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

Jeffery, Stephen; Merry, B.J.; Holehan, Anne M.; Carter, N D

doi:10.1042/bj2500303

Cited by 10 publications

(7 citation statements)

References 20 publications

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“…Using MALDI-TOF mass spectrometer, 18 proteins were able to identify in this study. Among the identified proteins (Table 1), sex-dependent expression of ornithine aminotransferase, carbonic anhydrase 2 or regucalcin was in accordance with that obtained by other immunochemical or proteomic analysis: expression of ornithine aminotransferase is higher in females than males when analyzed by Western blotting of kidney homogenates from mice 20) ; contents of carbonic anhydrase 2 are higher in females than males when measured by radioimmunoassay of rat liver extracts 21) ; and regucalcin has been shown to be lower in females than males by proteomic analysis of nuclear proteins from the rat liver. 22) Thus, our proteomic analysis used in the present study is considered to be sufficiently applicable for clarifying difference in the expression of renal proteins between I/R-treated male and female rats.…”

Section: Discussionmentioning

confidence: 64%

Sex Difference in Ischemic Acute Renal Failure in Rats: Approach by Proteomic Analysis

Takayama

Takaoka

Sugino

et al. 2007

Biological & Pharmaceutical Bulletin

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We also have now investigated global protein expression in the kidney of experimental animals, using a proteomic technique consisting of two-dimensional gel electrophoresis and matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry. In the present study, we report the sex differences in renal proteins increased or decreased by I/R treatment. It is known that female rats are resistant to ischemic acute renal failure (ARF), compared with male rats. To elucidate sex differences in ischemic ARF, we searched global protein expression in post-ischemic kidneys using proteomic techniques. Ischemic ARF was induced by 45-min ischemia followed by reperfusion. By proteomic analysis, many male-or female-dominant proteins were detected in sham-operated rat kidneys, and significantly increased or decreased proteins were found in post-ischemic kidneys 2 h after reperfusion, at which there were no significant deterioration in renal function of both sexes. We detected 86 proteins showing more than 1.5-fold significant alterations (pϽ0.01) in both sexes by ischemia/reperfusion (I/R) treatment. Among the altered proteins, we identified a significantly up-regulated protein in male rat kidneys, meprin a a, a subunit of meprin which had been reported to play a role in the pathophysiology of I/R-induced ARF. In addition, it is known that a potent meprin a a inhibitor, actinonin, can protect against I/R-induced renal injury when administered to male rats. We therefore compared the effect of actinonin on I/R-induced renal dysfunction between male and female rats. Renal function of both males and females showed significant deterioration when measured at 24 h after the reperfusion, although the degree of renal dysfunction was much less in females than in males. Pre-ischemic treatment with actinonin (30 mg/kg, i.v.) prevented the I/R-induced renal dysfunction in males but not in females. Our results provide information on differences in protein expression at an early phase after the reperfusion between male and female rats. Moreover, the present study suggests that up-regulation of meprin a a in the post-ischemic kidney is at least partly involved in aggravation of I/R-induced renal injury in male rats. The possibility that meprin a a is a key component of the sex difference in ischemic ARF, warrants further attention. MATERIALS AND METHODS Animals and Experimental Design Male and female

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Section: Discussionmentioning

confidence: 64%

Sex Difference in Ischemic Acute Renal Failure in Rats: Approach by Proteomic Analysis

Takayama

Takaoka

Sugino

et al. 2007

Biological & Pharmaceutical Bulletin

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“…Expression of the CA III gene in skeletal muscle may also be influenced by neuronal activity, for increased quantities of the isoenzyme are found in fast-twitch rat muscles after denervation, although the same procedure has little effect on CA III in the slow-twitch soleus muscles (Carter et al, 1988), and by thyroid hormone, as thyroidectomy has been shown to increase the concentration of CA III in soleus, with no accompanying change in fibre type or distribution (Jeffery et al, 1987). Some variations also occur with age; CA III concentrations in soleus rise to a maximum at about 100 days, with no subsequent decline occurring until after 600 days, no difference in activity (or in variation of activity with age) being evident between the sexes (Jeffery et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

Acetazolamide-insensitive carbonic anhydrase activities in liver and tonic skeletal muscle of adult male rats with streptozotocin-induced diabetes mellitus

Moynihan

Ennis

1990

Biochemical Journal

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One of the four discrete isoenzymes of carbonic anhydrase hitherto characterized, CA III, has the lowest turnover rate and the greatest resistance to inhibition by sulphonamides. Streptozotocin-induced diabetes mellitus resulted in a reduction in acetazolamide-resistant activity of carbonic anhydrase in the liver, but not in tonic skeletal muscle, of adult male rats. The hepatic activity declined with apparent first-order kinetics [calculated rate constant (k) 0.089 day-1] to a minimum of approx. 6% of control values; the reduction in activity was moderated by administration of insulin.

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“…For example in humans, where all adult muscles are a mixture of type 1 and type 2 fibres, CAIII protein is dectectable in fetal muscle at 10 weeks gestation, but remains in low amount until about 25 weeks gestation, when there is a steep rise to give 50 % of the adult value at birth (Jeffery et al, 1980;Lloyd et al, 1986). Similarly in the rat soleus, the amount of CAIII 3 weeks after birth is about 25 % of the adult value, and rises rapidly to the adult value during the next 10 weeks (Jeffery et al, 1988). Thus in both species the major increase in CAIII amount occurs at a stage in development when fetal polyneuronal innervation has regressed and the specific fibre/nerve impulse patterns are being established.…”

Section: Introductionmentioning

confidence: 99%

Induction of carbonic anhydrase III mRNA and protein by denervation of rat muscle

Carter

Wistrand

Isenberg³

et al. 1988

Biochemical Journal

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Carbonic anhydrase III (CAIII) protein and mRNA amounts in fast- and slow-twitch rat muscles were examined after resection of the sciatic nerve. Striking changes occur in the fast-twitch anterior tibialis (AT) and extensor digitorum longus (EDL) muscles, where CAIII protein and mRNA are increased several-fold 16 days after denervation. The data suggest that these changes are regulated in part by changes in gene transcription and that they perhaps signal a fast-to-slow fibre type transition in these denervated muscles. AT and EDL show some differences in the effects of denervation, which are suggestive of variation in the timing of denervation-induced responses and/or the CAIII protein/mRNA turnover rates in the two muscles.

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

Cited by 10 publications

References 20 publications

Sex Difference in Ischemic Acute Renal Failure in Rats: Approach by Proteomic Analysis

Sex Difference in Ischemic Acute Renal Failure in Rats: Approach by Proteomic Analysis

Acetazolamide-insensitive carbonic anhydrase activities in liver and tonic skeletal muscle of adult male rats with streptozotocin-induced diabetes mellitus

Induction of carbonic anhydrase III mRNA and protein by denervation of rat muscle

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