Am J Physiol Cell Physiol AJP: Renal Physiology
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Am J Physiol Cell Physiol 275: C1449-C1458, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 6, C1449-C1458, December 1998

Functional characterization of alternatively spliced human SERCA3 transcripts

Esteban Poch1, Stephen Leach2, Susan Snape2, Tasha Cacic2, David H. MacLennan3, and Jonathan Lytton1,2

1 Renal Division, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115; 2 Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta T2N 4N1; and 3 Banting and Best Department for Medical Research, University of Toronto, Toronto, Ontario, Canada M5G 1L6

The sarcoplasmic (or endoplasmic) reticulum Ca2+-ATPase (SERCA)-3 has been implicated in the possible dysregulation of Ca2+ homeostasis that accompanies the pathology of hypertension and diabetes. We report the molecular cloning of two alternatively spliced transcripts from the human SERCA3 gene, ATP2A3, that encode proteins that differ at their carboxy termini by 36 amino acids. SERCA3 transcripts were most abundantly expressed in lymphoid tissues, intestine, pancreas, and prostate. The two human SERCA3 proteins encoded by alternatively spliced transcripts were recognized by the monoclonal antibody PL/IM430 and demonstrated Ca2+ uptake and ATPase activity with an apparent Ca2+ affinity 0.5 pCa unit lower than that of other SERCA gene products. The subcellular distribution of SERCA3 protein was indistinguishable from that of SERCA2b, with expression in the nuclear envelope and in the endoplasmic reticulum throughout the cell. Two variant SERCA3 constructs, huS3-I and huS3-II, were isolated that encode proteins with three amino acid differences: Ala-673 (in huS3-I) substituted for Thr (in huS3-II), Ile-817 substituted for Met, and an insertion of Glu-994. huS3-I displayed a 10-fold lower capacity to transport Ca2+ than huS3-II.

molecular cloning; calcium-adenosinetriphosphatase; Jurkat T cells; kidney


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