Membrane specific carbonic anhydrase (CAIV) expression in human tissues

Carter, N.D.; Fryer, Anthony A.; Grant, Anne G.; Hume, Robert; Strange, Robert; Wistrand, Per J.

doi:10.1016/0005-2736(90)90340-t

Cited by 41 publications

(35 citation statements)

References 10 publications

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“…Carbonic anhydrase IV (CA IV) was found in human normal tissues like kidney and lung, with the remarkable diversity in tissue distribution, subcellular location, and biological function (9,10). Several CAs are reportedly involved in NSCLC tumorigenesis, progression, regulation of cell proliferation, target therapy and prognosis, excepted CA IV.…”

Section: Introductionmentioning

confidence: 99%

Downregulation of carbonic anhydrase IV contributes to promotion of cell proliferation and is associated with poor prognosis in non-small cell lung cancer

Chen

Zhang

et al. 2017

Oncology Letters

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Section: Introductionmentioning

confidence: 99%

Downregulation of carbonic anhydrase IV contributes to promotion of cell proliferation and is associated with poor prognosis in non-small cell lung cancer

Chen

Zhang

et al. 2017

Oncology Letters

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“…Initially, this extracellular CA activity was assumed to be CA IV, which was at the time the only known CA isozyme associated with the extracellular surface and had been demonstrated on certain endothelial and epithelial membranes (9)(10)(11). Subsequently, other extracellular CAs were described (12), including CA IX, CA XII, and CA XIV, all of which are membrane CAs whose CA domain faces the extracellular space.…”

mentioning

confidence: 99%

Carbonic anhydrase IV and XIV knockout mice: Roles of the respective carbonic anhydrases in buffering the extracellular space in brain

Shah

Ulmasov

Waheed

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

115

118

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Previous studies have implicated extracellular carbonic anhydrases (CAs) in buffering the alkaline pH shifts that accompany neuronal activity in the rat and mouse hippocampus. CAs IV and XIV both have been proposed to mediate this extracellular buffering. To examine the relative importance of these two isozymes in this and other physiological functions attributed to extracellular CAs, we produced CA IV and CA XIV knockout (KO) mice by targeted mutagenesis and the doubly deficient CA IV͞XIV KO mice by intercrossing the individual null mice. Although CA IV and CA XIV null mice both are viable, the CA IV nulls are produced in smaller numbers than predicted, indicating either fetal or postnatal losses, which preferentially affect females. CA IV͞XIV double KO mice are also produced in fewer numbers than predicted and are smaller than WT mice, and many females die prematurely before and after weaning. Electrophysiological studies on hippocampal slices on these KO mice showed that either CA can mediate buffering after synaptic transmission in hippocampal slices in the absence of the other, but that eliminating both is nearly as effective as the CA inhibitor, benzolamide, in blocking the buffering seen in the WT mice. Thus, both CA IV and CA XIV contribute to extracellular buffering in the central nervous system, although CA IV appears to be more important in the hippocampus. These individual and double KO mice should be valuable tools in clarifying the relative contributions of each CA to other physiological functions where extracellular CAs have been implicated. interstitial pH ͉ mouse hippocampus ͉ targeted mutagenesis

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“…However, subsequent studies on CA IVs from nine mammalian species revealed that the CA IVs have wide variation in specific activity from 300 to 3000 enzyme units (EU)͞mg of protein (5)(6)(7)(8)(9). Murine and rat CA IVs were among the isozymes with lowest activity, while human, bovine, and rabbit CA IVs were at the high end of the activity spectrum.…”

mentioning

confidence: 99%

Gly-63 → Gln substitution adjacent to His-64 in rodent carbonic anhydrase IVs largely explains their reduced activity

Tamai

Waheed

Cody

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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Carbonic anhydrase (CA) IV is a glycosylphosphatidylinositol-anchored isozyme expressed on plasma membranes of capillary endothelial cells and certain epithelial cells of the nephron, the colon, and the genitourinary tract. CA IVs purified from bovine and rabbit lungs are high-activity enzymes, like human CA IV, while CA IV from mouse and rat lungs had only 10-20% as much catalytic activity. To explain the molecular basis for these differences in activity, we isolated and characterized the full-length cDNAs for bovine and rabbit CA IVs and compared their sequences to those we previously reported for human, murine, and rat CA IVs. These comparisons led us to postulate that a Gly-63 3 Gln substitution adjacent to His-64 in the rodent enzymes accounts for their lower activity. To test this hypothesis, we made the Gly-63 3 Gln mutants of bovine and rabbit CA IVs and the Gln-63 3 Gly mutant of murine CA IV by site-directed mutagenesis, and compared the activities of mutant and wild-type CA IVs expressed in COS-7 cells. In addition, we produced recombinant cDNAs expressing secretory forms of the Gly-63 and Gln-63 forms of each of the three enzymes and compared the activities of the enzymes purified from transfected COS-7 cell secretions with the activities of CA IVs purified from lungs. These studies demonstrated that Gly-63 is important for the high activity of bovine and rabbit CA IVs, and they showed that the low activity of murine CA IV could be improved by the Gln-63 3 Gly substitution. We suggest that the lower activity of the rodent CA IVs can be largely explained by the Gln-63 substitution which reduces the efficiency of proton transfer by the adjacent His-64.

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Membrane specific carbonic anhydrase (CAIV) expression in human tissues

Cited by 41 publications

References 10 publications

Downregulation of carbonic anhydrase IV contributes to promotion of cell proliferation and is associated with poor prognosis in non-small cell lung cancer

Downregulation of carbonic anhydrase IV contributes to promotion of cell proliferation and is associated with poor prognosis in non-small cell lung cancer

Carbonic anhydrase IV and XIV knockout mice: Roles of the respective carbonic anhydrases in buffering the extracellular space in brain

Gly-63 → Gln substitution adjacent to His-64 in rodent carbonic anhydrase IVs largely explains their reduced activity

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