Carbonic anhydrase III, muscle specific

CA3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCA3, CAIII, Car3, carbonic anhydrase 3
External IDsMGI: 88270 HomoloGene: 31298 GeneCards: CA3
Gene location (Human)
Chr.Chromosome 8 (human)[1]
Band8q21.2Start85,373,436 bp[1]
End85,449,040 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

761

12350

Ensembl

ENSG00000164879

ENSMUSG00000027559

UniProt

P07451

P16015

RefSeq (mRNA)

NM_005181

NM_007606

RefSeq (protein)

NP_005172

NP_031632

Location (UCSC)Chr 8: 85.37 – 85.45 MbChr 3: 14.86 – 14.87 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Carbonic anhydrase 3 is an enzyme that in humans is encoded by the CA3 gene.[5]

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. CA3 is insufficient in muscles of Myasthenia Gravis patients.[6] A proportion of carriers of Duchenne muscle dystrophy have a higher CA3 level than normal. Autoantibodies to CA3 have been found to be significantly higher in patients with rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes.[7] The gene spans 10.3 kb and contains seven exons and six introns.[8]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000164879 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027559 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Shima K, Tashiro K, Hibi N, Tsukada Y, Hirai H (Jun 1983). "Carbonic anhydrase-III immunohistochemical localization in human skeletal muscle". Acta Neuropathol. 59 (3): 237–9. doi:10.1007/BF00703210. PMID 6221502.
  6. ↑ Du AL, Ren HM, Lu CZ, Tu JL, Xu CF, Sun YA (Mar 2009). "Carbonic anhydrase III is insufficient in muscles of myasthenia gravis patients". Autoimmunity. 42 (3): 209–15. doi:10.1080/08916930802668610. PMID 19301202.
  7. ↑ Liu C, Wei Y, Wang J, Pi L, Huang J, Wang P (Sep 2012). "Carbonic anhydrases III and IV autoantibodies in rheumatoid arthritis, systemic lupus erythematosus, diabetes, hypertensive renal disease, and heart failure". Clin Dev Immunol. 2012: 354594. doi:10.1155/2012/354594. PMC 3461255. PMID 23049597.
  8. ↑ "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. 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. doi:10.1097/00006982-199001010-00015. 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.
  • Väänänen HK, Autio-Harmainen H (1987). "Carbonic anhydrase III: a new histochemical marker for myoepithelial cells". J. Histochem. Cytochem. 35 (6): 683–6. doi:10.1177/35.6.3106467. 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. doi:10.1007/bf00953989. 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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