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Cathepsin D inactivates cysteine proteinase inhibitors, cystatins.

Abstract：

:The formation of inactive complexes in excess molar amounts of human cathepsins H and L with their protein inhibitors human stefin A, human stefin B and chicken cystatin at pH 5.6 has been shown by measurement of enzyme activity coupled with reverse-phase HPLC not to involve covalent cleavage of the inhibitors. Inhibition must be the direct result of binding. On the contrary the interaction of cystatins with aspartic proteinase cathepsin D at pH 3.5 for 60 min followed by HPLC resulted in their inactivation accompanied by peptide bond cleavage at several sites, preferentially those involving hydrophobic amino acid residues. The released peptides do not inhibit papain and cathepsin L. These results explain reported elevated levels of cysteine proteinases and lead to the proposal that cathepsin D exerts an important function, through inactivation of cystatins, in the increased activities of cysteine proteinases in human diseases including muscular distrophy.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lenarcic B,Kos J,Dolenc I,Lucovnik P,Krizaj I,Turk V

doi

10.1016/0006-291x(88)90206-9

subject

Has Abstract

pub_date

1988-07-29 00:00:00

pages

765-72

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(88)90206-9

journal_volume

154

pub_type

杂志文章

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