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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0005210,
umls-concept:C0005456,
umls-concept:C0009498,
umls-concept:C0015272,
umls-concept:C0019134,
umls-concept:C0033684,
umls-concept:C0055023,
umls-concept:C0205148,
umls-concept:C0205314,
umls-concept:C0205369,
umls-concept:C0242210,
umls-concept:C0679622,
umls-concept:C1622109,
umls-concept:C1704675
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pubmed:issue |
26
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pubmed:dateCreated |
1989-10-12
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pubmed:abstractText |
Human beta-endorphin (1-31) (beta H-endorphin) was found to specifically interact with purified complement S protein from human plasma. As found by chemical cross-linking beta H-endorphin bound to both, the 65- and 75-kDa molecular mass forms of S protein. The interaction of S protein with heparin as well as the adsorption of S protein to surfaces led to an almost 10-fold increase of specific binding which was due to the exposure of further beta H-endorphin-binding sites. The interaction of beta H-endorphin with S protein bore characteristics of a ligand-receptor interaction, such as time dependence, reversibility, high affinity, saturability, and structural specificity and was mediated through the non-opioid COOH terminus of the beta H-endorphin molecule. beta H-Endorphin binding to S protein was observed at physiological pH or cation concentrations, indicating that the interaction may well occur in vivo. Our results provide conclusive evidence that interactions of S protein with very different effectors led to similar conformational changes which uniformly resulted in exposure of a highly specific beta H-endorphin binding domain on S protein. With S protein as major beta H-endorphin-binding protein in the periphery, the molecular basis of a widespread system of humoral target sites of the neuroendocrine effector appears to be established. In view of S protein involvement in processes of inflammation and wound repair and beta-endorphin effects on immunocompetent cells, the demonstrated S protein-beta H-endorphin interaction appears to be of considerable functional significance.
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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/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosaminoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Succinimides,
http://linkedlifedata.com/resource/pubmed/chemical/Vitronectin,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Endorphin,
http://linkedlifedata.com/resource/pubmed/chemical/disuccinimidyl suberate
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
264
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15429-34
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2475499-Binding Sites,
pubmed-meshheading:2475499-Blood Proteins,
pubmed-meshheading:2475499-Cross-Linking Reagents,
pubmed-meshheading:2475499-Glycoproteins,
pubmed-meshheading:2475499-Glycosaminoglycans,
pubmed-meshheading:2475499-Heparin,
pubmed-meshheading:2475499-Humans,
pubmed-meshheading:2475499-Kinetics,
pubmed-meshheading:2475499-Molecular Weight,
pubmed-meshheading:2475499-Peptide Fragments,
pubmed-meshheading:2475499-Succinimides,
pubmed-meshheading:2475499-Vitronectin,
pubmed-meshheading:2475499-beta-Endorphin
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pubmed:year |
1989
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pubmed:articleTitle |
A novel beta-endorphin binding protein. Complement S protein (= vitronectin) exhibits specific non-opioid binding sites for beta-endorphin upon interaction with heparin or surfaces.
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pubmed:affiliation |
Rudolf-Buchheim-Institut für Pharmakologie, Max-Planck-Gesellschaft, Giessen, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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