Abstract:
:The cerebral deposition of 40-42 residue amyloid beta-protein (Abeta) is a characteristic of Alzheimer's disease. Cathepsin D is possibly involved in the intracellular clearance of Abeta (Hamazaki, H. (1996) FEBS Lett., in press). The present work shows that cathepsin D hydrolyzes wild-type Abeta 20 times faster than a variant Abeta with a substitution at residue 21 from Ala to Gly. Since the substitution has been linked to familial Alzheimer's disease and hereditary cerebral hemorrhage with amyloidosis (Hendriks et al. (1992) Nature Genet. 1, 218-221), the present observations suggest that the inefficient elimination of Abeta by cathepsin D is capable of being one of causes of the amyloid fibril formation.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hamazaki Hdoi
10.1016/s0014-5793(96)01202-1subject
Has Abstractpub_date
1996-11-18 00:00:00pages
313-5issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(96)01202-1journal_volume
397pub_type
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