Publication | Open Access
Rosetting of activated human T lymphocytes with autologous erythrocytes. Definition of the receptor and ligand molecules as CD2 and lymphocyte function-associated antigen 3 (LFA-3).
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Citations
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References
1987
Year
Ligand MoleculesLymphocyte DevelopmentCell AdhesionImmunologyImmune RegulationImmunologic MechanismAntigen ProcessingImmune SystemImmunotherapyHuman E. PretreatmentAutologous ErythrocytesHematologyLymphocyte BiologyT Cell AdhesionRadiation OncologyHealth SciencesImmune SurveillanceAutoimmunityT Cell ImmunityCell BiologyPurified Cd2Tumor MicroenvironmentT Cell BiologyActivated Human TCellular Immune ResponseMedicine
CD2, also known as LFA-2, T11, and the E rosette receptor, is a T lymphocyte surface protein functionally important in adhesion to target cells and T cell triggering. LFA-3 is a widely distributed cell surface protein that functions in adhesion on target cells. We find that LFA-3 is expressed on human E, and that CD2 is a receptor for LFA-3 that mediates T cell adhesion to human E. Pretreatment of T lymphocytes with CD2 mAb or of E with LFA-3 mAb inhibits rosetting. Purified CD2 molecules bind to human E and inhibit rosetting. 125I-CD2 binding to E is inhibited by LFA-3 mAb; reciprocally, binding of LFA-3 mAb to human E is inhibited by pretreatment with purified CD2. Higher concentrations of CD2 aggregate human E; aggregation is inhibited by mAb to LFA-3.
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