| pubmed-article:1706335 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1706335 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:1706335 | lifeskim:mentions | umls-concept:C0134835 | lld:lifeskim |
| pubmed-article:1706335 | lifeskim:mentions | umls-concept:C0032594 | lld:lifeskim |
| pubmed-article:1706335 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:1706335 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:1706335 | pubmed:dateCreated | 1991-4-23 | lld:pubmed |
| pubmed-article:1706335 | pubmed:abstractText | GMP-140 is a 140-kDa granule membrane glycoprotein localized to the alpha-granules of platelets and the Weibel-Palade bodies of endothelial cells. Expression of GMP-140 on the activated cell surface has been shown to mediate the adhesion of thrombin-activated platelets to neutrophils and monocytes and the transient adhesion of neutrophils to endothelium. In contrast, fluid-phase GMP-140 strongly inhibits the CD18-dependent adhesion of tumor necrosis factor alpha-activated neutrophils to endothelium suggesting that GMP-140 can also serve an anti-adhesive function. In the present report, it is demonstrated that fluid-phase GMP-140 which exists predominantly as a tetramer binds to a single class of high affinity receptor on neutrophils and HL60 cells. Binding of 125I-labeled GMP-140 to neutrophils and HL60 cells and the rosetting of neutrophils and HL60 cells by thrombin-activated platelets were inhibited by EDTA, excess unlabeled fluid-phase GMP-140, Fab fragments of an affinity-purified rabbit anti-GMP-140 antibody, and by the murine anti-GMP-140 monoclonal antibody, AK 4. Both neutrophil and HL60 GMP-140 binding and platelet rosetting were strongly inhibited by heparin, fucoidin, and dextran sulfate 500,000, were partially inhibited by dextran sulfate 5,000 and lambda- and kappa-carrageenan, but were not inhibited by chondroitins 4- and 6-sulfate. Since this sulfated glycan specificity is identical to that previously reported by us for GMP-140, the present results suggest that the sulfated glycan binding site and the neutrophil receptor binding site on GMP-140 are either identical or proximal. | lld:pubmed |
| pubmed-article:1706335 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1706335 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1706335 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1706335 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1706335 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1706335 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1706335 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1706335 | pubmed:author | pubmed-author:ChestermanC... | lld:pubmed |
| pubmed-article:1706335 | pubmed:author | pubmed-author:BurnsG FGF | lld:pubmed |
| pubmed-article:1706335 | pubmed:author | pubmed-author:LucasC MCM | lld:pubmed |
| pubmed-article:1706335 | pubmed:author | pubmed-author:BerndtM CMC | lld:pubmed |
| pubmed-article:1706335 | pubmed:author | pubmed-author:SkinnerM PMP | lld:pubmed |
| pubmed-article:1706335 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1706335 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:1706335 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:1706335 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1706335 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1706335 | pubmed:pagination | 5371-4 | lld:pubmed |
| pubmed-article:1706335 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1706335 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1706335 | pubmed:articleTitle | GMP-140 binding to neutrophils is inhibited by sulfated glycans. | lld:pubmed |
| pubmed-article:1706335 | pubmed:affiliation | Department of Medicine, University of Sydney, Westmead Hospital, N.S.W., Australia. | lld:pubmed |
| pubmed-article:1706335 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1706335 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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