title: Amyloidosis physiopathology.
abstract: Amyloidoses belong to the emerging group of conformational diseases. In the case of amyloid, the conformational change leads to pathologic deposition in tissues. Amyloid and amyloidosis are especially associated with inflammatory disorders and ageing. Twenty animal and human proteins with various primary structures are involved in amyloid deposits formation. Thermodynamic and kinetic aspects of the abnormal protein folding of amyloid proteins are better known. Several molecules of the extracellular matrix, especially amyloid P component and proteoglycans, are tightly linked to amyloid proteins within the deposits. However, their roles in amyloid deposits formation is not yet thoroughly established. Common treatments of amyloidoses are based on decreasing the availability of the amyloid protein precursor. Novel treatments will aim at blocking conformational changes of the amyloid protein and inhibiting amyloid protein-extracellular matrix interactions.
authors.affiliation: Service de médecine interne, Hôtel-Dieu, Paris, France.
authors.forename: G
authors.initials: G
authors.lastname: Grateau
mesh_terms: D000686:Amyloidosis / Q000235:genetics / Q000378:metabolism / Q000503:physiopathology*; D006801:Humans