Abstract
The carbonic anhydrases are involved in a variety of physiological functions that are important for the survival of nearly all species. The most important biochemical function of these enzymes is the interconversion of carbon dioxide and water into bicarbonate ions and protons. These metabolites are used in a wide variety of metabolic pathways (Tashian, 1989). Some of the enzymes have other catalytic activities, although their physiological importance is not understood at this time (Verpoorte et al., 1967; Cabiscol and Levine, 1996). In humans, twelve carbonic anhydrases or carbonic anhydrase-related proteins are known to exist that belong to the alpha family of CAs (Hewett-Emmett and Tashian, 1996).
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Bergenhem NCH, Venta PJ, Hopkins PJ, Kim HJ, Tashian RE (1992) Mutation creates an open reading frame within the 5´ untranslated region of macaque erythrocyte carbonic anhydrase (CA) I mRNA that suppresses CA I expression and supports the scanning model for translation. Proc Nati Acad Sci USA 89: 8798–8802
Boyer SH, Siggers DC, Kreuger LJ (1973) Caveat to protein replacement therapy for genetic disease. Immunological implications of accurate molecular diagnosis. Lancet 2 (830): 654–659
Brion LP, Suarez C, Zhang H, Cammer W (1994) Up-regulation of carbonic anhydrase isozyme IV in CNS of mice genetically deficient in carbonic anhydrase II. J Neurochem 63: 360–366
Cabiscol E, Levine RL (1996) The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation. Proc Nad Acad Sci USA 93: 4170–4174
Carter ND (1972) Carbonic anhydrase II polymorphism in Africa. Hum Hered 22: 539–541
Carter ND, Tanis RJ, Tashian RE, Ferrell RE (1973) Characterization of a new variant of human red cell carbonic anhydrase I, Ca If London (102 Glu → Lys). Biochem Genet 10: 399–408
Chegwidden WR, Wagner LE, Yenta PJ, Bergenhem NCH, Yu Y-SL, Tashian RE (1994) Marked zinc activation of ester hydrolysis by a mutation 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I. Hum Mutat 4: 294–296
Dahlberg G (1938) On rare defects in human populations with particular regard to inbreeding and isolation effects. Proc Roy Soc Edinburgh 58: 213–232
Dean M, Stephens JC, Winkler C, Lomb DA, Ramsburg M, Boaze R, Stewart C, Charbonneau L, Goldman D, Albaugh BJ et al. (1994) Polymorphic admixture typing in human ethnic populations. Am J Hum Genet 55: 788–808
Edwards Y, Williams S, West L, Lipowicz S, Sheer D, Attwood J, Sarkar R, Saha N, Povey S (1990) The polymorphic human DNA sequence D8S8 assigned to 8q13–21.1, close to the carbonic anhydrase gene cluster, by isotopic and nonisotopic in situ hybridization and by linkage analysis. Ann Hum Genet 54: 131–139
Fathallah DM, Bejaoui M, Sly WS, Lakhoua R, Dellagi K (1994) A unique mutation underlying carbonic anhydrase II deficiency syndrome in patients of Arab descent. Hum Genet 94: 581–582
Ghandour MS, Skoff RP, Venta PJ, Tashian RE (1989) Ologodendrocytes express a normal phenotype in carbonic anhydrase II-deficient mice. J Neurosci Res 23: 180–190
Giannelli F, Choo KH, Rees DJG, Boyd Y, Rizza CR, Brownlee GG (1983) Gene deletions in patients with haemophilia B and anti-factor IX antibodies. Nature 303: 181–182
Goriki K, Kawamoto S, Tashian RE (1980) The new variant carbonic anhydrase in the Japanese: CAINakasaki 1 (76 Arg → Gln) and CAIHiroshima 2. Hemoglobin 4: 653–657
Hewett-Emmett D, Welty RJ, Tashian RE (1983) A widespread silent polymorphism of human carbonic anhydrase III (31 Ile in equilibrium Val): implications for evolutionary genetics. Genetics 105: 409–420
Hewett-Emmett D, Tashian RE (1996) Functional diversity, conservation, and convergence in the evolution of the α-, β-, and γ-carbonic anhydrase gene families. Mol Phylogenet Evol 5: 50–77
Hu PY, Roth DE, Skaggs LA, Venta PJ, Tashian RE, Guibaud P, Sly WS (1992) A splice junction mutation in intron 2 of the carbonic anhydrase II gene of osteopetrosis patients from Arabic countries. Hum Mutat 1: 288–292
Hu PY, Ernst AR, Sly WS, Venta PJ, Skaggs LA, Tashian RE (1994) Carbonic anhydrase II deficiency: single-base deletion in exon 7 is the predominant mutation in Caribbean Hispanic patients. Am J Hum Genet 54: 602–608
Hu PY, Waheed A, Sly WS (1997) Partial rescue of human carbonic anhydrase II frameshift mutation by ribosomal frameshift. Proc Natl Acad Sci USA 92: 2136–2140
Jones GL (1982) A chemical and enzymological account of the effects of genetic and post-translational modifications on human erythrocyte CA II: Description of a new variant CA II Melbourne. Proc Hum Genet Soc Australia 6: 45
Jones GL, Shaw DC (1982) A polymorphic variant of human erythrocyte carbonic anhydrase I with widespread distribution in Australian Aborigines, CA I Australia-9 (8 Asp → Gly). Biochem Genet 20: 943–977
Jones GL, Sofro ASM, Shaw DC (1982) Chemical and enzymological characterization of an Indonesian variant of human erythrocyte carbonic anhydrase II, CA II Jogjakarta (17 His → Glu). Biochem Genet 20: 979–1000
Kageoka T, Hewett-Emmett D, Stroup SK, Yu Y-L, Tashian RE (1981) Amino acid substitution and chemical characterization of a Japanese variant of carbonic anhydrase I: CA I Hiroshima-1 (86 Asp → Gly). Biochem Genet 19: 535–549
Kendall AG, Tashian RE (1977) Erythrocyte carbonic annhydrase I: Inherited deficiency in humans. Science 197: 471–472
Lai L-W, Chan DM, Erickson RP, Hsu SJ, Lien Y-HH (1998) Correction of renal tubular acidosis in carbonic anhydrase II-deficient mice with gene therapy. J Clin Invest 101: 1320–1325
Lewis SE, Erickson RP, Barnett LB, Venta PJ, Tashian RE (1988) N-ethyl-N-nitrosoureainduced null mutation at the mouse Car-2 locus: an animal model for human carbonic anhydrase II deficiency syndrome. Proc Natl Acad Sci USA 85: 1962–1966
Lin K-TD, Deutsch HF (1972) Human carbonic anhydrases. VIII. Isolation and characterization of a polymorphic form of a C type isozyme. J Biol Chem 247: 3761–3766
Mancuso DJ, Tuley EA, Castillo R, de Bosch N, Mannucci PM, Sadler JE (1994) Characterization of partial gene deletions in type III von Willebrand disease with alloantibody inhibitors. Throm Haemost 72: 180–185
Meldrum NU, Roughton FJW (1933) Carbonic anhydrase: Its preparation and properties. J Physiol 80: 113–142
Mohrenweiser HW, Larsen RD, Neel JV (1989) Development of molecular approaches to estimating germinal mutation rates. I. Detection of insertion/deletion/rearrangements variants in the human genome. Mutation Res 212: 241–252
Mohrenweiser H, Neel JV, Mestriner MA, Salzano FM, Migliazza E, Simoes AL, Yoshihara CM (1979) Electrophoretic variants in three Amerindian tribes: the Baniwa, Kanamari, and Central Pano of western Brazil. Am J Phys Anthropol 50: 237–246
Osborne WRA, Tashian RE (1974) Thermal inactivation studies of normal and variant human erythrocyte carbonic anhydrases by using a sulphonamide-binding assay. Biochem J 141: 219–225
Roth DE, Venta PJ, Tashian RE, Sly WS (1992) Molecular basis of human carbonic anhydrase II deficiency. Proc Natl Acad Sci USA 89: 1804–1808
Sly WS, Hewett-Emmett D, Whyte MP, Yu Y-SL, Tashian RE (1983) Carbonic anhydrase II deficiency identified as the primary defect in the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification. Proc Nail Acad Sci USA 80: 2752–2756
Sly WS, Whyte MP, Sundram V, Tashian RE, Hewett-Emmett D, Guibaud P, Vainsel M, Baluarte HJ, Gruskin A, Al-Mosawi M, Sakati N, Ohlsson A (1985) Carbonic anhydrase II deficiency in 12 families with the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification. New Eng J Med 313: 139–145
Sly WS, Hu PY (1995a) The carbonic anhydrase II deficiency syndrome: osteopetrosis with renal tubular acidosis and cerebral calcification. In: A Beaudet, WS Sly, D Valle (eds): The metabolic basis of inherited disease, Seventh Edition, McGraw-Hill, New York, 4113–4124
Sly WS, Hu PY (1995b) Human carbonic anhydrases and carbonic anhydrase deficiencies. Annu Rev Biochem 64: 375–401
Soda H, Yukizane S, Koga Y, Aramaki S, Kato H (1996) A point mutation in exon 3 (His 107 Tyr) in two unrelated Japanese patients with carbonic anhydrase II deficiency and central nervous system involvement. Hum Genet 97: 435–437
Soda H, Yukizane S, Yoshida I, Aramaki S, Kato H (1995) Carbonic anhydrase II deficiency in a Japanese patient produced by a nonsense mutation (TAT → TAG) at Tyr 40 in exon 2, (Y40X). Hum Mutat 5: 348–350
Tanis RJ, Ferrell RE, Tashian RE (1973) Substitution of lysine for threonine at position 100 in human carbonic anhydrase Id Michigan. Biochem Biophys Res Commun 51: 699–703
Tashian RE, Riggs SK, Yu Y-L (1966) Characterization of a mutant human erythrocyte carbonic anhydrase: carbonic anhydrase Ic Guam. The amino acid substitution and carboxylesterase and hydratase activities. Arch Biochem Biophys 117: 320–327
Tashian RE (1989) The carbonic anhydrases: Widening perspectives on their evolution, expression, and function. BioEssays 10: 186–192
Tashian RE (1992) Genetics of the mammalian carbonic anhydrases. Adv Genet 30: 321–357
Tashian RE, Kendall AG, Carter ND (1980) Inherited variants of human red cell carbonic anhydrases. Hemoglobin 4: 635–651
Tashian RE, Hewett-Emmett D, Goodman M (1983) On the evolution and genetics of carbonic anhydrases I, II, and III. Isoymes: Curr Top Biol Med Res 7: 79–100
Tashian RE, Plato CC, Shows TB Jr (1963) Inherited variant of erythrocyte carbonic anhydrase in Micronesians from Guam and Saipan. Science 140: 53–54
Tashian RE, Venta PJ, Nicewander PH, Hewett-Emmett D (1990) Evolution, structure, and expression of the carbonic anhydrase multigene family. Prog Clin Biol Res 344: 159–175
Tu C, Couton JM, Van Heeke G, Richards NGJ, Silverman DN (1993) Kinetic analysis of a mutant (His107 → Tyr) responsible for human carbonic anhydrase II deficiency syndrome. J Biol Chem 268: 4775–4779
Venta PJ, Hewett-Emmett D, Tashian RE (1991b) Simple method to convert DNA sequence variation into sites cut by restriction endonucleases: utility shown by typing the human CA3 and mouse strain Car-2 polymorphisms. Am J Hum Genet 49: 445
Venta PJ, Tashian RE (1990) PCR detection of the TaqI polymorphism at the CA2 locus. Nucleic Acids Res 18: 5585
Venta PJ, Tashian RE (1991) PCR detection of a BstNI RSP in exon 6 of the human carbonic anhydrase II locus, CA2. Nucleic Acids Res 19: 4795
Venta PJ, Welty RJ, Johnson TM, Sly WS, Tashian RE (1991a) Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His → Tyr): complete structure of the normal human CA II gene. Am J Hum Genet 49: 1082–1090
Verpoorte JA, Mehta S, Edsall JT (1967) Esterase activities of human carbonic anhydrase B and C. J Biol Chem 242: 4221–4229
Velisek L, Moshe SL, Cammer W (1993) Reduced susceptibility to seizures in carbonic anhydrase II-deficient mutant mice. Brain Res Dev Brain Res 72: 321–324
Whyte MP, Murphy WA, Fallon MD, Sly WS, Teitelbaum SL, McAlister WH, Avioli LV (1980) Osteopetrosis, renal tubular acidosis and basal ganglia calcification in three sisters. Am J Med 69: 64–74
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Venta, P.J. (2000). Inherited deficiencies and activity variants of the mammalian carbonic anhydrases. In: Chegwidden, W.R., Carter, N.D., Edwards, Y.H. (eds) The Carbonic Anhydrases. EXS 90, vol 90. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8446-4_19
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DOI: https://doi.org/10.1007/978-3-0348-8446-4_19
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