Inactivation of human cystatin C and kininogen by human cathepsin D

B Lenarcic; M Krasovec; A Ritonja; I Olafsson; V Turk

doi:10.1016/0014-5793(91)80295-e

Inactivation of human cystatin C and kininogen by human cathepsin D

FEBS Lett. 1991 Mar 25;280(2):211-5. doi: 10.1016/0014-5793(91)80295-e.

Authors

B Lenarcic¹, M Krasovec, A Ritonja, I Olafsson, V Turk

Affiliation

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

PMID: 2013314
DOI: 10.1016/0014-5793(91)80295-e

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Cathepsin D / pharmacology*
Chromatography, High Pressure Liquid
Cystatin C
Cystatins / metabolism*
Cysteine Endopeptidases / metabolism
Enzyme Activation / drug effects
Humans
Kininogens / chemistry
Kininogens / metabolism*
Molecular Sequence Data
Placenta / enzymology
Protein Denaturation
Recombinant Proteins / metabolism

Substances

CST3 protein, human
Cystatin C
Cystatins
Kininogens
Recombinant Proteins
Cysteine Endopeptidases
Cathepsin D