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Oxygen-18 isotope of breath CO? linking to erythrocytes carbonic anhydrase activity: a biomarker for pre-diabetes and type 2 diabetes.

ABSTRACT: Carbonic anhydrase (CA), a well-characterized metalloenzyme, is associated with oxygen-18 ( (18)O)-isotopic fractionations of CO?. To investigate how CA activity links the (18)O of breath CO? to pre-diabetes (PD) and type 2 diabetes (T2D) during metabolism, we studied pre- and post-dose CA activities in erythrocytes with simultaneous monitoring of (18)O/ (16)O-isotope ratios of breath CO? and thereafter elucidated potential metabolic pathways underlying CA alteration in the pathogenesis of T2D. Here we show that the post-dose CA activity in both T2D and PD was markedly enhanced, whereas the non-diabetic controls (NDC) exhibited a considerable reduction in post-dose CA activity when compared with their basal CA activities. However, T2D and PD exhibited isotopic enrichments of (18)O in breath CO?, while a marked depletion of (18)O in CO? was manifested in NDC. Thus, the isotopic enrichments and depletions of (18)O in breath CO? were well correlated with the changes in CA activities for controls, PD and T2D. Our findings suggest the changes in CA activities in erythrocytes may contribute to the pathogenesis of T2D and the breath C (18)O (16)O regulated by the CA activity as a potential biomarker for non-invasive assessment of T2D, and thus may open a new method for treating T2D.

SUBMITTER: Ghosh C

PROVIDER: S-EPMC4311236 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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Oxygen-18 isotope of breath CO₂ linking to erythrocytes carbonic anhydrase activity: a biomarker for pre-diabetes and type 2 diabetes.

Ghosh Chiranjit C Banik Gourab D GD Maity Abhijit A Som Suman S Chakraborty Arpita A Selvan Chitra C Ghosh Shibendu S Chowdhury Subhankar S Pradhan Manik M

Scientific reports 20150130

Carbonic anhydrase (CA), a well-characterized metalloenzyme, is associated with oxygen-18 ( (18)O)-isotopic fractionations of CO₂. To investigate how CA activity links the (18)O of breath CO₂ to pre-diabetes (PD) and type 2 diabetes (T2D) during metabolism, we studied pre- and post-dose CA activities in erythrocytes with simultaneous monitoring of (18)O/ (16)O-isotope ratios of breath CO₂ and thereafter elucidated potential metabolic pathways underlying CA alteration in the pathogenesis of T2D. ...[more]

PMID: 25633556

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Project description:1. Three forms of the zinc-containing enzyme carbonic anhydrase (EC 4.2.1.1) were isolated from the erythrocytes of the rat and two forms from the dorsolateral prostate of the rat. Several additional minor components were observed but not isolated. Separation of the isoenzymes was achieved by ion-exchange chromatography, polyacrylamide-gel electrophoresis and isoelectric focusing. 2. The general properties of the isolated isoenzymes, their molecular weights and their contents of zinc were closely similar. As catalysts of the hydration of carbon dioxide, however, they were distinctly different. The two most abundant isoenzymes of the erythrocytes, which were found in equal proportions, differed 70-fold in specific activity, whereas the isoenzymes of the dorsolateral prostate were similar to one another and resembled the high-activity component of the erythrocytes. The inhibition of the latter by acetazolamide (5-acetamido-1-thia-3,4-diazole-2-sulphonamide) was mainly competitive, whereas in identical conditions the low-activity erythrocyte component and the dorsolateral prostate isoenzymes were non-competitively inhibited. 3. The use of chloroform-ethanol to remove haemoglobin from the rat haemolysate was found (a) to bring about changes in the kinetic properties of the soluble isoenzymes and (b) to cause the appearance of an additional isoenzyme. 4. The actions were compared of the inhibitors acetazolamide, 1,1-dimethylaminonaphthalene-5-sulphonamide and ethoxzolamide (6-ethoxybenzothiazole-2-sulphonamide) on the hydrolysis of p-nitrophenyl acetate catalysed by the isoenzymes. 5. The low-activity erythrocyte isoenzyme was an efficient catalyst of the hydrolysis of beta-naphthyl acetate whereas the high-activity forms were much less active towards this ester. Neither of the isoenzymes present in the dorsolateral prostate catalysed this reaction. 6. Carbonic anhydrase in the rat dorsolateral prostate accounts for no more than 5% of the unusually high content of zinc in this organ.

Dataset Information

Oxygen-18 isotope of breath CO? linking to erythrocytes carbonic anhydrase activity: a biomarker for pre-diabetes and type 2 diabetes.

Publications

Oxygen-18 isotope of breath CO₂ linking to erythrocytes carbonic anhydrase activity: a biomarker for pre-diabetes and type 2 diabetes.

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