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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1991-3-27
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pubmed:abstractText |
Leucocyte elastase in catalytic amounts was observed to rapidly cleave the Val-10-Gly-11 bond of the human cysteine-proteinase inhibitor cystatin C at neutral pH. The resulting modified inhibitor had size and amino acid composition consistent with a cystatin C molecule devoid of the N-terminal Ser-1-Val-10 decapeptide. Leucocyte-elastase-modified cystatin C had more than 240-fold lower affinity than native cystatin C for papain. Removal of the N-terminal decapeptide of human cystatin C also decreased inhibition of human cathepsins B and L by three orders of magnitude, but decreased inhibition of cathepsin H by only 5-fold. A tripeptidyldiazomethane analogue of of the N-terminal portion of cystatin C was a good inhibitor of cathepsins B and L but a poor inhibitor of cathepsin H. It therefore appears that amino acid side chains of the N-terminal segment of cystatin C bind in the substrate-binding pockets of cathepsins B and L but not in those of cathepsin H. It is argued that the N-terminal cystatin C interaction with cathepsin B is physiologically important and hence that leucocyte elastase could have a function as a regulator of extracellular cysteine-proteinase inhibitory activity at sites of inflammation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-1690669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-2237263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-2363674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-2400574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-2475916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-2476070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-2643059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-2845932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-2917648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-301739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3042461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-313856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3191914,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3202966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3488317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3490478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3491603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3495457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3496337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3517880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3753440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-3977867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-4123807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-50236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-5489841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-6165352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-6203523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-6283552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-6383897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-6388564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-6393977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-6437389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-6517881,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-6721883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-6915782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-7007374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-703988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-7043200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-7160384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1996959-730111
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
273 ( Pt 3)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
621-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1996959-Amino Acid Sequence,
pubmed-meshheading:1996959-Cystatin C,
pubmed-meshheading:1996959-Cystatins,
pubmed-meshheading:1996959-Electrophoresis, Agar Gel,
pubmed-meshheading:1996959-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1996959-Escherichia coli,
pubmed-meshheading:1996959-Humans,
pubmed-meshheading:1996959-Kinetics,
pubmed-meshheading:1996959-Leukocyte Elastase,
pubmed-meshheading:1996959-Molecular Sequence Data,
pubmed-meshheading:1996959-Molecular Weight,
pubmed-meshheading:1996959-Pancreatic Elastase,
pubmed-meshheading:1996959-Recombinant Proteins,
pubmed-meshheading:1996959-Substrate Specificity
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pubmed:year |
1991
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pubmed:articleTitle |
Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase.
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pubmed:affiliation |
Department of Clinical Chemistry, University of Lund, University Hospital, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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