Translocation of protein kinase C during membrane immunoglobulin- mediated transmembrane signaling in B lymphocytes

• Published in: The Journal of immunology (1950) Vol. 136; no. 6; pp. 2300 - 2304
• Main Authors: Chen, ZZ, Coggeshall, KM, Cambier, JC
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Am Assoc Immnol 15.03.1986; American Association of Immunologists
• Subjects: Analysis of the immune response. Humoral and cellular immunity; Animals; Antibodies, Anti-Idiotypic - immunology; Antibodies, Monoclonal - immunology; B-Lymphocytes - enzymology; B-Lymphocytes - physiology; B-Lymphocytes - ultrastructure; Biological and medical sciences; Bucladesine - pharmacology; Cell Compartmentation; Cell Membrane - physiology; cell surface; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Immunobiology; Immunoglobulin D - metabolism; Immunoglobulin M - metabolism; immunoglobulins; lymphocytes B; Mice; Organs and cells involved in the immune response; Phosphatidylinositols - metabolism; Protein Kinase C - metabolism; Receptors, Antigen, B-Cell - physiology; Theophylline - pharmacology; Intracellular transport; Immunoglobulins; Protein kinase C; Enzyme; Rodentia; Crosslinking; B-Lymphocyte; Metabolism; Vertebrata; Mammalia; Mouse; Inositophospholipide; Plasma membrane
• ISSN: 0022-1767; 1550-6606
• DOI: 10.4049/jimmunol.136.6.2300

Previous studies have implicated a role for protein kinase C (PKC) in transmembrane signal transduction by B cell surface immunoglobulin (Ig). Specifically, the pharmacologic PKC activator phorbol myristate acetate mimics the biologic effects of mIg cross-linking ligands, and cross-linking of membrane Ig (mIg) induces polyphosphoinositide hydrolysis generating diacylglycerol, a potent activator of PKC. Studies described here additionally implicate PKC in mIg-mediated signaling by demonstrating rapid translocation of activatable PKC (PKCa) from cytosol to Triton-soluble membrane fractions after cross-linking of cell surface IgM or IgD. This response, which is also induced by phorbol myristate acetate and lipolysaccharide, is detectable within 1 min of mIg cross-linking and is followed within 4 min by additional translocation of PKCa to a Triton-insoluble particulate compartment. The ability of dbcAMP plus theophylline to inhibit polyphosphoinositide hydrolysis, PKCa translocation, and the B cell's subsequent biological response suggests that these events may be causally related.