Calcium dependent activation of the NF-AT transcription factor by p59fyn

FEBS Lett. 1993 Jun 1;323(3):233-5. doi: 10.1016/0014-5793(93)81346-2.

Abstract

A reporter gene under the control of a T-cell antigen receptor element was activated in Jurkat cells by antigen receptor triggering or by a combination of phorbol myristate acetate, which activates protein kinase C, and a calcium ionophore. Both these signals were necessary for expression of the reporter gene. When co-transfected with a construct capable of overexpressing the tyrosine kinase p59fyn, the reporter gene was activated by PMA alone. Thus p59fyn could replace the calcium ionophore but not activation of protein kinase C. The activation by p59fyn plus PMA was blocked by EGTA and by the immunosuppressant drug cyclosporin A.

MeSH terms

  • Calcimycin / pharmacology
  • Calcium / pharmacology*
  • Chloramphenicol O-Acetyltransferase / genetics
  • Chloramphenicol O-Acetyltransferase / metabolism
  • Cyclosporine / pharmacology
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Egtazic Acid / pharmacology
  • Humans
  • NFATC Transcription Factors
  • Nuclear Proteins*
  • Plasmids
  • Protein-Tyrosine Kinases / metabolism*
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-fyn
  • Recombinant Proteins / metabolism
  • T-Lymphocytes / physiology
  • Tetradecanoylphorbol Acetate / pharmacology
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*
  • Transfection
  • Tumor Cells, Cultured

Substances

  • DNA-Binding Proteins
  • NFATC Transcription Factors
  • Nuclear Proteins
  • Proto-Oncogene Proteins
  • Recombinant Proteins
  • Transcription Factors
  • Calcimycin
  • Egtazic Acid
  • Cyclosporine
  • Chloramphenicol O-Acetyltransferase
  • Protein-Tyrosine Kinases
  • FYN protein, human
  • Proto-Oncogene Proteins c-fyn
  • Tetradecanoylphorbol Acetate
  • Calcium