Integrin-associated protein is an adhesion receptor on sickle red blood cells for immobilized thrombospondin

Julia Elizabeth Brittain, Kathryn J. Mlinar, Christopher S. Anderson, Eugene P. Orringer, Leslie V. Parise

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

The adhesive protein thrombospondin (TSP) potentially mediates sickle (SS) red blood cell (RBC) adhesion to the blood vessel wall, thereby contributing to vaso-occlusive crises in sickle cell disease. We previously reported that SS RBCs bind to immobilized TSP under flow conditions, whereas normal (AA) red cells do not. However, the SS RBC receptors that mediate this interaction are largely unknown. Here it is reported that integrin-associated protein (IAP), or CD47, mediates the adhesion of these cells to immobilized TSP under both flow and static conditions. A peptide derived from the C-terminal lAP binding site of TSP also supports sickle cell adhesion; adhesion to this peptide or to TSP is inhibited specifically by the anti-IAP monoclonal antibody, 1F7. Furthermore, these data suggest that IAP on SS RBCs is structurally different from that expressed on AA RBCs but that IAP expression levels do not vary between AA and SS RBCs. This structural difference may contribute to the enhanced adhesion of SS RBCs to immobilized TSP. These results identify IAP as a TSP receptor on SS RBCs and suggest that this receptor and its binding site within TSP represent potential therapeutic targets to decrease vaso-occlusion.

Original languageEnglish (US)
Pages (from-to)2159-2164
Number of pages6
JournalBlood
Volume97
Issue number7
DOIs
StatePublished - Apr 1 2001

Fingerprint

Thrombospondins
Integrins
Blood
Erythrocytes
Cells
Cell Adhesion
Proteins
Adhesion
Cell adhesion
Binding Sites
CD36 Antigens
Immobilized Cells
Peptides
Blood vessels
Sickle Cell Anemia
adhesion receptor
Adhesives
Blood Vessels
Monoclonal Antibodies

ASJC Scopus subject areas

  • Biochemistry
  • Immunology
  • Hematology
  • Cell Biology

Cite this

Brittain, J. E., Mlinar, K. J., Anderson, C. S., Orringer, E. P., & Parise, L. V. (2001). Integrin-associated protein is an adhesion receptor on sickle red blood cells for immobilized thrombospondin. Blood, 97(7), 2159-2164. https://doi.org/10.1182/blood.V97.7.2159

Integrin-associated protein is an adhesion receptor on sickle red blood cells for immobilized thrombospondin. / Brittain, Julia Elizabeth; Mlinar, Kathryn J.; Anderson, Christopher S.; Orringer, Eugene P.; Parise, Leslie V.

In: Blood, Vol. 97, No. 7, 01.04.2001, p. 2159-2164.

Research output: Contribution to journalArticle

Brittain, JE, Mlinar, KJ, Anderson, CS, Orringer, EP & Parise, LV 2001, 'Integrin-associated protein is an adhesion receptor on sickle red blood cells for immobilized thrombospondin', Blood, vol. 97, no. 7, pp. 2159-2164. https://doi.org/10.1182/blood.V97.7.2159
Brittain, Julia Elizabeth ; Mlinar, Kathryn J. ; Anderson, Christopher S. ; Orringer, Eugene P. ; Parise, Leslie V. / Integrin-associated protein is an adhesion receptor on sickle red blood cells for immobilized thrombospondin. In: Blood. 2001 ; Vol. 97, No. 7. pp. 2159-2164.
@article{51b87786d207446980285895157c670e,
title = "Integrin-associated protein is an adhesion receptor on sickle red blood cells for immobilized thrombospondin",
abstract = "The adhesive protein thrombospondin (TSP) potentially mediates sickle (SS) red blood cell (RBC) adhesion to the blood vessel wall, thereby contributing to vaso-occlusive crises in sickle cell disease. We previously reported that SS RBCs bind to immobilized TSP under flow conditions, whereas normal (AA) red cells do not. However, the SS RBC receptors that mediate this interaction are largely unknown. Here it is reported that integrin-associated protein (IAP), or CD47, mediates the adhesion of these cells to immobilized TSP under both flow and static conditions. A peptide derived from the C-terminal lAP binding site of TSP also supports sickle cell adhesion; adhesion to this peptide or to TSP is inhibited specifically by the anti-IAP monoclonal antibody, 1F7. Furthermore, these data suggest that IAP on SS RBCs is structurally different from that expressed on AA RBCs but that IAP expression levels do not vary between AA and SS RBCs. This structural difference may contribute to the enhanced adhesion of SS RBCs to immobilized TSP. These results identify IAP as a TSP receptor on SS RBCs and suggest that this receptor and its binding site within TSP represent potential therapeutic targets to decrease vaso-occlusion.",
author = "Brittain, {Julia Elizabeth} and Mlinar, {Kathryn J.} and Anderson, {Christopher S.} and Orringer, {Eugene P.} and Parise, {Leslie V.}",
year = "2001",
month = "4",
day = "1",
doi = "10.1182/blood.V97.7.2159",
language = "English (US)",
volume = "97",
pages = "2159--2164",
journal = "Blood",
issn = "0006-4971",
publisher = "American Society of Hematology",
number = "7",

}

TY - JOUR

T1 - Integrin-associated protein is an adhesion receptor on sickle red blood cells for immobilized thrombospondin

AU - Brittain, Julia Elizabeth

AU - Mlinar, Kathryn J.

AU - Anderson, Christopher S.

AU - Orringer, Eugene P.

AU - Parise, Leslie V.

PY - 2001/4/1

Y1 - 2001/4/1

N2 - The adhesive protein thrombospondin (TSP) potentially mediates sickle (SS) red blood cell (RBC) adhesion to the blood vessel wall, thereby contributing to vaso-occlusive crises in sickle cell disease. We previously reported that SS RBCs bind to immobilized TSP under flow conditions, whereas normal (AA) red cells do not. However, the SS RBC receptors that mediate this interaction are largely unknown. Here it is reported that integrin-associated protein (IAP), or CD47, mediates the adhesion of these cells to immobilized TSP under both flow and static conditions. A peptide derived from the C-terminal lAP binding site of TSP also supports sickle cell adhesion; adhesion to this peptide or to TSP is inhibited specifically by the anti-IAP monoclonal antibody, 1F7. Furthermore, these data suggest that IAP on SS RBCs is structurally different from that expressed on AA RBCs but that IAP expression levels do not vary between AA and SS RBCs. This structural difference may contribute to the enhanced adhesion of SS RBCs to immobilized TSP. These results identify IAP as a TSP receptor on SS RBCs and suggest that this receptor and its binding site within TSP represent potential therapeutic targets to decrease vaso-occlusion.

AB - The adhesive protein thrombospondin (TSP) potentially mediates sickle (SS) red blood cell (RBC) adhesion to the blood vessel wall, thereby contributing to vaso-occlusive crises in sickle cell disease. We previously reported that SS RBCs bind to immobilized TSP under flow conditions, whereas normal (AA) red cells do not. However, the SS RBC receptors that mediate this interaction are largely unknown. Here it is reported that integrin-associated protein (IAP), or CD47, mediates the adhesion of these cells to immobilized TSP under both flow and static conditions. A peptide derived from the C-terminal lAP binding site of TSP also supports sickle cell adhesion; adhesion to this peptide or to TSP is inhibited specifically by the anti-IAP monoclonal antibody, 1F7. Furthermore, these data suggest that IAP on SS RBCs is structurally different from that expressed on AA RBCs but that IAP expression levels do not vary between AA and SS RBCs. This structural difference may contribute to the enhanced adhesion of SS RBCs to immobilized TSP. These results identify IAP as a TSP receptor on SS RBCs and suggest that this receptor and its binding site within TSP represent potential therapeutic targets to decrease vaso-occlusion.

UR - http://www.scopus.com/inward/record.url?scp=0035313429&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035313429&partnerID=8YFLogxK

U2 - 10.1182/blood.V97.7.2159

DO - 10.1182/blood.V97.7.2159

M3 - Article

C2 - 11264185

AN - SCOPUS:0035313429

VL - 97

SP - 2159

EP - 2164

JO - Blood

JF - Blood

SN - 0006-4971

IS - 7

ER -