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Apolipoproteins and amyloid fibril formation in atherosclerosis.
Teoh, Chai Lean; Griffin, Michael D W; Howlett, Geoffrey J.
Afiliación
  • Teoh CL; Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Victoria 3010, Australia.
Protein Cell ; 2(2): 116-27, 2011 Feb.
Article en En | MEDLINE | ID: mdl-21400045
Amyloid fibrils arise from the aggregation of misfolded proteins into highly-ordered structures. The accumulation of these fibrils along with some non-fibrillar constituents within amyloid plaques is associated with the pathogenesis of several human degenerative diseases. A number of plasma apolipoproteins, including apolipoprotein (apo) A-I, apoA-II, apoC-II and apoE are implicated in amyloid formation or influence amyloid formation by other proteins. We review present knowledge of amyloid formation by apolipoproteins in disease, with particular focus on atherosclerosis. Further insights into the molecular mechanisms underlying their amyloidogenic propensity are obtained from in vitro studies which describe factors affecting apolipoprotein amyloid fibril formation and interactions. Additionally, we outline the evidence that amyloid fibril formation by apolipoproteins might play a role in the development and progression of atherosclerosis, and highlight possible molecular mechanisms that could contribute to the pathogenesis of this disease.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Apolipoproteínas / Aterosclerosis / Amiloide Límite: Humans Idioma: En Revista: Protein Cell Asunto de la revista: BIOQUIMICA Año: 2011 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Alemania

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Apolipoproteínas / Aterosclerosis / Amiloide Límite: Humans Idioma: En Revista: Protein Cell Asunto de la revista: BIOQUIMICA Año: 2011 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Alemania