Tags

Type your tag names separated by a space and hit enter

Expression and activity of beta-site amyloid precursor protein cleaving enzyme in Alzheimer's disease.
Biochem Soc Trans. 2005 Nov; 33(Pt 5):1096-100.BS

Abstract

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.

Authors+Show Affiliations

School of Biology and Biochemistry, The Queen's University of Belfast, Medical Biology Centre, Belfast BT9 7BL, Northern Ireland. j.a.johnston@qub.ac.ukNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

16246054

Citation

Johnston, J A., et al. "Expression and Activity of Beta-site Amyloid Precursor Protein Cleaving Enzyme in Alzheimer's Disease." Biochemical Society Transactions, vol. 33, no. Pt 5, 2005, pp. 1096-100.
Johnston JA, Liu WW, Todd SA, et al. Expression and activity of beta-site amyloid precursor protein cleaving enzyme in Alzheimer's disease. Biochem Soc Trans. 2005;33(Pt 5):1096-100.
Johnston, J. A., Liu, W. W., Todd, S. A., Coulson, D. T., Murphy, S., Irvine, G. B., & Passmore, A. P. (2005). Expression and activity of beta-site amyloid precursor protein cleaving enzyme in Alzheimer's disease. Biochemical Society Transactions, 33(Pt 5), 1096-100.
Johnston JA, et al. Expression and Activity of Beta-site Amyloid Precursor Protein Cleaving Enzyme in Alzheimer's Disease. Biochem Soc Trans. 2005;33(Pt 5):1096-100. PubMed PMID: 16246054.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Expression and activity of beta-site amyloid precursor protein cleaving enzyme in Alzheimer's disease. AU - Johnston,J A, AU - Liu,W W, AU - Todd,S A, AU - Coulson,D T R, AU - Murphy,S, AU - Irvine,G B, AU - Passmore,A P, PY - 2005/10/26/pubmed PY - 2006/5/4/medline PY - 2005/10/26/entrez SP - 1096 EP - 100 JF - Biochemical Society transactions JO - Biochem. Soc. Trans. VL - 33 IS - Pt 5 N2 - 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. SN - 0300-5127 UR - https://www.unboundmedicine.com/medline/citation/16246054/Expression_and_activity_of_beta_site_amyloid_precursor_protein_cleaving_enzyme_in_Alzheimer's_disease_ L2 - https://portlandpress.com/biochemsoctrans/article-lookup/doi/10.1042/BST20051096 DB - PRIME DP - Unbound Medicine ER -