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Antibody‐induced cAMP accumulation in splenocytes from athymic nude mice
Author(s) -
Wiener E.C.,
Griffor M.C.,
Scarpa Antonio
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80417-9
Subject(s) - forskolin , splenocyte , antibody , adenylate kinase , microbiology and biotechnology , chemistry , cyclase , endocrinology , protein kinase a , phosphatidylinositol , medicine , biology , enzyme , signal transduction , biochemistry , receptor , immunology
Products from the hydrolysis of phosphatidylinositol 4,5‐bisphosphate (IP 3 ) can increase and/or potentiate cAMP accumulation in a variety of cells. Antibody to surface immunoglobulins activates IP 3 hydrolysis in B‐lymphocytes. In this study we have examined whether anti‐Ig also stimulated and/or potentiated increases in the cAMP levels of splenocytes from athymic nude mice. Furthermore, since TPA potentiates anti‐Ig‐induced DNA synthesis and cAMP modulates DNA synthesis, the effects of TPA on any anti‐Ig‐induced changes in cAMP were also studied. Antibody (25 μg/ml) stimulated a rapid rise in cAMP which increased from 250 fmol/10 6 cells to 400 fmol/10 6 cells within 1 min and then subsided to 310 fmol/10 6 cells by 10 min. TPA (96 nM) suppressed the anti‐Ig‐induced cAMP accumulation at 1 min by 60%, but potentiated the forskolin (114 μM)‐induced rise by 151%. Two other activators of protein kinase C, dioctanoylglycerol (5 μM), and anti‐Ig (25 μg/ml), also potentiated the forskolin response by 198% and 52%, respectively. These results suggest that modulation of the adenylate cyclase system by anti‐Ig may act in concert with cytokines and/or prostaglandins secreted by other lymphoid cells to define the state of proliferation or differentiation in B‐cells.