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FEBS Lett. 1991 Mar 25;280(2):211-5.

Inactivation of human cystatin C and kininogen by human cathepsin D.

Author information

1
Department of Biochemistry, Jozef Stefan Institute, Slovenia, Yugoslavia.

Abstract

A papain inhibitor of 22 kDa was isolated from human placenta and shown to be identical to residues Cys246-Leu373 of the third domain of human kininogen. This kininogen domain and recombinant human cystatin C were inactivated by peptide bond cleavages at hydrophobic amino acid residues due to the action of cathepsin D. These results further support the proposed role of cathepsin D in the regulation of cysteine proteinase activity.

PMID:
2013314
DOI:
10.1016/0014-5793(91)80295-e
[Indexed for MEDLINE]
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