Author/Editor | Popovič, Tatjana; Cimerman, Nina; Dolenc, Iztok; Ritonja, Anka; Brzin, Jože | |
Title | Cathepsin L is capable of truncating cystatin C of 11 N-terminal amino acids | |
Type | članek | |
Source | FEBS Lett | |
Vol. and No. | Letnik 455 | |
Publication year | 1999 | |
Volume | str. 92-6 | |
Language | eng | |
Abstract | Abstract Cystatin C with the 11 N-terminal amino acids truncated shows a much lower affinity for cysteine proteinases than the intact inhibitor. Such truncation of cystatin C is recorded after action of glycyl endopeptidase and cathepsin L. Incubation of cystatin C with papain, cathepsin B or cathepsin H led to no changes in the cystatin C molecule. Isoelectric focusing of the cathepsin L and cystatin C mixture showed the formation of two new bands. One of them appeared whether E-64 or PMSF was added or not, evidently representing a cystatin C/cathepsin L complex. The other band is the truncated cystatin C molecule. N-terminal sequencing after separation by HPLC showed that cystatin C is cleaved by cathepsin L at the Gly11-GIy12 bond. The action of cathepsin L on cystatin C may be explained by the cleavage of the scissile bond in an inappropriate complex. | |
Descriptors | CATHEPSINS CYSTATINS CYSTEINE PROTEINASE INHIBITORS AMINO ACID SEQUENCE CHROMATOGRAPHY, HIGH PRESSURE LIQUID RECOMBINANT PROTEINS ELECTROPHORESIS, POLYACRYLAMIDE GEL ISOELECTRIC FOCUSING |