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Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia.
Blood. 1993 Dec 15; 82(12):3548-55.Blood

Abstract

The abnormal adherence of red blood cells, especially circulating reticulocytes (erythrocyte precursors), to the endothelium is believed to contribute to vascular occlusion observed in patients with sickle cell disease. Although several plasma proteins including von Willebrand factor and fibronectin have been proposed to mediate this adhesion, the mechanism of sickle cell adhesion to the endothelium remains unknown. Using flow cytometry, we screened sickle red blood cells with monoclonal antibodies (MoAbs) against known adhesion receptors and detected integrin subunits alpha 4 and beta 1 and the nonintegrin glycoprotein IV on reticulocytes but not on erythrocytes. No reactivity was detected against integrin subunits alpha 2, alpha 3, alpha 5, alpha 6, alpha v, beta 2, beta 3, integrin alpha IIb beta 3, or the nonintegrin glycoprotein Ib. Immunoprecipitation of reticulocytes with either alpha 4- or beta 1-specific antibodies identified the alpha 4 beta 1 complex (alpha 4(70) and alpha 4(80) forms), a receptor for fibronectin and vascular cell adhesion molecule-1. An antibody against glycoprotein IV, a receptor reported to bind thrombospondin and collagen, immunoprecipitated an 88-kD protein consistent with its reported M(r). MoAbs against alpha 4 and glycoprotein IV bound to an average of 4,600 and 17,500 sites per reticulocyte, respectively. Identification of alpha 4 beta 1 and glycoprotein IV on reticulocytes suggests both plasma-dependent and independent mechanisms of reticulocyte adhesion to endothelium and exposed extracellular matrix.

Authors+Show Affiliations

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

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7505118

Citation

Joneckis, C C., et al. "Integrin Alpha 4 Beta 1 and Glycoprotein IV (CD36) Are Expressed On Circulating Reticulocytes in Sickle Cell Anemia." Blood, vol. 82, no. 12, 1993, pp. 3548-55.
Joneckis CC, Ackley RL, Orringer EP, et al. Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia. Blood. 1993;82(12):3548-55.
Joneckis, C. C., Ackley, R. L., Orringer, E. P., Wayner, E. A., & Parise, L. V. (1993). Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia. Blood, 82(12), 3548-55.
Joneckis CC, et al. Integrin Alpha 4 Beta 1 and Glycoprotein IV (CD36) Are Expressed On Circulating Reticulocytes in Sickle Cell Anemia. Blood. 1993 Dec 15;82(12):3548-55. PubMed PMID: 7505118.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia. AU - Joneckis,C C, AU - Ackley,R L, AU - Orringer,E P, AU - Wayner,E A, AU - Parise,L V, PY - 1993/12/15/pubmed PY - 1993/12/15/medline PY - 1993/12/15/entrez SP - 3548 EP - 55 JF - Blood JO - Blood VL - 82 IS - 12 N2 - The abnormal adherence of red blood cells, especially circulating reticulocytes (erythrocyte precursors), to the endothelium is believed to contribute to vascular occlusion observed in patients with sickle cell disease. Although several plasma proteins including von Willebrand factor and fibronectin have been proposed to mediate this adhesion, the mechanism of sickle cell adhesion to the endothelium remains unknown. Using flow cytometry, we screened sickle red blood cells with monoclonal antibodies (MoAbs) against known adhesion receptors and detected integrin subunits alpha 4 and beta 1 and the nonintegrin glycoprotein IV on reticulocytes but not on erythrocytes. No reactivity was detected against integrin subunits alpha 2, alpha 3, alpha 5, alpha 6, alpha v, beta 2, beta 3, integrin alpha IIb beta 3, or the nonintegrin glycoprotein Ib. Immunoprecipitation of reticulocytes with either alpha 4- or beta 1-specific antibodies identified the alpha 4 beta 1 complex (alpha 4(70) and alpha 4(80) forms), a receptor for fibronectin and vascular cell adhesion molecule-1. An antibody against glycoprotein IV, a receptor reported to bind thrombospondin and collagen, immunoprecipitated an 88-kD protein consistent with its reported M(r). MoAbs against alpha 4 and glycoprotein IV bound to an average of 4,600 and 17,500 sites per reticulocyte, respectively. Identification of alpha 4 beta 1 and glycoprotein IV on reticulocytes suggests both plasma-dependent and independent mechanisms of reticulocyte adhesion to endothelium and exposed extracellular matrix. SN - 0006-4971 UR - https://www.unboundmedicine.com/medline/citation/7505118/Integrin_alpha_4_beta_1_and_glycoprotein_IV__CD36__are_expressed_on_circulating_reticulocytes_in_sickle_cell_anemia_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-4971(20)66097-9 DB - PRIME DP - Unbound Medicine ER -