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Systemic amyloid fibril main peptide chains [extracellular region]
Stable Identifier
R-HSA-976760
Type
Set [DefinedSet]
Species
Homo sapiens
Compartment
extracellular region
Locations in the PathwayBrowser
Expand all
Metabolism of proteins (Homo sapiens)
Amyloid fiber formation (Homo sapiens)
Amyloid fibrils have additional components (Homo sapiens)
Amyloid fibril main peptide chains [extracellular region] (Homo sapiens)
Systemic amyloid fibril main peptide chains [extracellular region] (Homo sapiens)
Amyloid fibrils [plasma membrane] (Homo sapiens)
Amyloid fibril main peptide chains [extracellular region] (Homo sapiens)
Systemic amyloid fibril main peptide chains [extracellular region] (Homo sapiens)
Amyloid precursor proteins form ordered fibrils (Homo sapiens)
Amyloid fibril main peptide chains [extracellular region] (Homo sapiens)
Systemic amyloid fibril main peptide chains [extracellular region] (Homo sapiens)
General
Amyloid is a term used to describe deposits of fibrillar proteins, typically extracellular. The abnormal accumulation of amyloid, amyloidosis, is a term associated with tissue damage caused by amyloid deposition, seen in numerous diseases including neurodegenerative diseases such as Alzheimer's, Parkinson's and Huntington's. Amyloid deposits consist predominantly of amyloid fibrils, rigid, non-branching structures that form ordered assemblies, characteristically with a cross beta-sheet structure where the sheets run parallel to the direction of the fibril (Sawaya et al. 2007). Often the fibril has a left-handed twist (Nelson & Eisenberg 2006). At least 27 human proteins form amyloid fibrils (Sipe et al. 2010). Many of these proteins have non-pathological functions; the trigger that leads to abnormal aggregations differs between proteins and is not well understood but in many cases the peptides are abnormal fragments or mutant forms arising from polymorphisms, suggesting that the initial event may be aggregation of misfolded or unfolded peptides. Early studies of Amyloid-beta assembly led to a widely accepted model that assembly was a nucleation-dependent polymerization reaction (Teplow 1998) but it is now understood to be more complex, with multiple 'off-pathway' events leading to a variety of oligomeric structures in addition to fibrils (Roychaudhuri et al. 2008), though it is unclear whether these intermediate steps are required in vivo. An increasing body of evidence suggests that these oligomeric forms are primarily responsible for the neurotoxic effects of Amyloid-beta (Roychaudhuri et al. 2008), alpha-synuclein (Winner et al. 2011) and tau (Dance & Strobel 2009, Meraz-Rios et al. 2010). Amyloid oligomers are believed to have a common structural motif that is independent of the protein involved and not present in fibrils (Kayed et al. 2003). Conformation dependent, aggregation specific antibodies suggest that there are 3 general classes of amyloid oligomer structures (Glabe 2009) including annular structures which may be responsible for the widely reported membrane permeabilization effect of amyloid oligomers. Toxicity of amyloid oligomers preceeds the appearance of plaques in mouse models (Ferretti et al. 2011).
Fibrils are often associated with other molecules, notably heparan sulfate proteoglycans and Serum Amyloid P-component, which are universally associated and seem to stabilize fibrils, possibly by protecting them from degradation.
Literature References
PubMed ID
Title
Journal
Year
16302959
Aspects on human amyloid forms and their fibril polypeptides
Westermark, P
FEBS J
2005
Participants
members
Amyloid protein A fibril [extracellular region]
(Homo sapiens)
Apolipoprotein A-IV fibril [extracellular region]
(Homo sapiens)
Beta2-microglobulin fibril [extracellular region]
(Homo sapiens)
Transthyretin fibril [extracellular region]
(Homo sapiens)
Variant apolipoprotein AI fibril [extracellular region]
(Homo sapiens)
Variant apolipoprotein AII fibril [extracellular region]
(Homo sapiens)
Gelsolin amyloid fibril [extracellular region]
(Homo sapiens)
Variant lysozyme C fibril [extracellular region]
(Homo sapiens)
Variant fibrinogen alpha chain fibril [extracellular region]
(Homo sapiens)
Variant cystatin-C fibril [extracellular region]
(Homo sapiens)
ABri/ADan amyloid fibril [extracellular region]
(Homo sapiens)
Participates
as a member of
Amyloid fibril main peptide chains [extracellular region] (Homo sapiens)
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