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  • Title: Amyloidosis: a clinico-pathophysiological synopsis.
    Author: Hirschfield GM.
    Journal: Semin Cell Dev Biol; 2004 Feb; 15(1):39-44. PubMed ID: 15036205.
    Abstract:
    Amyloidosis encompasses a spectrum of diseases in which there is disordered folding of certain proteins that leads to them being deposited as insoluble fibrils in the extracellular space. The result of this process is impaired tissue structure and function. Amyloidosis may be acquired or hereditary and local or systemic, and is defined according to the identity of the fibril precursor protein. Over 20 unrelated proteins can form amyloid fibrils in vivo, which all share a lamellar cross-beta-sheet structure composed of non-covalently associated protein or peptide subunits. Glycosaminoglycans and the pentraxin protein, serum amyloid P component, are universal non-fibrillar constituents of amyloid deposits that are believed to play a role in fibrillogenesis and fibril persistence. Greater understanding of the processes underlying amyloidogenesis, at all levels from cellular to clinical, has led to improvements in diagnosis, monitoring and treatment of this group of diseases, as well as pointing to possible future therapies.
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