title: [Mechanisms of amyloidosis and the proteins involved].
abstract: BACKGROUND
  Recent data in amyloid research have shed light on the amyloid substance and have broadened our knowledge on the mechanism of amyloid deposition.
  
  
  BACKGROUND
  Despite uniform physical properties relating to the presence of beta-pleates, amyloid deposits are chemically heterogeneous and have different origins; additional types will probably be described in the future. Immunohistochemical techniques using specific antisera for each of the major protein present in fibrils could help greatly to subclassify these disorders. In most circumstances, a circulating precursor protein may result from overproduction of either intact or aberrant molecule, a reduction in its degradation or excretion, or genetic abnormalities associated with variant proteins. The cleavage of protein precursor molecules of the protein component of amyloid fibrils characterizes amyloidogenesis, though it is not necessary for some amyloidosis forms. This review summarizes advances in the understanding of the nature of amyloid substances, the mechanism of amyloid deposition and the principal pathogenic hypothesis.
  
  
  CONCLUSIONS
  SAP component is common in all amyloidosis and may be the target for future therapy.
authors.affiliation: Laboratoire de biochimie, faculté des sciences Ben M'sik, Casablanca, Maroc.
authors.forename: H
authors.initials: H
authors.lastname: Lebrazi
authors.forename: E
authors.initials: E
authors.lastname: Hachulla
authors.forename: R
authors.initials: R
authors.lastname: Saïle
mesh_terms: D016229:Amyloid beta-Peptides / Q000494:pharmacology*; D000686:Amyloidosis / Q000503:physiopathology*; D006801:Humans; D058225:Plaque, Amyloid; D000685:Serum Amyloid A Protein / Q000494:pharmacology*
chemical_list: D016229:Amyloid beta-Peptides; D000685:Serum Amyloid A Protein