Location of a membrane-bound carbonic anhydrase isoenzyme (CA IV) in the human male reproductive tract.

Parkkila, Seppo; Parkkila, Anna‐Kaisa; Kaunisto, Kari; Waheed, Abdül; Sly, W S; Rajaniemi, Hannu

doi:10.1177/41.5.8468457

Cited by 43 publications

(17 citation statements)

References 17 publications

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“…Antibodies against rat CA IV have been used to demonstrate surface localization of this enzyme in morphological investigations of various tissues (Brown et al, 1990;Parkkila et al, 1993Parkkila et al, , 1996Sender et al, 1994;Decker et al, 1996;Sender et al, 1998;Ekstedt et al, 2004;Fanjul et al, 2004). In similar studies of the CNS, however, the presence and localization of this enzyme has been less clear, as immunohistochemical findings have varied considerably.…”

Section: Discussionmentioning

confidence: 96%

Functional demonstration of surface carbonic anhydrase IV activity on rat astrocytes

Svichar

Esquenazi

Waheed

et al. 2005

Glia

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Buffering of the brain extracellular fluid is catalyzed by carbonic anhydrase (CA) activity. Whereas the extracellular isoform CA XIV has been localized exclusively to neurons in the brain, and to glial cells in the retina, there has been uncertainty regarding the form or forms of CA on the surface of brain astrocytes. We addressed this issue using physiological methods on cultured and acutely dissociated rat astrocytes. Prior work showed that the intracellular lactate-induced acidification (LIA) of astrocytes is diminished by benzolamide, a poorly permeant, nonspecific CA inhibitor. We demonstrate that pretreatment of astrocytes with phosphatidylinositol-specific phospholipase C (PI-PLC) results in a similar inhibition of the mean LIA (by 66 +/- 3%), suggesting that the glycosylphosphatidylinositol-anchored CA IV was responsible. Pretreatment of astrocytes with CA IV inhibitory antisera also markedly reduced the mean LIA in both cultured cortical (by 46 +/- 4%) and acutely dissociated hippocampal astrocytes (by 54 +/- 8%). Pre-immune sera had no effect. The inhibition produced by PIPLC or CA IV antisera was not significantly less than that by benzolamide, suggesting that the majority of detectable surface CA activity was attributable to CA IV. Thus, our data collectively document the presence of CAIV on the surface of brain astrocytes, and suggest that this is the predominant CA isoform on these cells.

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Section: Discussionmentioning

confidence: 96%

Functional demonstration of surface carbonic anhydrase IV activity on rat astrocytes

Svichar

Esquenazi

Waheed

et al. 2005

Glia

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“…CA IV, the first membrane isozyme described, is a glycosylphosphatidylinositol-anchored protein expressed on the apical surface of epithelial cells in colon (43), kidney (44), male genitourinary tract (45,46), and on the plasma face of endothelial cells of several capillary beds, including the pulmonary microvasculature (47). CA IV facilitates the reversible hydration of CO 2 at sites where CO 2 and HCO 3 Ϫ flux across membranes needs to be very rapid.…”

Section: Discussionmentioning

confidence: 99%

Human carbonic anhydrase XII: cDNA cloning, expression, and chromosomal localization of a carbonic anhydrase gene that is overexpressed in some renal cell cancers

Türeci

Şahin

Vollmar

et al. 1998

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

334

324

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We report the cloning and characterization of a tumor-associated carbonic anhydrase (CA) that was identified in a human renal cell carcinoma (RCC) by serological expression screening with autologous antibodies. The cDNA sequence predicts a 354-amino acid polypeptide with a molecular mass of 39,448 Da that has features of a type I membrane protein. The predicted sequence includes a 29-amino acid signal sequence, a 261-amino acid CA domain, an additional short extracellular segment, a 26-amino acid hydrophobic transmembrane domain, and a hydrophilic Cterminal cytoplasmic tail of 29 amino acids that contains two potential phosphorylation sites. The extracellular CA domain shows 30-42% homology with known human CAs, contains all three Zn-binding histidine residues found in active CAs, and contains two potential sites for asparagine glycosylation. When expressed in COS cells, the cDNA produced a 43-to 44-kDa protein in membranes that had around one-sixth the CA activity of membranes from COS cells transfected with the same vector expressing bovine CA IV. We have designated this human protein CA XII. Northern blot analysis of normal tissues demonstrated a 4.5-kb transcript only in kidney and intestine. However, in 10% of patients with RCC, the CA XII transcript was expressed at much higher levels in the RCC than in surrounding normal kidney tissue. The CA XII gene was mapped by using f luorescence in situ hybridization to 15q22. CA XII is the second catalytically active membrane CA reported to be overexpressed in certain cancers. Its relationship to oncogenesis and its potential as a clinically useful tumor marker clearly merit further investigation.

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“…arbonic anhydrase (CA) IV is a glycosylphosphatidylinositol-anchored membrane protein, which is highly expressed at the plasma membrane of epithelial cells of kidney (1)(2)(3) and endothelial cells of pulmonary and other microcapillary beds (4)(5)(6)(7)(8)(9). In the human eye, CA IV is highly expressed in the choriocapillaris but not in retina (10).…”

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confidence: 99%

Chemical chaperones protect from effects of apoptosis-inducing mutation in carbonic anhydrase IV identified in retinitis pigmentosa 17

Bonapace

Waheed

Shah

et al. 2004

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

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Carbonic anhydrase (CA) IV is a glycosylphosphotidylinositol-anchored enzyme highly expressed on the plasma face of microcapillaries and especially strongly expressed in the choriocapillaris of the human eye. In collaboration with scientists at the University of Cape Town (Rondebosch, South Africa), we recently showed that the R14W mutation in the signal sequence of CA IV, which they identified in patients with the retinitis pigmentosa ( protein-folding disease ͉ unfolded protein response ͉ endoplasmic reticulum-associated protein degradation ͉ signal sequence mutation

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Location of a membrane-bound carbonic anhydrase isoenzyme (CA IV) in the human male reproductive tract.

Cited by 43 publications

References 17 publications

Functional demonstration of surface carbonic anhydrase IV activity on rat astrocytes

Functional demonstration of surface carbonic anhydrase IV activity on rat astrocytes

Human carbonic anhydrase XII: cDNA cloning, expression, and chromosomal localization of a carbonic anhydrase gene that is overexpressed in some renal cell cancers

Chemical chaperones protect from effects of apoptosis-inducing mutation in carbonic anhydrase IV identified in retinitis pigmentosa 17

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