Abstract:
:Amyloid beta peptide (Abeta) is a physiological peptide that is constantly catabolized in the brain. We previously demonstrated that an endopeptidase sensitive to phosphoramidon and thiorphan conducts the initial rate-limiting proteolysis of Abeta in vivo, but the exact molecular identity of the peptidase(s) has remained unknown because of the molecular redundancy of such activity. We analyzed the brain-derived enzyme by means of immuno-depletion and gene disruption, and demonstrate here that neprilysin accounts for the majority of the Abeta-degrading activity. Furthermore, kinetic analysis, giving a K(m) value of 2.8 +/- 0.76 microM, indicated that Abeta(1-42) is a relevant substrate for neprilysin.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Takaki Y,Iwata N,Tsubuki S,Taniguchi S,Toyoshima S,Lu B,Gerard NP,Gerard C,Lee HJ,Shirotani K,Saido TCdoi
10.1093/oxfordjournals.jbchem.a022839keywords:
subject
Has Abstractpub_date
2000-12-01 00:00:00pages
897-902issue
6eissn
0021-924Xissn
1756-2651journal_volume
128pub_type
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