Inactivation of human cystatin C and kininogen by human cathepsin D
- 25 March 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 280 (2), 211-215
- https://doi.org/10.1016/0014-5793(91)80295-e
Abstract
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.Keywords
This publication has 26 references indexed in Scilit:
- Mechanism of inhibition of papain by chicken egg white cystatinFEBS Letters, 1989
- Efficient production of native, biologically active human cystatin C by Escherichia coliFEBS Letters, 1988
- Cathepsin D inactivates cysteine proteinase inhibitors cystatinsBiochemical and Biophysical Research Communications, 1988
- Identification of T-kinin-leu(T-kinin-containing peptide) released from T-kininogen by cathepsin D of granulomatous tissues in ratsBiochemical and Biophysical Research Communications, 1988
- Fucose-Containing Oligosaccharides from Human Milk from a Donor of Blood Group 0 LeaNonsecretorBiological Chemistry Hoppe-Seyler, 1988
- The pH dependence of breakdown of various purified brain proteins by cathepsin D preparationsNeurochemistry International, 1985
- Isolation and structure of T-kininBiochemical and Biophysical Research Communications, 1983
- Secretion and localization of cathepsin D in synovial tissues removed from rheumatoid and traumatized joints. An immunohistochemical studyArthritis & Rheumatism, 1976
- Hydrolysis of myelin basic protein with brain acid proteinaseBiochemical and Biophysical Research Communications, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970