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J Biol Chem, Vol. 273, Issue 38, 24620-24623, September 18, 1998
Expression of Carbonic Anhydrase V in Pancreatic Beta Cells
Suggests Role for Mitochondrial Carbonic Anhydrase in Insulin
Secretion
Anna-Kaisa
Parkkila,
Anna L.
Scarim,
Seppo
Parkkila,
Abdul
Waheed,
John A.
Corbett, and
William S.
Sly
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.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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