Evolution of the Carbonic Anhydrase Isozymes

Tashian, Richard E.; Goodman, Morris; Tanis, Robert J.; Ferrell, Robert E.; Osborne, William

doi:10.1016/b978-0-12-472704-5.50019-7

Cited by 26 publications

(27 citation statements)

References 30 publications

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“…The evidence presented in this paper, although lacking definitive amino acid sequence information, is not consistent with this proposal, since it suggests that the A, B and C isozymes of mammals are also present in birds. In contrast to previous studies on avian carbonic anhydrases [5,36], three distinct isozymes of chicken carbonic anhydrases have been observed. The tissue distributions of these isozymes closely resemble those reported for some mammalian species : A being predominantly localized in red skeletal muscles; €3 found in regions of the digestive tract; C being widely distributed throughout the body.…”

Section: Discussioncontrasting

confidence: 51%

“…These isozymes shared a 60% sequence homology and were very similar in their tertiary structures, which conclusively confirmed their common evolutionary origin from the ancestral gene, In addition, genetic studies of the primate [ll], guinea-pig [I21 and mouse [I31 B and C isozymes demonstrated these loci (Cur-I and Cur-2 respectively) to be closely linked in mammals, which further confirmed the mode of evolution of these loci as involving tandem gene duplication of an ancestral locus [52]. Tashian and coworkers [5] have also examined the relative rates of evolutionary sequence divergence by comparing the amino acid sequences of a number of mammalian B and C isozymes. Carbonic anhydrase C showed a significantly higher evolutionary rate over the past 90 million years of mammalian evolution; however, this trend is strikingly reversed in the higher primates.…”

Section: Discussionsupporting

confidence: 50%

“…The low-activity B isozyme (also called type I) and the high-activity C isozyme (type IT) have been reported in humans [14], other primates [ 5 ] , horses [18,37], pigs [22], cattle [38,39], guineapigs [12], sheep [23], dogs [25] and cats [24], and are differentially distributed in various tissues of the body.…”

Section: Discussionmentioning

confidence: 99%

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Purification, Molecular Properties and Ontogeny of Carbonic Anhydrase Isozymes. Evidence for A, B and C Isozymes in Avian and Mammalian Tissues

Holmes

1977

Eur J Biochem

105

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Carbonic anhydrase A from sheep and chicken red skeletal muscles and carbonic anhydrases B and C from chicken intestine and red cells respectively have been isolated in a high state of purity by affinity chromatography. The subunit and native molecular weights of sheep carbonic anhydrase A determined by sodium dodecyl sulphate/polyacrylamide gel electrophoresis and Sephadex gel filtration respectively were both approximately 34000. In contrast, carbonic anhydrases A, B and C from chicken exhibited a molecular weight determined by sodium dodecyl sulphate electrophoresis of 30000. The amino acid composition of sheep muscle carbonic anhydrase A was distinct from the B and C isozymes, particularly in basic amino acid content, which was significantly higher for the A isozyme (38 cJ: 24-291mol). The zinc content of sheep carbonic anhydrase A was found to be 0.81 g atom Zn/mol. The specific activities of chicken carbonic anhydrase isozyme differed significantly according to the ratio A:B:C = 1 :6:47. In addition, these isozymes differed in their affinities for sulphonamide. Chicken carbonic anhydrase A was approximately 100 times less sensitive to acetazolamide inhibition than the chicken C isozyme. Ontogenetic studies in cats showed carbonic anhydrase C to be the only form of the enzyme present in mid-term fetal animals, with carbonic anhydrase A appearing in muscle in the late stages, and carbonic anhydrase B appearing in caecum within 2 days of birth.The evidence is consistent with previous proposals for a third locus encoding carbonic anhydrase in mammalian and avian species. This isozyme (A) is a monomeric, zinc metalloenzyme, which differs from the extensively studied B and C isozymes of carbonic anhydrase in terms of catalytic efficiency, amino acid composition, molecular weight (in sheep), time of ontogenic appearance, sulphonamide inhibition and tissue distribution.

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Section: Discussioncontrasting

confidence: 51%

Section: Discussionsupporting

confidence: 50%

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Purification, Molecular Properties and Ontogeny of Carbonic Anhydrase Isozymes. Evidence for A, B and C Isozymes in Avian and Mammalian Tissues

Holmes

1977

Eur J Biochem

105

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“…This CA isozyme, which was formerly called CA C, is normally widely distributed in man and has been identified (immunologically or by purification) in erythrocytes, brain, kidney, eye, cartilage, liver, lung, skeletal muscle, pancreas, gastric mucosa, and anterior pituitary body (2,3). The other CA isozymes, whose activities toward C02 and HC03-are lower than those of CA I1 in the order of CA II>CA IV>CA I>CA I11 (4-6), appear to have a more limited tissue distribution.…”

mentioning

confidence: 99%

Positive Renal Response to Intravenous Acetazolamide in Patients with Carbonic Anhydrase II Deficiency

et al. 1985

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“…Seven distinct isozymes of carbonic anhydrase, designated CA I-CA VII, have been characterized from mammals (Tashian et al 1991). Few enzymes approach the distributional and functional diversity of carbonic anhydrase, which may be cytosolic (I, II, III, and VII), mitochondrial (V), membrane-bound (IV, V), or secreted (VI), and these range in distribution from their presence in many cell types throughout the animal kingdom (II) to more limited expressions in plants and bacteria (Fernley 1988).…”

Section: Discussionmentioning

confidence: 99%

Localization of Carbonic Anhydrase in Living Osteoclasts with Bodipy 558/568-modified Acetazolamide, a Thiadiazole Carbonic Anhydrase Inhibitor

Brubaker¹,

Mao

1999

J Histochem Cytochem.

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SUMMARYWe describe the synthesis of Bodipy 558/568-modified acetazolamide, a fluorescent inhibitor of carbonic anhydrase and its use to localize the enzyme in living cells. The modified acetazolamide, with its specific sulfonamide group intact, labeled cells at concentrations as low as 10 -9 M, with a minimal loading time of 5 min. The staining was decreased by 57.4% by preincubating cells with unaltered acetazolamide (1:100) or with trifluoromethane sulfonamide, 6-ethoxyzolamide, and 5-(3-hydroxybenzoyl)-thiophene-2-sulfonamide. The efficacy of the inhibitor was unchanged by the fluorescent label, as determined by an acridine orange assay that detects acidification of osteoclasts, the cell model used in this study. This compound should prove to be useful for studying carbonic anhydrase in many organisms because of the high degree of conservation of the active site of this enzyme. (J Histochem Cytochem 47:545-550, 1999)

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Evolution of the Carbonic Anhydrase Isozymes

Cited by 26 publications

References 30 publications

Purification, Molecular Properties and Ontogeny of Carbonic Anhydrase Isozymes. Evidence for A, B and C Isozymes in Avian and Mammalian Tissues

Purification, Molecular Properties and Ontogeny of Carbonic Anhydrase Isozymes. Evidence for A, B and C Isozymes in Avian and Mammalian Tissues

Positive Renal Response to Intravenous Acetazolamide in Patients with Carbonic Anhydrase II Deficiency

Localization of Carbonic Anhydrase in Living Osteoclasts with Bodipy 558/568-modified Acetazolamide, a Thiadiazole Carbonic Anhydrase Inhibitor

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