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J Biol Chem, Vol. 273, Issue 38, 24620-24623, September 18, 1998
From the Edward A. Doisy Department of Biochemistry and Molecular
Biology, Saint Louis University School of Medicine,
St. Louis, Missouri 63104
Carbonic anhydrase V (CA-V) is a mitochondrial
enzyme that provides bicarbonate for pyruvate carboxylase in liver and
kidney. In the course of a survey of the tissue distribution of CA-V, we detected intense immunostaining in pancreatic islets when sections from rat and mouse pancreases were reacted with a polyclonal antibody to recombinant mouse CA-V. The distribution and large number of CA-V-positive cells in each islet suggested that they represented beta
cells. Double immunofluorescence staining of tissue sections and
isolated islet cells showed cellular colocalization of CA-V and
insulin, confirming that beta cells contain CA-V. Western blotting of
rat islets of Langerhans and primary beta cells showed 33- and 30-kDa
polypeptides of precursor and mature CA-V, respectively. The CA-V
expression was beta cell-specific since no CA-V immunoreaction was
detected in the primary alpha cells. Immunohistochemical staining for
CA-I, CA-II, CA-IV, CA-VI, and CA-IX was negative in beta cells, and
Western blotting of beta cells also failed to identify any CA in beta
cells except CA-V. The specific localization of CA-V in beta cells led
us to hypothesize that CA-V may be functionally linked to the
regulation of insulin secretion. Consistent with this hypothesis, the
CA inhibitor acetazolamide was found to be a strong inhibitor of
glucose-stimulated insulin secretion by isolated rat pancreatic
islets.
Expression of Carbonic Anhydrase V in Pancreatic Beta Cells
Suggests Role for Mitochondrial Carbonic Anhydrase in Insulin
Secretion
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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