| http://purl.uniprot.org/citations/18940719 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18940719 | http://www.w3.org/2000/01/rdf-schema#comment | "Phosphatidylserine (PS)-dependent erythrocyte adhesion to endothelium and subendothelial matrix components is mediated in part via thrombospondin (TSP). Although TSP exhibits multiple cell-binding domains, the PS-binding site on TSP is unknown. Because a cell-binding domain for anionic heparin is located at the amino-terminus, we hypothesized that PS-positive red blood cells (PS(+ve)-RBCs) bind to this domain. We demonstrate that both heparin and its low-molecular-weight derivative enoxaparin (0.5-50 u/mL) inhibited PS(+ve)-RBC adhesion to immobilized TSP in a concentration-dependent manner (21% to 77% inhibition, P < 0.05). Preincubation of immobilized TSP with an antibody against the heparin-binding domain blocked PS(+ve)-RBC adhesion to TSP. Antibodies that recognize the collagen- and the carboxy-terminal CD47-binding domain on TSP had no effect on this process. Although preincubation of PS(+ve)-RBCs with TSP peptides from the heparin-binding domain that contained the specific heparin-binding motif KKTRG inhibited PS(+ve)-erythrocyte adhesion to matrix TSP (P < 0.001), these peptides in the immobilized form supported PS-mediated erythrocyte adhesion. A TSP-peptide that lacks the binding motif neither inhibited nor supported PS(+ve)-RBC adhesion. Additional experiments show that soluble TSP also interacted with PS(+ve)-RBCs via its heparin-binding domain. Our results demonstrate that PS-positive erythrocytes bind to both immobilized and soluble TSP via its heparin-binding domain and that both heparin and enoxaparin, at clinically relevant concentrations, block this interaction. Other studies have shown that heparin inhibited P-selectin- and soluble-TSP-mediated sickle erythrocyte adhesion to endothelial cells. Our results, taken together with the previously documented findings, provide a rational basis for clinical use of heparin or its low-molecular-weight derivatives as therapeutic agents in treating vaso-occlusive pain in patients with sickle cell disease."xsd:string |
| http://purl.uniprot.org/citations/18940719 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.trsl.2008.07.007"xsd:string |
| http://purl.uniprot.org/citations/18940719 | http://purl.uniprot.org/core/author | "Gayen Betal S."xsd:string |
| http://purl.uniprot.org/citations/18940719 | http://purl.uniprot.org/core/author | "Setty B.N."xsd:string |
| http://purl.uniprot.org/citations/18940719 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18940719 | http://purl.uniprot.org/core/name | "Transl Res"xsd:string |
| http://purl.uniprot.org/citations/18940719 | http://purl.uniprot.org/core/pages | "165-177"xsd:string |
| http://purl.uniprot.org/citations/18940719 | http://purl.uniprot.org/core/title | "Phosphatidylserine-positive erythrocytes bind to immobilized and soluble thrombospondin-1 via its heparin-binding domain."xsd:string |
| http://purl.uniprot.org/citations/18940719 | http://purl.uniprot.org/core/volume | "152"xsd:string |
| http://purl.uniprot.org/citations/18940719 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18940719 |
| http://purl.uniprot.org/citations/18940719 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18940719 |
| http://purl.uniprot.org/uniprot/P07996#attribution-5E9C2DEB7D31CFCAAD0740970A14A035 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/18940719 |