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PMID:1645961

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Citation

Tagawa, K, Kunishita, T, Maruyama, K, Yoshikawa, K, Kominami, E, Tsuchiya, T, Suzuki, K, Tabira, T, Sugita, H and Ishiura, S (1991) Alzheimer's disease amyloid beta-clipping enzyme (APP secretase): identification, purification, and characterization of the enzyme. Biochem. Biophys. Res. Commun. 177:377-87

Abstract

Alzheimer's disease (AD) is the most frequent cause of dementia, although no genetic abnormality has been identified. Recent studies have elucidated the molecular defect in AD, including the abnormal deposition of amyloid beta peptide (beta/A4) in senile plaques of affected individuals. Normal brain contains the enzyme, APP secretase, which cleaves inside the beta/A4 portion of the precursor protein (APP); abnormal processing of APP occurs in AD brain. Until now, no evidence has been provided that APP secretase is an intracellular proteinase. We have now prepared two synthetic substrates of APP secretase, both of which contain the cleavage point and are much more sensitive than substrates previously available to identify APP secretase. Using these substrates, we found an intracellular proteinase that has APP secretase activity. This proteinase has been identified as cathepsin B.

Links

PubMed

Keywords

Alzheimer Disease/enzymology; Amino Acid Sequence; Amyloid beta-Peptides/metabolism; Animals; Brain/enzymology; Cathepsin B/isolation & purification; Cathepsin B/metabolism; Chromatography/methods; Chromatography, Gel/methods; Chromatography, High Pressure Liquid/methods; Chromatography, Ion Exchange/methods; Durapatite; Humans; Hydroxyapatites; Kinetics; Liver/enzymology; Molecular Sequence Data; Peptide Mapping; Rats; Substrate Specificity

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:CATB

located_in

GO:0005622: intracellular anatomical structure

ECO:0000304: author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

HUMAN:CATB

enables

GO:0004197: cysteine-type endopeptidase activity

ECO:0000304: author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

HUMAN:CATB

part_of

GO:0005622: intracellular

ECO:0000304: author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete


See also

References

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