Human Carbonic Anhydrase XIV (CA14): cDNA Cloning, mRNA Expression, and Mapping to Chromosome 1

Fujikawa-Adachi, Kiyomi; Nishimori, Isao; Taguchi, Takahiro; Onishi, Saburo

doi:10.1006/geno.1999.5938

Cited by 118 publications

(92 citation statements)

References 43 publications

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“…Four of these are cytoplasmic (CA I, CA II, CA III, and CA VII) (Sly and Hu, 1995;Earnhardt et al, 1998), two are mitochondrial (CA VA and CA VB) (Fujikawa-Adachi et al, 1999), one is secreted (CA VI) (Murakami and Sly, 1987), and four are membrane associated (CA IV, CA IX, CA XII, and CA XIV) (Zhu and Sly, 1990;Pastorek et al, 1994;Ivanov et al, 1998;Tü reci et al, 1998;Mori et al, 1999). Some isozymes such as CA II are expressed in a number of different tissues, whereas others (e.g., CA VI, IX, and XIV) show a more limited distribution.…”

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confidence: 99%

Expression of hypoxia‐inducible, membrane‐bound carbonic anhydrase isozyme XII in mouse tissues

et al. 2004

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Carbonic anhydrase (CA) XII is a membrane-associated enzyme that has been demonstrated to be normally expressed in some human tissues, to be upregulated in some cancers, and to be a hypoxia-inducible gene product. In mouse, CA XII has been recently localized in the kidney. In the present study, we investigated CA XII gene and protein expression in other mouse tissues, with the kidney serving as a positive control for the reagents. The expression of CA XII mRNA was examined using polymerase chain reaction (PCR) amplification of commercial cDNAs produced from selected mouse tissues. A strong positive signal for CA XII mRNA was detected in the kidney, and weak signals were obtained in the testis and lung. Heart, spleen, liver, and skeletal muscle were negative. Immunohistochemical staining was performed using a mouse CA XII-specific antibody and biotin-streptavidin complex method. The results showed high expression of CA XII in the kidney, as expected. It was also highly expressed in the surface epithelial cells of the colon, whereas it was absent in the stomach, proximal small intestine, pancreas, liver, heart, and skeletal muscle. The maturing sperm cells showed a weak staining in a pattern that most probably indicates expression in the developing acrosomal membrane. The high expression in the kidney and colon suggests a role for CA XII in the maintenance of body ion and pH homeostasis in the mouse. However, the present findings demonstrated that CA XII has a very limited distribution in mouse tissues outside these two organs. Anat Rec Part A 277A: 171-177, 2004.

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confidence: 99%

Expression of hypoxia‐inducible, membrane‐bound carbonic anhydrase isozyme XII in mouse tissues

et al. 2004

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“…Three recently discovered isoenzymes (CA IX, XII, and XIV) are transmembrane proteins whose active sites are located on the cell exterior (11)(12)(13)(14)(15). Two of them (CA IX and XII) are highly expressed in some tumors and may be functionally related to oncogenesis (9)(10)(11)(12).…”

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confidence: 99%

Carbonic anhydrase inhibitor suppresses invasion of renal cancer cells in vitro

Parkkila

Rajaniemi

Parkkila

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

246

166

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Acidification of the extracellular milieu of malignant tumors is reported to increase the invasive behavior of cancer cells. In normal tissues, production of acid is catalyzed by carbonic anhydrases (CAs), some of which are known to be overexpressed in certain cancers. To investigate the functional role of CA activity in such cancer cells, we analyzed the effect of acetazolamide, a potent CA inhibitor, on the invasive capacity of four renal carcinoma cell lines (Caki-1, Caki-2, ACHN, and A-498). We found that 10 M acetazolamide inhibited the relative invasion rate of these cell lines between 18 -74%. The Caki-2 and ACHN cell lines displayed the highest responsiveness, and their responses clearly depended on the acetazolamide concentration in the culture medium. Immunocytochemical and Western blotting results identified the presence of CA isoenzyme II in the cytoplasm of all four cell lines and CA XII on the plasma membrane in three of four cell lines. Because acetazolamide alone reduced invasiveness of these cancer cells in vitro, we conclude that the CAs overexpressed in these renal cancer cells contribute to invasiveness, at least in vitro, and suggest that CA inhibitors may also reduce invasiveness in other tumors that overexpress one or more CAs.

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“…The basic principle of the assay is that hydration of CO 2 will cause acidi®cation of the solution, which can be detected by changes in the indicator color. The reaction vessel was a single glass tube (10 (Figure 1). CO 2 gas continually¯owed in at a rate of 150 mL/min through the No.…”

Section: Carbonic Anhydrase (Ca) Assaymentioning

confidence: 99%

“…Carbonic anhydrases (CAs) constitute a family of enzymes, consisting of 11 known forms in mammals [10,11,21,25,33]. This enzyme participates in various physiological processes that involve pH regulation, CO 2 , and HCO 3 7 transport, ion transport, and water and the electrolyte balance [32].…”

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confidence: 99%

Influence of Acetazolamide on Aqp1 Gene Expression in Testis and on Sperm Count/Motility in Epididymis of Rats

Sun

Bai

et al. 2002

Archives of Andrology

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Human Carbonic Anhydrase XIV (CA14): cDNA Cloning, mRNA Expression, and Mapping to Chromosome 1

Cited by 118 publications

References 43 publications

Expression of hypoxia‐inducible, membrane‐bound carbonic anhydrase isozyme XII in mouse tissues

Expression of hypoxia‐inducible, membrane‐bound carbonic anhydrase isozyme XII in mouse tissues

Carbonic anhydrase inhibitor suppresses invasion of renal cancer cells in vitro

Influence of Acetazolamide on Aqp1 Gene Expression in Testis and on Sperm Count/Motility in Epididymis of Rats

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