Carbonic anhydrase III, muscle specific
Carbonic anhydrase 3 is an enzyme that in humans is encoded by the CA3 gene.[1]
Carbonic anhydrase III (CAIII) is a member of a multigene family (at least six separate genes are known) that encode carbonic anhydrase isozymes. These carbonic anhydrases are a class of metalloenzymes that catalyze the reversible hydration of carbon dioxide and are differentially expressed in a number of cell types. The expression of the CA3 gene is strictly tissue-specific and present at high levels in skeletal muscle and much lower levels in cardiac and smooth muscle. A proportion of carriers of Duchenne muscle dystrophy have a higher CA3 level than normal. The gene spans 10.3 kb and contains seven exons and six introns.[2]
References
Further reading
- Sly WS, Hu PY (1995). "Human carbonic anhydrases and carbonic anhydrase deficiencies.". Annu. Rev. Biochem. 64: 375–401. doi:10.1146/annurev.bi.64.070195.002111. PMID 7574487.
- Carter N, Jeffery S, Shiels A, et al. (1980). "Characterization of human carbonic anhydrase III from skeletal muscle.". Biochem. Genet. 17 (9–10): 837–54. doi:10.1007/BF00504307. PMID 120192.
- Oikarinen A, Vuori J, Autio P, et al. (1993). "Comparison of muscle-derived serum carbonic anhydrase III and myoglobin in dermatological patients: effects of isotretinoin treatment". Acta Derm. Venereol. 72 (5): 352–4. PMID 1361281.
- Oguni M, Setogawa T, Tanaka O, et al. (1992). "Immunohistochemical study of carbonic anhydrase III in the extraocular muscles of human embryos". Acta Anat (Basel) 144 (4): 316–9. doi:10.1159/000147322. PMID 1414196.
- Vuori J, Rasi S, Takala T, Väänänen K (1992). "Dual-label time-resolved fluoroimmunoassay for simultaneous detection of myoglobin and carbonic anhydrase III in serum". Clin. Chem. 37 (12): 2087–92. PMID 1764784.
- Shamsutdinov NSh, Islamov RI, Valuillin VV (1991). "[Carbonic anhydrase III--a marker of the myoepithelial cells of human salivary glands]". Biulleten' eksperimental'noĭ biologii i meditsiny 111 (3): 320–1. PMID 1905166.
- Nork TM, Wallow IH, Sramek SJ, et al. (1990). "Immunocytochemical study of an eye with proliferative vitreoretinopathy and retinal tacks". Retina (Philadelphia, Pa.) 10 (1): 78–85. PMID 1971453.
- Lloyd J, Brownson C, Tweedie S, et al. (1987). "Human muscle carbonic anhydrase: gene structure and DNA methylation patterns in fetal and adult tissues". Genes Dev. 1 (6): 594–602. doi:10.1101/gad.1.6.594. PMID 2824285.
- Lloyd JC, Isenberg H, Hopkinson DA, Edwards YH (1986). "Isolation of a cDNA clone for the human muscle specific carbonic anhydrase, CAIII". Ann. Hum. Genet. 49 (Pt 3): 241–51. doi:10.1111/j.1469-1809.1985.tb01698.x. PMID 3000276.
- Lloyd J, McMillan S, Hopkinson D, Edwards YH (1986). "Nucleotide sequence and derived amino acid sequence of a cDNA encoding human muscle carbonic anhydrase". Gene 41 (2–3): 233–9. doi:10.1016/0378-1119(86)90103-4. PMID 3086182.
- Wade R, Gunning P, Eddy R, et al. (1987). "Nucleotide sequence, tissue-specific expression, and chromosome location of human carbonic anhydrase III: the human CAIII gene is located on the same chromosome as the closely linked CAI and CAII genes". Proc. Natl. Acad. Sci. U.S.A. 83 (24): 9571–5. doi:10.1073/pnas.83.24.9571. PMC 387182. PMID 3099285. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=387182.
- Väänänen HK, Autio-Harmainen H (1987). "Carbonic anhydrase III: a new histochemical marker for myoepithelial cells". J. Histochem. Cytochem. 35 (6): 683–6. PMID 3106467.
- Nakagawa Y, Perentes E, Rubinstein LJ (1987). "Non-specificity of anti-carbonic anhydrase C antibody as a marker in human neurooncology". J. Neuropathol. Exp. Neurol. 46 (4): 451–60. doi:10.1097/00005072-198707000-00004. PMID 3110380.
- Edwards YH, Lloyd J, Parkar M, Povey S (1988). "The gene for human muscle specific carbonic anhydrase (CAIII) is assigned to chromosome 8". Ann. Hum. Genet. 50 (Pt 1): 41–7. doi:10.1111/j.1469-1809.1986.tb01937.x. PMID 3122635.
- Väänänen HK, Paloniemi M, Vuori J (1985). "Purification and localization of human carbonic anhydrase. III. Typing of skeletal muscle fibers in paraffin embedded sections". Histochemistry 83 (3): 231–5. PMID 3930440.
- Carter ND, Heath R, Jeffery S, Rodeck C (1982). "Fetal plasma carbonic anhydrase III in Duchenne dystrophy". Lancet 1 (8262): 39–40. doi:10.1016/S0140-6736(82)92574-0. PMID 6119426.
- Heath R, Schwartz MS, Brown IR, Carter ND (1983). "Carbonic anhydrase III in neuromuscular disorders". J. Neurol. Sci. 59 (3): 383–8. doi:10.1016/0022-510X(83)90023-0. PMID 6410007.
- Wåhlstrand T, Wistrand PJ (1980). "Carbonic anhydrase C in the human renal medulla". Ups. J. Med. Sci. 85 (1): 7–17. doi:10.3109/03009738009179167. PMID 6770531.
- Jeffery S, Edwards Y, Carter N (1981). "Distribution of CAIII in fetal and adult human tissue". Biochem. Genet. 18 (9–10): 843–9. doi:10.1007/BF00500117. PMID 6784712.
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PDB gallery
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1flj: CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III
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1z93: Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.
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1z97: Human Carbonic Anhydrase III: Structural and Kinetic Study of Catalysis and Proton Transfer.
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2hfw: Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III
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2hfx: Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III
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2hfy: Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III
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