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Phosphorylation of smg p21B in rat peritoneal mast cells in association with histamine release inhibition by dibutyryl‐cAMP
Author(s) -
Izushi Keiji,
Shirasaka Taihei,
Chokki Manabu,
Tasaka Kenji
Publication year - 1992
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(92)81480-a
Subject(s) - histamine , phosphorylation , mast cell , protein kinase a , compound 48/80 , kinase , phosphoprotein , protein phosphorylation , microbiology and biotechnology , biology , endocrinology , medicine , biochemistry , degranulation , receptor , immunology
IP 3 formation and histamine release from rat peritoneal mast cells stimulated by compound 48/80 were dose‐dependently inhibited by Bt 2 cAMP. These inhibitions were restored to the control level in the presence of H‐8, a protein kinase A inhibitor. The 22 kDa protein in mast cells was revealed as a markedly phosphorylated protein by incubating with Bt 2 cAMP, and this phosphorylation was also diminished by H‐8. The 22 kDa phosphoprotein of rat mast cells comigrated with phosphorylated smg p21B, purified from human platelets and phosphorylated by protein kinase A in cell‐free system, in both one‐ and two‐dimensional PAGE analysis. Moreover, 22 kDa protein in mast cells was identified as smg p21B by immunoblot analysis using an antibody against smg p21B. From the present study, it became clear that smg p21B is phosphorylated by means or protein kinase A system in rat peritoneal mast cells, and it was assumed that phosphorylated smg p21B plays some important role in the suppression of IP 3 formation and histamine release from rat peritoneal mast cells.