Inactivation of human cystatin C and kininogen by human cathepsin D

FEBS Letters

Lenarčič, Brigita¹  Olafsson, Isleifur²  Krašovec, Marta¹  Ritonja, Anka¹  Turk, Vito¹ 

[1] Department of Biochemistry, Jožef Stefan Institute, Jamova 39, 61000 Ljubljana, Slovenia, Yugoslavia;Department of Clinical Chemistry, University of Lund, University Hospital, S-221 85 Lund, Sweden

关键词: Cystatin C;    Kininogen;    Cathepsin D;    Proteinase inhibitor inactivation;   

DOI  :  10.1016/0014-5793(91)80295-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A papain inhibitor or 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 cathepsin D in the regulation of cysteine proteinase activity.

【 授权许可】

Unknown