Activation of human T lymphocytes via the CD2 antigen results in tyrosine phosphorylation of T cell antigen receptor ζ-chains

Eva Monostori, Dev Desai, Marion H. Brown, Doreen A. Cantrell, Michael J. Crumpton

Research output: Contribution to journalArticlepeer-review

83 Scopus citations

Abstract

The phosphorylation of the invariant chains associated with the human TCR has been investigated after the stimulation of T lymphocytes with CD2 mAb T112 and T113, PHA, or phorbol 12,13-dibutyrate. As described previously, stimulation of T cells with either CD2 mAb or phorbol 12,13-dibutyrate resulted in the phosphorylation of the CD3 γ-chain. The combination of T112 and T113 mAb also induced phosphorylation of the TCR ζ-chain. The phosphorylated ζ-polypeptide of CD2-activated cells was immunoprecipitated with antiphosphotyrosine antibodies and migrated to a 21- to 23-kDa position during SDS/PAGE. These results indicate that stimulation of human T cells via the CD2 Ag with the T112 and T113 mAb activates not only protein kinase C but also tyrosine kinase(s), resulting in the phosphorylation of the CD3 γ-chain and the tyrosine phosphorylation of the ζ-chain, respectively.

Original languageEnglish (US)
Pages (from-to)1010-1014
Number of pages5
JournalJournal of Immunology
Volume144
Issue number3
StatePublished - Jan 1 1990

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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