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Gene Review

Car3  -  carbonic anhydrase 3

Mus musculus

Synonyms: BB219044, CA-III, Ca3, Car-3, Carbonate dehydratase III, ...
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Disease relevance of Car3

  • Expression of CA III in rodent models of obesity [1].
  • Protracted 60 min ischemia yielded equal amounts of both partially and completely (both sulfhydryls) modified CAIII due to irreversible oxidization [2].
  • The physiological role of carbonic anhydrase III in slow-twitch skeletal muscle was investigated using isolated mouse soleus (N = 30) contracting once every 1.7 min for 75 min in Krebs-Henseleit solution gassed with either 95% oxygen - 5% carbon dioxide (normocapnia) or 90% oxygen - 10% carbon dioxide (hypercapnia) [3].

High impact information on Car3

  • RNA blots demonstrate that CAIII messages can be detected in a variety of cell types but that high-level expression is limited to human fetal and adult skeletal muscle and to rodent slow skeletal muscle and liver [4].
  • Previous reports have established the CAI and CAII isozyme genes to be closely linked on chromosome 8, and the assignment of the CAIII gene to the same chromosome raises the possibility that these genes may all be linked at a single complex locus [4].
  • We have isolated a full-length representative of a CAIII mRNA transcript from an adult human muscle cDNA library, and we present the complete nucleotide sequence of this cDNA clone [4].
  • They had normal amounts and distribution of fat, despite the fact that carbonic anhydrase III constitutes about 30% of the soluble protein in adipocytes [5].
  • Carbonic anhydrase III has also been implicated in the response to oxidative stress [5].

Chemical compound and disease context of Car3


Biological context of Car3


Anatomical context of Car3

  • Compared with cultures maintained in the absence of insulin, 3T3 adipocytes maintained in the presence of insulin exhibited 65-90% lower concentrations of CA III [10].
  • Protein and mRNA analyses show that CAIII is present at low levels in cultured myoblasts and is abundant in adult skeletal muscle and in liver [11].
  • As the notochord forms the nucleus pulposus in fetal mice, CAIII mRNA levels remain very high [9].
  • By two weeks post partum (p.p.), CAIII mRNAs are detected mainly in slow muscle fibers [9].
  • In addition to the notochord, CAIII transcripts are detected prenatally in several other non-muscle tissues: in cells of the choroid plexus, endocardial cushion and ureter, and in adipocytes [9].

Associations of Car3 with chemical compounds

  • Inhibition of the sulfonamide-sensitive activity had no effect on contractile and fatigue characteristics, whereas inhibition of the sulfonamide-resistant carbonic anhydrase III activity led to a significant increase in resistance to fatigue [12].
  • Similarly, cultures maintained in a low bicarbonate/CO2 media (GibCO2-I medium containing 1 mM bicarbonate under an atmosphere of 100% humidified air) displayed 30-50% lower CA II and CA III concentrations [10].
  • The high sensitivity of mucus CA to acetazolamide rules out its identity with cytosolic CAIII [13].
  • When the active site residue Phe 198 in human CA III was replaced with Leu, measurement of catalysis showed that Glu 64 retained but Asp 64 lost its capacity to act as a proton shuttle [14].
  • Maximal turnover rates for the hydration of CO2 and the depletion of 18O from CO2 catalyzed by carbonic anhydrase III (CA III) and carbonic anhydrase V (CA V) are limited by proton transfer involving zinc-bound water or hydroxide in the active site [14].

Other interactions of Car3

  • Copper loading of normal mice also decreased hepatic CAIIIA mRNA, suggesting that the decrease in CAIII mRNA in the tx mouse liver is a secondary consequence of the high copper levels in the liver [6].
  • Carbonic anhydrase III occurred alone in some and with CA II in other sites but was often absent from CA-II-containing types of cells [15].
  • Importantly, Car1, Car3, and Car13 showed very high expression levels in certain tissues as compared to the other CAs, suggesting that these low activity isozymes may also participate in physiological processes other than CA catalysis and high expression levels are required to fulfil their functions in the body [16].
  • Both CA III and non-CA III activities, measured by 18O mass spectrometry, were present in 3T3-L1 and 3T3-F442A adipocytes; however, no CA activity was detected in 3T3 preadipocytes of either line [10].
  • One potential muscle marker, carbonic anhydrase III, is expressed in early mesoderm and subsequently in the notochord, similarly to the Brachyury gene [17].

Analytical, diagnostic and therapeutic context of Car3


  1. Expression of CA III in rodent models of obesity. Stanton, L.W., Ponte, P.A., Coleman, R.T., Snyder, M.A. Mol. Endocrinol. (1991) [Pubmed]
  2. Anti-oxidative response of carbonic anhydrase III in skeletal muscle. Zimmerman, U.J., Wang, P., Zhang, X., Bogdanovich, S., Forster, R. IUBMB Life (2004) [Pubmed]
  3. Carbonic anhydrase III inhibition in normocapnic and hypercapnic contracting mouse soleus. Barclay, J.K. Can. J. Physiol. Pharmacol. (1987) [Pubmed]
  4. 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. Wade, R., Gunning, P., Eddy, R., Shows, T., Kedes, L. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  5. Carbonic anhydrase III is not required in the mouse for normal growth, development, and life span. Kim, G., Lee, T.H., Wetzel, P., Geers, C., Robinson, M.A., Myers, T.G., Owens, J.W., Wehr, N.B., Eckhaus, M.W., Gros, G., Wynshaw-Boris, A., Levine, R.L. Mol. Cell. Biol. (2004) [Pubmed]
  6. Decreased carbonic anhydrase III levels in the liver of the mouse mutant 'toxic milk' (tx) due to copper accumulation. Grimes, A., Paynter, J., Walker, I.D., Bhave, M., Mercer, J.F. Biochem. J. (1997) [Pubmed]
  7. Mapping of mouse carbonic anhydrase-3, Car-3: another locus in the homologous region of mouse chromosome 3 and human chromosome 8. Beechey, C., Tweedie, S., Spurr, N., Ball, S., Peters, J., Edwards, Y. Genomics (1990) [Pubmed]
  8. Nucleotide sequence and structure of the mouse carbonic anhydrase III gene. Kim, G., Lee, T., Wynshaw-Boris, A., Levine, R.L. Gene (2001) [Pubmed]
  9. Carbonic anhydrase III, an early mesodermal marker, is expressed in embryonic mouse skeletal muscle and notochord. Lyons, G.E., Buckingham, M.E., Tweedie, S., Edwards, Y.H. Development (1991) [Pubmed]
  10. Differentiation-dependent expression of carbonic anhydrase II and III in 3T3 adipocytes. Lynch, C.J., Hazen, S.A., Horetsky, R.L., Carter, N.D., Dodgson, S.J. Am. J. Physiol. (1993) [Pubmed]
  11. Mouse carbonic anhydrase III: nucleotide sequence and expression studies. Tweedie, S., Edwards, Y. Biochem. Genet. (1989) [Pubmed]
  12. Carbonic anhydrase in mouse skeletal muscle and its influence on contractility. Côté, C.H., Jomphe, N., Odeimat, A., Frémont, P. Biochem. Cell Biol. (1994) [Pubmed]
  13. A distinct carbonic anhydrase in the mucus of the colon of humans and other mammals. Kleinke, T., Wagner, S., John, H., Hewett-Emmett, D., Parkkila, S., Forssmann, W.G., Gros, G. J. Exp. Biol. (2005) [Pubmed]
  14. Glutamate and aspartate as proton shuttles in mutants of carbonic anhydrase. Qian, M., Tu, C., Earnhardt, J.N., Laipis, P.J., Silverman, D.N. Biochemistry (1997) [Pubmed]
  15. Comparative distribution of carbonic anhydrase isozymes III and II in rodent tissues. Spicer, S.S., Ge, Z.H., Tashian, R.E., Hazen-Martin, D.J., Schulte, B.A. Am. J. Anat. (1990) [Pubmed]
  16. A systematic quantification of carbonic anhydrase transcripts in the mouse digestive system. Pan, P.W., Rodriguez, A., Parkkila, S. BMC Mol. Biol. (2007) [Pubmed]
  17. Myogenesis in the mouse. Buckingham, M.E., Lyons, G.E., Ott, M.O., Sassoon, D.A. Ciba Found. Symp. (1992) [Pubmed]
  18. Production and characterization of monoclonal antibodies to human carbonic anhydrase III. Azzazy, H.M., Cummings, P.J., Ambrozak, D.R., Christenson, R.H. Hybridoma (1998) [Pubmed]
  19. Characterisation of cDNA clones for rat muscle carbonic anhydrase III. Kelly, C.D., Carter, N.D., Jeffery, S., Edwards, Y.H. Biosci. Rep. (1988) [Pubmed]
  20. Forced MyHCIIB expression following targeted genetic manipulation of conditionally immortalized muscle precursor cells. Harris, J.M., Morgan, J.E., Rosenblatt, J.D., Peckham, M., Edwards, Y.H., Partridge, T.A., Porter, A.C. Exp. Cell Res. (1999) [Pubmed]
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