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Glycoprotein IV-independent adhesion of sickle red blood cells to immobilized thrombospondin under flow conditions.
Blood. 1996 Jun 01; 87(11):4862-70.Blood

Abstract

The abnormal adherence of red blood cells (RBC to the blood vessel wall is believed to contribute to the vascular occlusion observed in patients with sickle call anemia. The cell adhesion receptors GPIV (CD36) and integrin alpha 4 beta 1 (CD49d/CD29) were previously identified on circulating sickle reticulocytes, and shown to mediate sickle RBC adhesion to the endothelium. The presence of damaged endothelium in these patients suggests that exposed extracellular matrix proteins could provide a potential substrate for sickle RBC adhesion. To determine whether RBC adhesion receptors could mediate adhesion to extracellular matrix proteins, we tested their ability to adhere to a variety of immobilized, purified proteins under flow conditions. Neither sickle nor normal RBC adhered to fibronectin, vitronectin, fibrinogen, or collagen. In contrast, we observed substantial adhesion of sickle but not normal RBC to thrombospondin (TSP). The adhesion was not inhibited with known antagonists of the GPIV-TSP interaction, nor by inhibitors of several other known binding domains in TSP. Moreover, the adhesion was resistant to inhibition by soluble TSP, suggesting that immobilization of TSP exposes an adhesive site that is cryptic on TSP in solution. However, the glycosaminoglycans, chondroitin sulfate A, and dextran sulfate were potent inhibitors of this adhesion. These results suggest that a mechanism distinct from GPIV is responsible for sickle RBC adhesion to immobilized TSP under flow conditions.

Authors+Show Affiliations

Department of Pharmacology, The University of North Carolina at Chapel Hill 27599-7365, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8639860

Citation

Joneckis, C C., et al. "Glycoprotein IV-independent Adhesion of Sickle Red Blood Cells to Immobilized Thrombospondin Under Flow Conditions." Blood, vol. 87, no. 11, 1996, pp. 4862-70.
Joneckis CC, Shock DD, Cunningham ML, et al. Glycoprotein IV-independent adhesion of sickle red blood cells to immobilized thrombospondin under flow conditions. Blood. 1996;87(11):4862-70.
Joneckis, C. C., Shock, D. D., Cunningham, M. L., Orringer, E. P., & Parise, L. V. (1996). Glycoprotein IV-independent adhesion of sickle red blood cells to immobilized thrombospondin under flow conditions. Blood, 87(11), 4862-70.
Joneckis CC, et al. Glycoprotein IV-independent Adhesion of Sickle Red Blood Cells to Immobilized Thrombospondin Under Flow Conditions. Blood. 1996 Jun 1;87(11):4862-70. PubMed PMID: 8639860.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Glycoprotein IV-independent adhesion of sickle red blood cells to immobilized thrombospondin under flow conditions. AU - Joneckis,C C, AU - Shock,D D, AU - Cunningham,M L, AU - Orringer,E P, AU - Parise,L V, PY - 1996/6/1/pubmed PY - 1996/6/1/medline PY - 1996/6/1/entrez SP - 4862 EP - 70 JF - Blood JO - Blood VL - 87 IS - 11 N2 - The abnormal adherence of red blood cells (RBC to the blood vessel wall is believed to contribute to the vascular occlusion observed in patients with sickle call anemia. The cell adhesion receptors GPIV (CD36) and integrin alpha 4 beta 1 (CD49d/CD29) were previously identified on circulating sickle reticulocytes, and shown to mediate sickle RBC adhesion to the endothelium. The presence of damaged endothelium in these patients suggests that exposed extracellular matrix proteins could provide a potential substrate for sickle RBC adhesion. To determine whether RBC adhesion receptors could mediate adhesion to extracellular matrix proteins, we tested their ability to adhere to a variety of immobilized, purified proteins under flow conditions. Neither sickle nor normal RBC adhered to fibronectin, vitronectin, fibrinogen, or collagen. In contrast, we observed substantial adhesion of sickle but not normal RBC to thrombospondin (TSP). The adhesion was not inhibited with known antagonists of the GPIV-TSP interaction, nor by inhibitors of several other known binding domains in TSP. Moreover, the adhesion was resistant to inhibition by soluble TSP, suggesting that immobilization of TSP exposes an adhesive site that is cryptic on TSP in solution. However, the glycosaminoglycans, chondroitin sulfate A, and dextran sulfate were potent inhibitors of this adhesion. These results suggest that a mechanism distinct from GPIV is responsible for sickle RBC adhesion to immobilized TSP under flow conditions. SN - 0006-4971 UR - https://www.unboundmedicine.com/medline/citation/8639860/Glycoprotein_IV_independent_adhesion_of_sickle_red_blood_cells_to_immobilized_thrombospondin_under_flow_conditions_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-4971(20)63650-3 DB - PRIME DP - Unbound Medicine ER -