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Expression and activity of beta-site amyloid precursor protein cleaving enzyme in Alzheimer's disease.
Johnston, J A; Liu, W W; Todd, S A; Coulson, D T R; Murphy, S; Irvine, G B; Passmore, A P.
Afiliación
  • Johnston JA; School of Biology and Biochemistry, The Queen's University of Belfast, Medical Biology Centre, Belfast BT9 7BL, Northern Ireland. j.a.johnston@qub.ac.uk
Biochem Soc Trans ; 33(Pt 5): 1096-100, 2005 Nov.
Article en En | MEDLINE | ID: mdl-16246054
Several lines of evidence indicate that the Abeta peptide is involved at some level in the pathological process that results in the clinical symptoms of AD (Alzheimer's disease). The N-terminus of Abeta is generated by cleavage of the Met-Asp bond at position 671-672 of APP (amyloid precursor protein), catalysed by a proteolytic activity called beta-secretase. Two 'beta-secretase' proteases have been identified: BACE (beta-site APP-cleaving enzyme) and BACE2. The cause of sporadic AD is currently unknown, but some studies have reported elevated BACE/beta-secretase activity in brain regions affected by the disease. We have demonstrated that robust beta-secretase activity is also detectable in platelets that contain APP and release Abeta. This review considers the current evidence for alterations in beta-secretase activity, and/or alterations in BACE expression, in post-mortem brain tissue and platelets from individuals with AD.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Endopeptidasas / Precursor de Proteína beta-Amiloide / Enfermedad de Alzheimer Límite: Humans Idioma: En Revista: Biochem Soc Trans Año: 2005 Tipo del documento: Article Pais de publicación: Reino Unido
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Endopeptidasas / Precursor de Proteína beta-Amiloide / Enfermedad de Alzheimer Límite: Humans Idioma: En Revista: Biochem Soc Trans Año: 2005 Tipo del documento: Article Pais de publicación: Reino Unido