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Volume 271, Number 33, Issue of August 16, 1996 pp. 20096-20101
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Purification, Cloning, and Expression of a Novel, Endogenous, Calcium-sensitive, 28-kDa Phosphoprotein

(Received for publication, April 29, 1996, and in revised form, May 30 1996)

John A. Parente Jr. , James R. Goldenring , Anne C. Petropoulos ^§ , Ulf Hellman ^¶ and Catherine S. Chew

From the  Institute of Molecular Medicine and Genetics, Medical College of Georgia and the Augusta VA Medical Center, Augusta, Georgia 30912, ^§ Curateck Pharmaceuticals, Elk Grove Village, Illinois 60007, and the ^¶ Ludwig Institute for Cancer Research, Box 595, S-751 24 Uppsala, Sweden

In gastric parietal cells, cholinergically induced increases in intracellular free calcium concentrations have been well characterized, but little is known about the signaling events beyond the initial rise in intracellular calcium. In the present study, we report the isolation of a 28-kDa protein, which is rapidly phosphorylated in intact, enriched parietal cells in response to both the cholinergic agonist, carbachol, and the calcium ionophore, ionomycin. A combination of in situ ³²P labeling and one- and two-dimensional gel electrophoresis was used to acquire sufficient quantities of protein to obtain partial amino acid sequence. Cloning of the pp28 cDNA revealed a novel protein which we have named CSPP28 based on its calcium-sensitive phosphorylation. There are three CSPP28 mRNA species (1.7, 2.2, and 3.3 kilobases) that are widely distributed throughout a variety of rabbit tissues. Recombinant CSPP28 was phosphorylated by both crude parietal cell homogenate and purified CaM kinase II in a calcium/calmodulin-dependent manner. We propose that CSPP28 may play an important and ubiquitous role in the calcium signaling pathway.

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