Platelet-erythrocyte adhesion in sickle cell disease

Theodore Wun, Teresa Paglieroni, Cara L. Field, Jeanna L Welborn, Anthony Cheunt, Naomi J. Walker, Fern Tablin

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Background: The abnormal adherence of sickle red blood cells (sRBC) to other cell types likely contributes to vasoocclusion. Increased numbers of platelet-erythrocyte aggregates (PEA) and platelet activation have been described in sickle cell disease. The present study was undertaken to determine the contribution, if any, of the extracellular matrix protein thrombospondin to the adhesion of sRBC and platelets. Methods: Platelet activation and PEA were measured using fluoresecent-labeled monoclonal antibodies and flow cytometry. Platelet red-cell adhesion was measured by a gravity sedimentation assay. Erythrocyte-bound thrombospondin (TSP) was determined by enzyme-linked immunoabsorbant assay (ELISA). Results: Our studies demonstrate significant platelet activation and adhesion of sRBC to platelets in sickle cell disease. Thrombospondin was detected on sRBC. There was variable inhibition of sRBC-platelet adhesion by antibodies to CD36 (thrombospondin receptor) and antibodies to thrombospondin. Conclusions: Thrombospondin on sRBC may mediate, at least in part, sRBC-platelet adhesion in sickle cell disease. The study of heterotypic cell-cell interactions is important in understanding the pathogenesis of vaso-occlusion in sickle cell disease.

Original languageEnglish (US)
Pages (from-to)121-127
Number of pages7
JournalJournal of Investigative Medicine
Volume47
Issue number3
StatePublished - Mar 1999

Fingerprint

Sickle Cell Anemia
Platelets
Blood Platelets
Adhesion
Erythrocytes
Thrombospondins
Blood
Platelet Activation
Cell Adhesion
Cells
Chemical activation
Assays
CD36 Antigens
Erythrocyte Count
Antibodies
Extracellular Matrix Proteins
Gravitation
Flow cytometry
Cell adhesion
Platelet Count

Keywords

  • CD 36
  • Platelet-erythrocyte aggregates
  • Platelets
  • Sickle cell disease
  • Thrombospondin

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Wun, T., Paglieroni, T., Field, C. L., Welborn, J. L., Cheunt, A., Walker, N. J., & Tablin, F. (1999). Platelet-erythrocyte adhesion in sickle cell disease. Journal of Investigative Medicine, 47(3), 121-127.

Platelet-erythrocyte adhesion in sickle cell disease. / Wun, Theodore; Paglieroni, Teresa; Field, Cara L.; Welborn, Jeanna L; Cheunt, Anthony; Walker, Naomi J.; Tablin, Fern.

In: Journal of Investigative Medicine, Vol. 47, No. 3, 03.1999, p. 121-127.

Research output: Contribution to journalArticle

Wun, T, Paglieroni, T, Field, CL, Welborn, JL, Cheunt, A, Walker, NJ & Tablin, F 1999, 'Platelet-erythrocyte adhesion in sickle cell disease', Journal of Investigative Medicine, vol. 47, no. 3, pp. 121-127.
Wun T, Paglieroni T, Field CL, Welborn JL, Cheunt A, Walker NJ et al. Platelet-erythrocyte adhesion in sickle cell disease. Journal of Investigative Medicine. 1999 Mar;47(3):121-127.
Wun, Theodore ; Paglieroni, Teresa ; Field, Cara L. ; Welborn, Jeanna L ; Cheunt, Anthony ; Walker, Naomi J. ; Tablin, Fern. / Platelet-erythrocyte adhesion in sickle cell disease. In: Journal of Investigative Medicine. 1999 ; Vol. 47, No. 3. pp. 121-127.
@article{677845c629a946688028819f865e24c5,
title = "Platelet-erythrocyte adhesion in sickle cell disease",
abstract = "Background: The abnormal adherence of sickle red blood cells (sRBC) to other cell types likely contributes to vasoocclusion. Increased numbers of platelet-erythrocyte aggregates (PEA) and platelet activation have been described in sickle cell disease. The present study was undertaken to determine the contribution, if any, of the extracellular matrix protein thrombospondin to the adhesion of sRBC and platelets. Methods: Platelet activation and PEA were measured using fluoresecent-labeled monoclonal antibodies and flow cytometry. Platelet red-cell adhesion was measured by a gravity sedimentation assay. Erythrocyte-bound thrombospondin (TSP) was determined by enzyme-linked immunoabsorbant assay (ELISA). Results: Our studies demonstrate significant platelet activation and adhesion of sRBC to platelets in sickle cell disease. Thrombospondin was detected on sRBC. There was variable inhibition of sRBC-platelet adhesion by antibodies to CD36 (thrombospondin receptor) and antibodies to thrombospondin. Conclusions: Thrombospondin on sRBC may mediate, at least in part, sRBC-platelet adhesion in sickle cell disease. The study of heterotypic cell-cell interactions is important in understanding the pathogenesis of vaso-occlusion in sickle cell disease.",
keywords = "CD 36, Platelet-erythrocyte aggregates, Platelets, Sickle cell disease, Thrombospondin",
author = "Theodore Wun and Teresa Paglieroni and Field, {Cara L.} and Welborn, {Jeanna L} and Anthony Cheunt and Walker, {Naomi J.} and Fern Tablin",
year = "1999",
month = "3",
language = "English (US)",
volume = "47",
pages = "121--127",
journal = "Journal of Investigative Medicine",
issn = "1081-5589",
publisher = "Lippincott Williams and Wilkins",
number = "3",

}

TY - JOUR

T1 - Platelet-erythrocyte adhesion in sickle cell disease

AU - Wun, Theodore

AU - Paglieroni, Teresa

AU - Field, Cara L.

AU - Welborn, Jeanna L

AU - Cheunt, Anthony

AU - Walker, Naomi J.

AU - Tablin, Fern

PY - 1999/3

Y1 - 1999/3

N2 - Background: The abnormal adherence of sickle red blood cells (sRBC) to other cell types likely contributes to vasoocclusion. Increased numbers of platelet-erythrocyte aggregates (PEA) and platelet activation have been described in sickle cell disease. The present study was undertaken to determine the contribution, if any, of the extracellular matrix protein thrombospondin to the adhesion of sRBC and platelets. Methods: Platelet activation and PEA were measured using fluoresecent-labeled monoclonal antibodies and flow cytometry. Platelet red-cell adhesion was measured by a gravity sedimentation assay. Erythrocyte-bound thrombospondin (TSP) was determined by enzyme-linked immunoabsorbant assay (ELISA). Results: Our studies demonstrate significant platelet activation and adhesion of sRBC to platelets in sickle cell disease. Thrombospondin was detected on sRBC. There was variable inhibition of sRBC-platelet adhesion by antibodies to CD36 (thrombospondin receptor) and antibodies to thrombospondin. Conclusions: Thrombospondin on sRBC may mediate, at least in part, sRBC-platelet adhesion in sickle cell disease. The study of heterotypic cell-cell interactions is important in understanding the pathogenesis of vaso-occlusion in sickle cell disease.

AB - Background: The abnormal adherence of sickle red blood cells (sRBC) to other cell types likely contributes to vasoocclusion. Increased numbers of platelet-erythrocyte aggregates (PEA) and platelet activation have been described in sickle cell disease. The present study was undertaken to determine the contribution, if any, of the extracellular matrix protein thrombospondin to the adhesion of sRBC and platelets. Methods: Platelet activation and PEA were measured using fluoresecent-labeled monoclonal antibodies and flow cytometry. Platelet red-cell adhesion was measured by a gravity sedimentation assay. Erythrocyte-bound thrombospondin (TSP) was determined by enzyme-linked immunoabsorbant assay (ELISA). Results: Our studies demonstrate significant platelet activation and adhesion of sRBC to platelets in sickle cell disease. Thrombospondin was detected on sRBC. There was variable inhibition of sRBC-platelet adhesion by antibodies to CD36 (thrombospondin receptor) and antibodies to thrombospondin. Conclusions: Thrombospondin on sRBC may mediate, at least in part, sRBC-platelet adhesion in sickle cell disease. The study of heterotypic cell-cell interactions is important in understanding the pathogenesis of vaso-occlusion in sickle cell disease.

KW - CD 36

KW - Platelet-erythrocyte aggregates

KW - Platelets

KW - Sickle cell disease

KW - Thrombospondin

UR - http://www.scopus.com/inward/record.url?scp=0033093026&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033093026&partnerID=8YFLogxK

M3 - Article

VL - 47

SP - 121

EP - 127

JO - Journal of Investigative Medicine

JF - Journal of Investigative Medicine

SN - 1081-5589

IS - 3

ER -