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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1988-3-7
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pubmed:abstractText |
C4b-binding protein, C4bp, is a regulatory factor of the complement system and is also known to be a binding protein of vitamin K-dependent coagulation factor, protein S. Whereas the C4b-binding site is known to be located in the middle part of the subunit chains of C4bp, the location and properties of protein S-binding site are uncertain. Therefore, we have examined the characteristics of the interaction between human protein S and C4bp. Proteolysis of C4bp-protein S complex with chymotrypsin yielded N-terminal-derived 48-kDa fragments of C4bp subunit chains and a C-terminal-derived 160-kDa core fragment of C4bp, to which protein S was still bound. This result suggested that the protein S-binding site is located in the core domain of C4bp. Gel filtration of guanidine-treated C4bp-protein S complex in the absence of guanidine resulted in the separation of C4bp and protein S. Binding assay with 125I-labeled protein S showed that the guanidine-treated C4bp lacked the protein S-binding activity. This result suggests that the protein S-binding site in C4bp is denatured irreversibly by guanidine treatment and therefore seems to be dependent on a specific conformation of C4bp. The C4bp-binding site of protein S was lost upon thrombin treatment, suggesting that the N-terminal thrombin-sensitive region of protein S may be related to the C4bp-binding site. Although free protein S was susceptible to chymotrypsin, leukocyte elastase, and cathepsin G, C4bp-bound protein S was found to be resistant to these proteases.(ABSTRACT TRUNCATED AT 250 WORDS)
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Complement Inactivator Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanidines,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein S,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
102
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
599-605
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:2962995-Carrier Proteins,
pubmed-meshheading:2962995-Chromatography, Gel,
pubmed-meshheading:2962995-Complement Inactivator Proteins,
pubmed-meshheading:2962995-Glycoproteins,
pubmed-meshheading:2962995-Guanidines,
pubmed-meshheading:2962995-Humans,
pubmed-meshheading:2962995-Hydrolysis,
pubmed-meshheading:2962995-Immunodiffusion,
pubmed-meshheading:2962995-Iodine Radioisotopes,
pubmed-meshheading:2962995-Peptide Hydrolases,
pubmed-meshheading:2962995-Protein S,
pubmed-meshheading:2962995-Thrombin
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pubmed:year |
1987
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pubmed:articleTitle |
Characterization of the interaction between human protein S and C4b-binding protein (C4bp).
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pubmed:affiliation |
Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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