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J Biol Chem, Vol. 274, Issue 48, 34343-34349, November 26, 1999

Calbindin-D_28k Controls [Ca²⁺]_i and Insulin Release
EVIDENCE OBTAINED FROM CALBINDIN-D_28k KNOCKOUT MICE AND  CELL LINES

Karen Sooy, Thomas Schermerhorn^¶, Mitsuhiko Noda^¶, Manju Surana, William B. Rhoten^**, Michael Meyer, Norman Fleischer, Geoffrey W. G. Sharp^¶, and Sylvia Christakos

From the  Department of Biochemistry and Molecular Biology, University of Medicine and Dentistry of New Jersey, New Jersey Medical School and Graduate School of Biomedical Sciences, Newark, New Jersey 07103, the ^¶ Department of Molecular Medicine, New York State College of Veterinary Medicine, Cornell University, Ithaca, New York 14853, the ^** Department of Anatomy, Cell and Neurobiology, Marshall University School of Medicine, Huntington, West Virginia 25704, the  Department of Neurochemistry, Max-Planck Institute, D-82152 Martinsried, Germany, and the  Department of Medicine and the Diabetes Research and Training Center, Albert Einstein College of Medicine, Bronx, New York 10461

The role of the calcium-binding protein, calbindin-D_28k in potassium/depolarization-stimulated increases in the cytosolic free Ca²⁺ concentration ([Ca²⁺]_i) and insulin release was investigated in pancreatic islets from calbindin-D_28k nullmutant mice (knockouts; KO) or wild type mice and  cell lines stably transfected and overexpressing calbindin. Using single islets from KO mice and stimulation with 45 mM KCl, the peak of [Ca²⁺]_i was 3.5-fold greater in islets from KO mice compared with wild type islets (p < 0.01) and [Ca²⁺]_i remained higher during the plateau phase. In addition to the increase in [Ca²⁺]_i in response to KCl there was also a significant increase in insulin release in islets isolated from KO mice. Evidence for modulation by calbindin of [Ca²⁺]_i and insulin release was also noted using  cell lines. Rat calbindin was stably expressed in TC-3 and HC-13 cells. In response to depolarizing concentrations of K⁺, insulin release was decreased by 45-47% in calbindin expressing TC cells and was decreased by 70-80% in calbindin expressing HC cells compared with insulin release from vector transfected TC or HC cells (p < 0.01). In addition, the K⁺-stimulated intracellular calcium peak was markedly inhibited in calbindin expressing HC cells compared with vector transfected cells (225 nM versus 1,100 nM, respectively). Buffering of the depolarization-induced rise in [Ca²⁺]_i was also observed in calbindin expressing TC cells. In summary, our findings, using both isolated islets from calbindin-D_28k KO mice and  cell lines, establish a role for calbindin in the modulation of depolarization-stimulated insulin release and suggest that calbindin can control the rate of insulin release via regulation of [Ca²⁺]_i.

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