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Journal of Histochemistry and Cytochemistry, Vol. 47, 517-524, April 1999, Copyright © 1999, The Histochemical Society, Inc.

ARTICLE

Cell-specific Expression of Mitochondrial Carbonic Anhydrase in the Human and Rat Gastrointestinal Tract

Juha Saarnioa, Seppo Parkkilab,c, Anna-Kaisa Parkkilab, Abdul Waheede, Tuomo Karttunend, and William S. Slye
a Departments of Surgery, University of Oulu, Oulu, Finland
b Anatomy, University of Oulu, Oulu, Finland
c Clinical Chemistry, University of Oulu, Oulu, Finland
d Pathology, University of Oulu, Oulu, Finland
e Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St Louis, Missouri

Correspondence to: William S. Sly, Edward A. Doisy Dept. of Biochemistry and Molecular Biology, Saint Louis U. School of Medicine, 1402 S. Grand Blvd, St Louis, MO 63104.

Mitochondrial carbonic anhydrase V (CA V) in liver provides HCO3- to pyruvate carboxylase for the first step in gluconeogenesis and HCO3- to carbamyl phosphate synthetase I for the first step in ureagenesis. Because carbamyl phosphate synthetase I and ornithine transcarbamylase are also expressed in enterocytes, we tested the hypothesis that CA V is expressed in the gastrointestinal tract in addition to liver. Polyclonal rabbit antisera were raised against a polypeptide of 17 C-terminal amino acids of human CA V and against purified recombinant mouse isozyme and were used in Western blotting and immunoperoxidase staining of human and rat tissues. Immunohistochemistry showed that CA V is expressed cell-specifically in the alimentary canal mucosa from stomach to rectum. Immunoreactions for CA V were detected in the parietal cells and gastrin-producing G-cells of the stomach and in intestinal enterocytes. Western blotting of human and rat gastrointestinal tissues with isozyme-specific antibodies showed positive signals for CA V with the expected molecular mass. The findings in human tissues paralleled those in rat. The cell-specific pattern of CA V expression suggests a role for CA V in alimentary canal physiology. We propose that mitochondrial CA V participates in the detoxification of ammonia produced in the gastrointestinal tract by providing bicarbonate to carbamyl phosphate synthetase I. (J Histochem Cytochem 47:517–524, 1999)

Key Words: alimentary tract, carbonic anhydrase, enterocyte, G-cell, gut, immunohistochemistry, intestine, mitochondria, parietal cell


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