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J Biol Chem, Vol. 274, Issue 22, 15701-15705, May 28, 1999
From the Carbonic anhydrase (CA) is involved in various
physiological processes such as acid-base balance and transport of
carbon dioxide and ions. In this study, we have succeeded in the
isolation of a novel CA from the mouse kidney by use of the signal
sequence trap method. It is a 337-amino acid polypeptide with a
calculated molecular mass of 37.5 kDa, consisting of a putative
amino-terminal signal sequence, a CA domain, a transmembrane domain,
and a short hydrophilic carboxyl terminus, which we designated CA
XIV. The CA domain of
CA XIV is highly homologous with those of known CAs, especially
extracellular CAs including CA XII, IX, VI, and IV. The expression
study of an epitope-tagged protein has suggested that CA XIV is located
on the plasma membrane. When expressed in COS-7 cells, CA XIV exhibits
CA activity that is predominantly associated with the membrane
fraction. By Northern blot analysis, the gene expression of CA XIV is
most abundant in the kidney and heart, followed by the skeletal muscle,
brain, lung, and liver. In situ hybridization has revealed
that, in the kidney, the gene is expressed intensely in the proximal
convoluted tubule, which is the major segment for bicarbonate
reabsorption and also in the outer border of the inner stripe of the
outer medulla. In conclusion, we have cloned a functional cDNA
encoding a novel membrane-bound CA. This study will bring new insights
into our understanding of carbon dioxide metabolism and acid-base balance.
Isolation and Characterization of CA XIV, a Novel Membrane-bound
Carbonic Anhydrase from Mouse Kidney
,,,,
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Department of Medicine and Clinical Science,
Kyoto University Graduate School of Medicine, 54 Shogoin
Kawahara-cho, Sakyo-ku, Kyoto 606-8507, Japan, ¶ Center for
Molecular Biology and Genetics, Kyoto University, 53 Shogoin
Kawahara-cho, Sakyo-ku, Kyoto 606-8057, Japan, and the
Department of Nephrology, Saiseikai Nakatsu Hospital, Shibata
2-chome 10-39, Kita-ku, Osaka 530-0012, Japan
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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