Immunoassay of carbonic anhydrase III in rat tissues

Carter, Nicholas; Jeffery, Stephen; Shiels, Alan

doi:10.1016/0014-5793(82)80866-1

Cited by 40 publications

(11 citation statements)

References 8 publications

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“…However, only one set of four abundant proteins with a mol wt of approximately 30,000 and narrowly varying isoelectric points was reproducibly decreased in the obese sample relative to the lean (Fig. 1A, [10][11][12][13][14][15]. A sample (350 M9 total protein) was applied to duplicate gels.…”

Section: Resultsmentioning

confidence: 99%

“…The presence of CA III in rodent white fat had been previously reported (10,11), but its presence there has received little attention. Our work demonstrates that CA III is a major component of white adipose tissue in mice (Fig.…”

Section: Discussionmentioning

confidence: 96%

“…In red muscle, which contains the highest level of CA III of any known tissue (10,15), it has been suggested that it serves as a source for protons involved in calcium release and reuptake by the sarcoplasmic reticulum (16). No direct experiments on the function of CA III in adipose tissue have been performed.…”

Section: Discussionmentioning

confidence: 98%

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Expression of CA III in Rodent Models of Obesity

Stanton¹,

Ponte²,

Coleman³

et al. 1991

Molecular Endocrinology

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To achieve a better understanding of the biochemical basis of obesity, we have undertaken comparative analyses of adipose tissue of lean and obese mice. By two-dimensional gel analysis, carbonic anhydrase-III (CA III) has been identified as a major constituent of murine adipose tissue. Quantitative comparisons of CA III protein and mRNA levels indicate that this enzyme is expressed at lower levels in adipose tissue from animals that were either genetically obese or had experimentally induced obesity compared to levels in the corresponding lean controls. This decrease in CA III expression was unique to adipose tissue, since other CA III-containing organs and tissues did not show a change when lean and obese animals were compared. Additionally, levels of CA III in adipose tissue from obese animals responded to acute changes in energy balance of the animal. These results are discussed in light of possible metabolic roles for CA III.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 96%

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Expression of CA III in Rodent Models of Obesity

Stanton¹,

Ponte²,

Coleman³

et al. 1991

Molecular Endocrinology

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“…Preparation of anti-CA II and anti-CA III serum Rabbit antisera to purified rat CA II and CA III were prepared as described previously (Carter et al 1981;Carter, Jeffery & Shiels, 1982) and stored at -70°C.…”

Section: Hypophysectomy Experimentsmentioning

confidence: 99%

Effects of hypophysectomy and growth hormone infusion on rat hepatic carbonic anhydrases

Jeffery¹,

Wilson²,

Mode³

et al. 1986

Journal of Endocrinology

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Rat liver exhibits a reversed sexual dimorphism of its two endogenous soluble carbonic anhydrase (CA) isozymes, CA II and CA III. Normal males have hepatic CA III concentrations ten-twenty times those in the female, while female liver contains two-three times more CA II than the male. Hypophysectomy abolishes this sexual differentiation, having no effect on male liver but producing isozyme concentrations in the female liver similar to those in the male. Infusion of a continuous level of GH into male rats induces a female-like isozyme pattern for both CA II and CA III.

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“…Both CAII and CAIII exhibit sexual dimorphism in rat liver, CAIII being present in male liver at concentrations 10-20 times those in females, whereas CAII shows a reverse pattern, being 1.5-3 times higher in female liver than in that of males. A preliminary study had suggested that, in rat skeletal muscle, there is no difference in CAIII concentrations between male and female (Carter et al, 1982). There is known to be a clear effect of age on CAIII concentrations in liver (Shiels et al, 1983), but there is no information on age and CAIII in muscle.…”

Section: Introductionmentioning

confidence: 99%

The effects of aging on carbonic anhydrase concentrations in rat liver and skeletal muscle

Jeffery

Merry²,

Holehan³

et al. 1988

Biochemical Journal

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The isoenzymes carbonic anhydrase II (CAII) and III (CAIII) have been measured by radioimmunoassay in the livers of male and female rats aged from 21 to 800 days. No sexual dimorphism at 21 days was found, but from 50 to 400 days both isoenzymes show sexual differences. From 600 days onwards, these differences are less apparent. CAIII concentrations in two 'fast' fibre muscles and one 'slow' fibre muscle have been determined. There is no sexual dimorphism in muscle, but a wide variation between individuals was observed. Fast muscles show maximal CAIII levels at 800 days, whereas in slow muscle the concentration of the isoenzyme is declining at this time.

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Immunoassay of carbonic anhydrase III in rat tissues

Cited by 40 publications

References 8 publications

Expression of CA III in Rodent Models of Obesity

Expression of CA III in Rodent Models of Obesity

Effects of hypophysectomy and growth hormone infusion on rat hepatic carbonic anhydrases

The effects of aging on carbonic anhydrase concentrations in rat liver and skeletal muscle

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