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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1988-5-17
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin B,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Kininogens,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
173
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
185-90
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:3356189-Amino Acid Sequence,
pubmed-meshheading:3356189-Animals,
pubmed-meshheading:3356189-Cathepsin B,
pubmed-meshheading:3356189-Cysteine,
pubmed-meshheading:3356189-Hydrolysis,
pubmed-meshheading:3356189-Kinetics,
pubmed-meshheading:3356189-Kininogens,
pubmed-meshheading:3356189-Peptide Fragments,
pubmed-meshheading:3356189-Protease Inhibitors,
pubmed-meshheading:3356189-Rats,
pubmed-meshheading:3356189-Substrate Specificity
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pubmed:year |
1988
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pubmed:articleTitle |
Cysteine-proteinase-inhibiting function of T kininogen and of its proteolytic fragments.
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pubmed:affiliation |
Laboratoire de Biochimie, Faculté de Médecine, Université François Rabelais, Tours, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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