Ia binding ligands and cAMP stimulate nuclear translocation of PKC in B lymphocytes

Nature. 1987 Jun 18-24;327(6123):629-32. doi: 10.1038/327629a0.


Altered subcellular distribution and activity of protein kinase C (PKC) is associated with transmembrane signalling in a variety of systems in which receptor occupancy leads to increased hydrolysis of polyphosphoinositides. Here we report evidence that in B lymphocytes, cyclic-cAMP-generating signal transduction pathways can activate translocation of PKC from the cytosol to the nucleus. Elevated cAMP levels and translocation of PKC to the nucleus are induced by antibodies against Ia antigens in normal B lymphocytes. Further, cAMP analogues mediate the translocation of PKC to the nucleus of these cells. These findings suggest that in physiological situations, ligation of B-lymphocyte Ia molecules by helper T cells leads to increased cAMP production which in turn causes PKC translocation to the nucleus. In view of recent observations that antibodies against Ia antigens induce differentiation of B cells, we conclude that nuclear PKC may function in the regulation of gene expression.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antibodies*
  • B-Lymphocytes / drug effects
  • B-Lymphocytes / enzymology*
  • B-Lymphocytes / immunology
  • Bucladesine / pharmacology*
  • Cell Nucleus / enzymology*
  • Cells, Cultured
  • Cyclic AMP / physiology*
  • Cytosol / enzymology
  • Histocompatibility Antigens Class II / immunology*
  • Immunoglobulin D / immunology
  • Immunoglobulin M / immunology
  • Kinetics
  • Ligands
  • Mice
  • Mice, Inbred AKR
  • Protein Kinase C / immunology
  • Protein Kinase C / metabolism*


  • Antibodies
  • Histocompatibility Antigens Class II
  • Immunoglobulin D
  • Immunoglobulin M
  • Ligands
  • Bucladesine
  • Cyclic AMP
  • Protein Kinase C