CA9

From Wikipedia, the free encyclopedia

Carbonic anhydrase IX

Identifiers

CA9; CAIX; MN

External IDs

OMIM: 603179 MGI: 2447188 HomoloGene: 20325

Gene ontology
Molecular Function:	• carbonate dehydratase activity • zinc ion binding • lyase activity • metal ion binding
Cellular Component:	• nucleus • membrane • integral to membrane
Biological Process:	• morphogenesis of an epithelium • one-carbon compound metabolic process • secretion

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001216 (mRNA)
NP_001207 (protein)

NM_139305 (mRNA)
NP_647466 (protein)

Location

Chr 9: 35.66 - 35.67 Mb

Chr 4: 43.53 - 43.53 Mb

Pubmed search

[1]

[2]

Carbonic anhydrase IX, also known as CA9, is a human gene.^[1]

Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. CA IX is a transmembrane protein and the only tumor-associated carbonic anhydrase isoenzyme known. It is expressed in all clear-cell renal cell carcinoma, but is not detected in normal kidney or most other normal tissues. It may be involved in cell proliferation and transformation. This gene was mapped to 17q21.2 by fluorescence in situ hybridization, however, radiation hybrid mapping localized it to 9p13-p12.^[1]

[edit] References

^ ^a ^b Entrez Gene: CA9 carbonic anhydrase IX.

[edit] Further reading

Nishimori I, Onishi S (2001). "Carbonic anhydrase isozymes in the human pancreas.". Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver 33 (1): 68–74. PMID 11303978.
Pastoreková S, Závadová Z, Kostál M, et al. (1992). "A novel quasi-viral agent, MaTu, is a two-component system.". Virology 187 (2): 620–6. PMID 1312272.
Pastorek J, Pastoreková S, Callebaut I, et al. (1994). "Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment.". Oncogene 9 (10): 2877–88. PMID 8084592.
Závada J, Závadová Z, Pastoreková S, et al. (1993). "Expression of MaTu-MN protein in human tumor cultures and in clinical specimens.". Int. J. Cancer 54 (2): 268–74. PMID 8486430.
Opavský R, Pastoreková S, Zelník V, et al. (1996). "Human MN/CA9 gene, a novel member of the carbonic anhydrase family: structure and exon to protein domain relationships.". Genomics 33 (3): 480–7. PMID 8661007.
Pastoreková S, Parkkila S, Parkkila AK, et al. (1997). "Carbonic anhydrase IX, MN/CA IX: analysis of stomach complementary DNA sequence and expression in human and rat alimentary tracts.". Gastroenterology 112 (2): 398–408. PMID 9024293.
Saarnio J, Parkkila S, Parkkila AK, et al. (1998). "Immunohistochemistry of carbonic anhydrase isozyme IX (MN/CA IX) in human gut reveals polarized expression in the epithelial cells with the highest proliferative capacity.". J. Histochem. Cytochem. 46 (4): 497–504. PMID 9524195.
Ivanov SV, Kuzmin I, Wei MH, et al. (1998). "Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes.". Proc. Natl. Acad. Sci. U.S.A. 95 (21): 12596–601. PMID 9770531.
Nakagawa Y, Uemura H, Hirao Y, et al. (1998). "Radiation hybrid mapping of the human MN/CA9 locus to chromosome band 9p12-p13.". Genomics 53 (1): 118–9. doi:10.1006/geno.1998.5483. PMID 9787087.
Grabmaier K, Vissers JL, De Weijert MC, et al. (2000). "Molecular cloning and immunogenicity of renal cell carcinoma-associated antigen G250.". Int. J. Cancer 85 (6): 865–70. PMID 10709109.
Kivelä AJ, Parkkila S, Saarnio J, et al. (2001). "Expression of transmembrane carbonic anhydrase isoenzymes IX and XII in normal human pancreas and pancreatic tumours.". Histochem. Cell Biol. 114 (3): 197–204. PMID 11083462.
Wingo T, Tu C, Laipis PJ, Silverman DN (2001). "The catalytic properties of human carbonic anhydrase IX.". Biochem. Biophys. Res. Commun. 288 (3): 666–9. doi:10.1006/bbrc.2001.5824. PMID 11676494.
Kivela AJ, Saarnio J, Karttunen TJ, et al. (2001). "Differential expression of cytoplasmic carbonic anhydrases, CA I and II, and membrane-associated isozymes, CA IX and XII, in normal mucosa of large intestine and in colorectal tumors.". Dig. Dis. Sci. 46 (10): 2179–86. PMID 11680594.
Koukourakis MI, Giatromanolaki A, Sivridis E, et al. (2002). "Hypoxia-regulated carbonic anhydrase-9 (CA9) relates to poor vascularization and resistance of squamous cell head and neck cancer to chemoradiotherapy.". Clin. Cancer Res. 7 (11): 3399–403. PMID 11705854.
Grabmaier K, de Weijert M, Uemura H, et al. (2002). "Renal cell carcinoma-associated G250 methylation and expression: in vivo and in vitro studies.". Urology 60 (2): 357–62. PMID 12137853.
Kaluz S, Kaluzová M, Chrastina A, et al. (2002). "Lowered oxygen tension induces expression of the hypoxia marker MN/carbonic anhydrase IX in the absence of hypoxia-inducible factor 1 alpha stabilization: a role for phosphatidylinositol 3'-kinase.". Cancer Res. 62 (15): 4469–77. PMID 12154057.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Swinson DE, Jones JL, Richardson D, et al. (2003). "Carbonic anhydrase IX expression, a novel surrogate marker of tumor hypoxia, is associated with a poor prognosis in non-small-cell lung cancer.". J. Clin. Oncol. 21 (3): 473–82. PMID 12560438.
Bui MH, Seligson D, Han KR, et al. (2003). "Carbonic anhydrase IX is an independent predictor of survival in advanced renal clear cell carcinoma: implications for prognosis and therapy.". Clin. Cancer Res. 9 (2): 802–11. PMID 12576453.