Plasma membrane-bound carbonic anhydrase activity in the regenerating rat liver

Marin, J. J. G.; Urbieta, Arancha Tabernero; Barriocanal, Fernando Pérez; Barbero, Emilio Rodríguez; Eleno, Nélida

doi:10.1016/0005-2736(91)90262-7

Cited by 7 publications

(2 citation statements)

References 22 publications

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“…The plasma membrane-associated CA activity in hepatocytes was originally demonstrated by Garcia-Marín et al [21] using a biochemical method and by Ono et al [22] using a histochemical cobalt precipitation technique. At the same time, information on different ion transport proteins in hepatocyte plasma membrane accumulated that linked the plasma membrane-bound CA activity to ion transport mechanisms.…”

Section: Discussionmentioning

confidence: 99%

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The plasma membrane carbonic anhydrase in murine hepatocytes identified as isozyme XIV

et al. 2002

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Background: Biochemical and histochemical studies have both previously indicated plasma membrane-associated carbonic anhydrase (CA) activity in hepatocytes which has been assumed to be CA IV. However, immunohistochemical data did not support this assignment. Recent northern blotting results indicated the presence of mRNA for the most recently discovered membranebound CA isozyme, CA XIV, in the liver. The present study was designed to examine whether CA XIV could contribute to the CA activity described in the hepatocytes.

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Section: Discussionmentioning

confidence: 99%

“…Garcia-Marin et al [21] observed that membrane-bound CA activity correlates with hepatic regeneration following partial hepatectomy. They measured CA activity in both soluble and plasma membrane-enriched fractions obtained from liver homogenate from rats undergoing hepatectomy.…”

Section: Discussionmentioning

confidence: 99%

The plasma membrane carbonic anhydrase in murine hepatocytes identified as isozyme XIV

et al. 2002

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Bile acid-induced modifications in DNA synthesis by the regenerating perfused rat liver

et al. 1993

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Liver cell proliferation is a complex process that can be affected by a large number of factors such as bile acids, which have been reported to be associated to the pathogenesis of liver cancer. In this work, bile acid-induced modifications in DNA synthesis by regenerating perfused rat liver were investigated. Two-thirds hepatectomy was carried out 24 hr before perfusion of liver with recirculating, erythrocyte-free Krebs-Henseleit solution. The viability of the preparations was maintained under all experimental conditions, as indicated by bile flow, oxygen uptake, perfusion pressure, perfusion flow and release of lactate dehydrogenase and potassium into the perfusate. Livers received (min 10 to min 60) bile acid infusion at a rate of 25 nmol/min/gm liver (i.e., maximal secretion rate/2) in regenerating livers as calculated for taurocholate in separate experiments). Trace amounts of [methyl-14C]thymidine were added to the perfusate at min 30. At the end of the experiments (min 60) the livers were washed, removed, weighed and homogenized to determine radioactivity in whole tissue, in DNA and in non-DNA-related fractions. Taurocholate and, to a lesser extent, taurodeoxycholate and dehydrocholate (but not ursodeoxycholate) were found to reduce 14C incorporation into DNA. This was not due to changes in the content of 14C in whole, regenerating liver tissue. Taurocholate, taurodeoxycholate, dehydrocholate and ursodeoxycholate had no effect on thymidine uptake; moreover, the proportion of 14C found in bile was negligible. However, bile acid-induced modification in the fate of intracellular thymidine was observed. In regenerating livers receiving no bile acid, the 14C carried by thymidine metabolites accounted for about 60% of 14C in whole liver tissue. Taurocholate markedly increased this proportion to about 80%. Reverse-phase high-pressure liquid chromatography revealed that most of this 14C (about 80%) was recovered at the elution time, corresponding to thymidine catabolites rather than to DNA precursors. These results suggest that bile acids induce enhancement of thymidine catabolism that reduces its incorporation into DNA; inhibition in the process of DNA synthesis itself, leading to a subsequent increase in the metabolism of DNA precursors; or both. Moreover, from the diversity in this property for bile acid species it might be inferred that changes in the composition and size of the bile acid pool during liver carcinogenesis or regeneration play a role in the modulation of the proliferative process.

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Membrane Associated Carbonic Anhydrase IV (CA IV): A Personal and Historical Perspective

Waheed

Sly

2013

Subcellular Biochemistry

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Carbonic anhydrase IV is one of 12 active human isozymes and one of four expressed on the extracellular surfaces of certain endothelial and epithelial cells. It is unique in being attached to the plasma membrane by a glycosyl-phosphatiydyl-inositol (GPI) anchor rather than by a membrane-spanning domain. It is also uniquely resistant to high concentrations of sodium dodecyl sulfate (SDS), which allows purification from tissues by inhibitor affinity chromatography without contamination by other isozymes. This unique resistance to SDS and recovery following denaturation is explained by the two disulfide bonds. The 35-kDa human CA IV is a "high activity" isozyme in CO2 hydration activity, like CA II, and has higher activity than other isozymes in catalyzing the dehydration of HCO3 (-). Human CA IV is also unique in that it contains no oligosaccharide chains, where all other mammalian CA IVs are glycoproteins with one to several oligosaccharide side chains.Although CA IV has been shown to be active in mediating CO2 and HCO3 (-) transport in many important tissues like kidney and lung, and in isolated cells from brain and muscle, the gene for CA IV appears not to be essential. The CA IV knockout mouse produced by targeted mutagenesis, though slightly smaller and produced in lower than expected numbers, is viable and has no obvious mutant phenotype. Conversely, several dominant negative mutations in humans are associated with one form of reitinitis pigmentosa (RP-17), which we attribute to unfolded protein accumulation in the choreocapillaris, leading to apoptosis of cells in the overlying retina.

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Plasma membrane-bound carbonic anhydrase activity in the regenerating rat liver

Cited by 7 publications

References 22 publications

The plasma membrane carbonic anhydrase in murine hepatocytes identified as isozyme XIV

The plasma membrane carbonic anhydrase in murine hepatocytes identified as isozyme XIV

Bile acid-induced modifications in DNA synthesis by the regenerating perfused rat liver

Membrane Associated Carbonic Anhydrase IV (CA IV): A Personal and Historical Perspective

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