Expression of the Genes of Arginine-Synthesizing Enzymes in the Rat Kidney during Development

Goutal, I.; Fairand, Alain; Husson, Annie

doi:10.1159/000014166

Cited by 12 publications

(11 citation statements)

References 32 publications

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“… Tissue distribution of ASS mRNA during adult and fetal periods in rats. Total RNA (25 µg per lane) was prepared from various tissues of adult (A) and 19.5‐day‐old fetuses (B) rats, and analysed by Northern blot (see [110] for experimental protocol). Hybridizations were performed successively with the ASS cDNA and the 18S rRNA probe as an internal standard.…”

Section: Ass a Ubiquitous Enzymementioning

confidence: 99%

“…Levels of mRNA (open circles) and enzyme activity (black circles) are shown. Data are from [60,110]. Adult values were taken as reference (100%); ASS activity in adult was 110.9 ± 11.7 U·g −1 liver, n = 7.…”

Section: Ass a Key Step In Urea Productionmentioning

confidence: 99%

“…In contrast to liver however, the factors modulating ASS gene expression are not known both in enterocytes and kidney cells. Indeed, glucocorticoids neither affected ASS activity in porcine enterocytes [111] nor modulated the ASS mRNA level in kidneys of both newborn [110] and adult rats [112]. Finally, protein deprivation did not change renal ASS activity [113], although an increase in mRNA level was reported [112].…”

Section: Ass a Key Step In Arginine Productionmentioning

confidence: 99%

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Argininosuccinate synthetase from the urea cycle to the citrulline–NO cycle

Husson¹,

Brasse‐Lagnel²,

Fairand³

et al. 2003

European Journal of Biochemistry

276

239

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Argininosuccinate synthetase (ASS, EC 6.3.4.5) catalyses the condensation of citrulline and aspartate to form argininosuccinate, the immediate precursor of arginine. First identified in the liver as the limiting enzyme of the urea cycle, ASS is now recognized as a ubiquitous enzyme in mammalian tissues. Indeed, discovery of the citrulline–NO cycle has increased interest in this enzyme that was found to represent a potential limiting step in NO synthesis. Depending on arginine utilization, location and regulation of ASS are quite different. In the liver, where arginine is hydrolyzed to form urea and ornithine, the ASS gene is highly expressed, and hormones and nutrients constitute the major regulating factors: (a) glucocorticoids, glucagon and insulin, particularly, control the expression of this gene both during development and adult life; (b) dietary protein intake stimulates ASS gene expression, with a particular efficiency of specific amino acids like glutamine. In contrast, in NO‐producing cells, where arginine is the direct substrate in the NO synthesis, ASS gene is expressed at a low level and in this way, proinflammatory signals constitute the main factors of regulation of the gene expression. In most cases, regulation of ASS gene expression is exerted at a transcriptional level, but molecular mechanisms are still poorly understood.

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Section: Ass a Ubiquitous Enzymementioning

confidence: 99%

Section: Ass a Key Step In Urea Productionmentioning

confidence: 99%

Section: Ass a Key Step In Arginine Productionmentioning

confidence: 99%

See 1 more Smart Citation

Argininosuccinate synthetase from the urea cycle to the citrulline–NO cycle

Husson¹,

Brasse‐Lagnel²,

Fairand³

et al. 2003

European Journal of Biochemistry

276

239

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“…l-Cit is endogenously synthesized from l-glutamine in the intestines and released to the venous blood, 20 filtered in the glomeruli, and subsequently taken up by the proximal tubule. Proximal tubular cells express both argininosuccinate synthase and argininosuccinate lyase 27,28 and can, therefore, convert l-Cit to lArg. 21 The intestinal-renal axis of de novo synthesis of l-Arg from l-glutamine has been demonstrated using radiolabeled l-glutamine.…”

Section: Discussionmentioning

confidence: 99%

l -Citrulline, But Not l -Arginine, Prevents Diabetes Mellitus–Induced Glomerular Hyperfiltration and Proteinuria in Rat

et al. 2014

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Diabetes mellitus–induced oxidative stress causes increased renal oxygen consumption and intrarenal tissue hypoxia. Nitric oxide is an important determinant of renal oxygen consumption and electrolyte transport efficiency. The present study investigates whether l-arginine or l-citrulline to promote nitric oxide production prevents the diabetes mellitus–induced kidney dysfunction. Glomerular filtration rate, renal blood flow, in vivo oxygen consumption, tissue oxygen tension, and proteinuria were investigated in control and streptozotocin-diabetic rats with and without chronic l-arginine or l-citrulline treatment for 3 weeks. Untreated and l-arginine–treated diabetic rats displayed increased glomerular filtration rate (2600±162 versus 1599±127 and 2290±171 versus 1739±138 μL/min per kidney), whereas l-citrulline prevented the increase (1227±126 versus 1375±88 μL/min per kidney). Filtration fraction was increased in untreated diabetic rats because of the increase in glomerular filtration rate but not in l-arginine– or l-citrulline–treated diabetic rats. Urinary protein excretion was increased in untreated and l-arginine–treated diabetic rats (142±25 versus 75±7 and 128±7 versus 89±7 μg/min per kidney) but not in diabetic rats administered l-citrulline (67±7 versus 61±5 μg/min per kidney). The diabetes mellitus–induced tissue hypoxia, because of elevated oxygen consumption, was unaltered by any of the treatments. l-citrulline administered to diabetic rats increases plasma l-arginine concentration, which prevents the diabetes mellitus–induced glomerular hyperfiltration, filtration fraction, and proteinuria, possibly by a vascular effect.

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“…Furthermore, the expression of ASS and ASL genes based on the measurement of their transcripts, proteins, and enzyme activities has been reported during development of rat [6,7] and mouse [8] kidneys as well as in adult rat [9][10][11] and mouse [12] kidneys. Physiological studies clearly demonstrated the renal synthesis of L-arginine by quantitating arterial and renal venous concentrations of L-citrulline and L-arginine.…”

Section: Introductionmentioning

confidence: 99%

l-Arginine metabolism in dog kidney and isolated nephron segments

Levillain¹,

Rabier²,

Duclos³

et al. 2008

Metabolism

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The renal basic amino acid metabolism often differs in rodents, strict carnivore, and omnivore species. Given the pivotal role of L-arginine and L-ornithine in several metabolic pathways and the fact that the dog is closely related to humain being also an omnivore, we tested whether L-arginine metabolism and L-ornithine catabolism take place in the dog kidney. We examined the metabolic of L-arginine in dog cortical tubules to integrate local L-arginine metabolism into a general physiological and metabolic framework. To achieve these goals, we first ascertained the protein expression of relevant enzymes identified by Western blotting. Larginine catabolism was studied in suspensions of canine cortical proximal tubules, medullary thick ascending limbs, and papillary collecting ducts either incubated without exogenous Larginine being added (small endogenous quantities) or incubated with L-arginine being added in supraphysiological amounts (2 mmol/L with or without the presence of alternative metabolic substrates, 2 mmol/L L-glutamine, or lactate). The results revealed that dog kidneys consumed L-citrulline and released L-arginine and L-ornithine. Argininosuccinate synthetase and lyase, arginase II, and ornithine aminotransferase were detected in the renal cortex. Arginase II activity was found in a suspension of proximal tubules by measuring the amounts of urea and L-ornithine produced. A fraction of this L-ornithine was further partially metabolized through the intramitochondrial ornithine aminotransferase pathway, leading to changes in L-glutamate, glucose, L-alanine, and ammonia metabolism without L-proline accumulation. Medullary thick ascending limbs expressed a very low arginase activity whereas papillary collecting ducts did not. In conclusion, the dog kidney produces L-arginine. Part of this L-arginine is further catabolized by arginase II, suggesting that its physiological role was to produce L-ornithine for the body.-3 -

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Expression of the Genes of Arginine-Synthesizing Enzymes in the Rat Kidney during Development

Cited by 12 publications

References 32 publications

Argininosuccinate synthetase from the urea cycle to the citrulline–NO cycle

Argininosuccinate synthetase from the urea cycle to the citrulline–NO cycle

l -Citrulline, But Not l -Arginine, Prevents Diabetes Mellitus–Induced Glomerular Hyperfiltration and Proteinuria in Rat

l-Arginine metabolism in dog kidney and isolated nephron segments

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