Carbonic anhydrase III, muscle specific

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Carbonic anhydrase III, muscle specific
PDB rendering based on 1flj.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols CA3 ; CAIII; Car3
External IDs Template:OMIM5 Template:MGI HomoloGene: 31298
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Carbonic anhydrase III, muscle specific, also known as CA3, is a human gene.

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.[1]

References

  1. ↑ "Entrez Gene: CA3 carbonic anhydrase III, muscle specific".

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. 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. 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. 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. 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. 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. PMID 3099285.
  • 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. 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. 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. PMID 6119426.
  • Shima K, Tashiro K, Hibi N; et al. (1983). "Carbonic anhydrase-III immunohistochemical localization in human skeletal muscle". Acta Neuropathol. 59 (3): 237–9. PMID 6221502.
  • Heath R, Schwartz MS, Brown IR, Carter ND (1983). "Carbonic anhydrase III in neuromuscular disorders". J. Neurol. Sci. 59 (3): 383–8. PMID 6410007.
  • Wåhlstrand T, Wistrand PJ (1980). "Carbonic anhydrase C in the human renal medulla". Ups. J. Med. Sci. 85 (1): 7–17. 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. PMID 6784712.
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