RGD Reference Report - Cysteine-proteinase-inhibiting function of T kininogen and of its proteolytic fragments. - Rat Genome Database

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Cysteine-proteinase-inhibiting function of T kininogen and of its proteolytic fragments.

Authors: Moreau, T  Esnard, F  Gutman, N  Degand, P  Gauthier, F 
Citation: Moreau T, etal., Eur J Biochem. 1988 Apr 5;173(1):185-90.
RGD ID: 1600550
Pubmed: PMID:3356189   (View Abstract at PubMed)

Previous attempts to liberate T kinin from T kininogen [Moreau et al. (1986) Eur. J. Biochem. 159, 341-346; Gutman et al. (1988) Eur. J. Biochem. 171, 577-582] have shown that complete fragmentation of the precursor molecule into inhibitory peptides was achieved before any vasoactive peptide was released, suggesting a possible physiological significance for this phenomenon. In this study, cysteine-proteinase-inhibiting properties of rat T kininogen and of its proteolytic fragments issuing from trypsin and submaxillary gland endopeptidase k hydrolysis, have been investigated using rat lysosomal cathepsins B, H and L, papain and bovine calpains I and II. All three lysosomal cathepsins were inhibited by T kininogen but tighter interactions were observed with cathepsin L and papain. Though higher Ki values were obtained for cathepsins B and H, rate constants for association were found to have high and almost similar values (in the 10(6) M-1 s-1 range) whatever the enzyme used. Proteolytic fragments also inhibited cathepsin L and papain very strongly and even better than the entire molecule for some of them, but no significant inhibition of cathepsins B and H was observed. Bovine calpains were not inhibited by T kininogen nor by its proteolytic fragments. From the results of this kinetic analysis, which indicates that both the association and the dissociation of lysosomal cysteine proteinases with T kininogen may occur rapidly, an hypothesis has been put forward on the possible in vivo functioning of T kininogen as a proteinase inhibitor.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
negative regulation of proteolysis  IDA 1600550 RGD 
regulation of endopeptidase activity  IDA 1600550 RGD 

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Ctsb  (cathepsin B)
Ctsh  (cathepsin H)
Ctsl  (cathepsin L)
Kng2  (kininogen 2)


Additional Information