Isolation and Characterization of CA XIV, a Novel Membrane-bound Carbonic Anhydrase from Mouse Kidney

• DOI: 10.1074/jbc.274.22.15701
• Publication Date: 2002-07-26T15:01:01Z
• Authors: Kiyoshi Mori; Yoshihiro Ogawa; Ken Ebihara; Naohisa Tamura; Kei Tashiro; Takashi Kuwahara; Masashi Mukoyama; Akira Sugawara; Shoichi Ozaki; Issei Tanaka; Kazuwa Nakao
• Keywords: Isolation

Carbonic anhydrase (CA) is involved in various physiological processes such as acid-base balance and transport of carbon dioxide ions. In this study, we have succeeded the isolation a novel CA from mouse kidney by use signal sequence trap method. It 337-amino acid polypeptide with calculated molecular mass 37.5 kDa, consisting putative amino-terminal sequence, domain, transmembrane short hydrophilic carboxyl terminus, which designated XIV.11The designation XIV for cloned protein Car14 gene has been approved Specialist Advisor Anhydrases Human Gene Nomenclature Committee (http://www.gene.ucl.ac.uk/nomenclature). The domain highly homologous those known CAs, especially extracellular CAs including XII, IX, VI, IV. expression study an epitope-tagged suggested that located on plasma membrane. When expressed COS-7 cells, exhibits activity predominantly associated membrane fraction. By Northern blot analysis, most abundant heart, followed skeletal muscle, brain, lung, liver. <i>In situ</i> hybridization revealed that, kidney, intensely proximal convoluted tubule, major segment bicarbonate reabsorption also outer border inner stripe medulla. conclusion, functional cDNA encoding membrane-bound CA. This will bring new insights into our understanding metabolism balance.