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Biochem Pharmacol. 1996 Aug 9;52(3):413-24.

Characterization of the 78 kDa mast cell protein phosphorylated by the antiallergic drug cromolyn and homology to moesin.

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Department of Pharmacology and Experimental Therapeutics, Tufts University School of Medicine, Boston, MA 02111, USA.


Mast cells (MC) can be stimulated to secrete by cross-linking immunoglobulin E bound to specific surface receptors, as well as in response to polycationic molecules such as substance P and compound 48/80. The antiallergic drug disodium cromoglycate (cromolyn) inhibited MC secretion and rapidly incorporated phosphate into a 78 kDa protein, speculated to be its mode of action. This protein was purified by single and two-dimensional gel electrophoresis, and was shown to be phosphorylated primarily on serine residues by protein kinase C. Partial amino acid sequencing of two generated fragments was identical to that of portions of mouse moesin, a member of the band 4.1 superfamily of proteins, with no definitive function known to date. Polyclonal antibodies raised against the rat basophil leukemia cell moesin cDNA expressed in Escherichia coli immunoprecipitated the 78 kDa phosphoprotein quantitatively, and immunocytochemistry localized it to the plasma membrane. Reversible phosphorylation of this 78 kDa phosphoprotein could affect its possible cytoskeletal binding through which it may regulate stimulus-secretion coupling in MC.

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