| pubmed-article:9192758 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9192758 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:9192758 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:9192758 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:9192758 | lifeskim:mentions | umls-concept:C1415189 | lld:lifeskim |
| pubmed-article:9192758 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:9192758 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:9192758 | pubmed:dateCreated | 1997-7-10 | lld:pubmed |
| pubmed-article:9192758 | pubmed:abstractText | The glycoprotein (GP) Ib-IX-V complex contains a high-affinity binding site for thrombin on the platelet surface with a poorly defined role in platelet activation by this agonist. Four polypeptides comprise the complex: GP Ib alpha, GP Ib beta, GP IX, and GP V. The site within the complex that binds thrombin has been localized to a 45-kD region at the amino terminus of GP Ib alpha, which also contains the site through which the complex interacts with von Willebrand factor. A GP Ib-IX complex that lacks GP V can be efficiently expressed on the surface of transfected cells. We examined the ability of L cells expressing the GP Ib-IX complex (L2H cells) to bind thrombin at high affinity, and found no increase over the level of thrombin binding to control L cells. Because it is one of the few substrates for thrombin on the platelet surface, GP V has also been implicated as possibly participating in thrombin's actions on the platelet. To examine the role of GP V in forming the high-affinity thrombin-binding site, we compared the binding of thrombin to L2H cells versus cells that express the entire GP Ib-IX-V complex (L2H/V cells). Surface expression of GP Ib alpha was equivalent in these two stable cell lines. Thrombin binding to L2H/V cells was detectable at 0.25 nmol/L thrombin and reached a plateau at 1 nmol/L. No binding to L2H cells was detectable at these concentrations. Comparable results were obtained when thrombin binding to L2H cells transiently expressing GP V was compared with its binding to sham-transfected L2H cells. Again, only cells transiently expressing GP V bound thrombin specifically. As with the platelet polypeptide, thrombin cleaved GP V from the surface of L2H/V cells. To test whether GP V cleavage was required for enhancing thrombin binding to the complex, we tested the binding of enzymatically inactive D-phenylalanyl-L-prolyl-L-arginine chloromethylketone (PPACK)-thrombin to L2H and L2H/V cells. Like native thrombin, PPACK-thrombin at 1 nmol/L bound only to L2H/V cells, indicating that GP V cleavage is not a prerequisite for the formation of the high-affinity thrombin receptor. These data provide the first indication of a physiologic function for GP V, and suggest that formation of the high-affinity thrombin receptor on the platelet surface has complex allosteric requirements. | lld:pubmed |
| pubmed-article:9192758 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9192758 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9192758 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9192758 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9192758 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:9192758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9192758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9192758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9192758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9192758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9192758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9192758 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9192758 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9192758 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:9192758 | pubmed:author | pubmed-author:LópezJ AJA | lld:pubmed |
| pubmed-article:9192758 | pubmed:author | pubmed-author:DongJ FJF | lld:pubmed |
| pubmed-article:9192758 | pubmed:author | pubmed-author:Sae-TungGG | lld:pubmed |
| pubmed-article:9192758 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9192758 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9192758 | pubmed:volume | 89 | lld:pubmed |
| pubmed-article:9192758 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9192758 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9192758 | pubmed:pagination | 4355-63 | lld:pubmed |
| pubmed-article:9192758 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:meshHeading | pubmed-meshheading:9192758-... | lld:pubmed |
| pubmed-article:9192758 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9192758 | pubmed:articleTitle | Role of glycoprotein V in the formation of the platelet high-affinity thrombin-binding site. | lld:pubmed |
| pubmed-article:9192758 | pubmed:affiliation | Department of Internal Medicine, Baylor College of Medicine and Veterans Affairs Medical Center, Houston, TX 77030, USA. | lld:pubmed |
| pubmed-article:9192758 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9192758 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9192758 | lld:pubmed |
