominant condition caused by mutations in VCP, HNRPA2B1 or HNRNPA1; it is a multisystem degenerative disorder that can affect muscle, bone, and/or the central nervous system.
It is contrasted to systemic amyloidosis, and it can be caused by several different types of amyloid. [1] In almost all of the organ-specific pathologies, there is debate as to whether the amyloid plaques are the causal agent of the disease or instead a downstream consequence of a common idiopathic agent. The associated proteins are indicated ...