Cellular and subcellular localization of enzymes of arginine metabolism in rat kidney

Dhanakoti, Srinivas; Brosnan, Margaret E.; Herzberg, Gene R.; Brosnan, John T.

doi:10.1042/bj2820369

Cited by 65 publications

(37 citation statements)

References 40 publications

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“…Virtually all flux of plasma citrulline is associated with endogenous synthesis of arginine in adult humans [62] and rats [20], but apparently not in adult dogs [60]. Endogenous synthesis of arginine from citrulline is not responsive to reduced dietary intake of arginine in adult rats [59] or humans [54].…”

Section: Arginine Synthesismentioning

confidence: 99%

“…Data for exogenous supply of arginine to the circulation and endogenous synthesis of arginine from citrulline were calculated on the basis of arginine intake (91 µmol/h per kg body wt.) [59] and on the fact that only 60 % of intestinal luminal arginine is absorbed intact into the portal circulation in the adult rat [191]. Endogenous flux of arginine was calculated on the basis of whole-body protein degradation (8.1 g/day) in the adult rat (394 g) [58] and arginine concentration in the rat (73 mg/g of protein) [57].…”

Section: Arginine Synthesismentioning

confidence: 99%

“…Approximately 60 % of net arginine synthesis in adult mammals occurs in the kidney [50,60], where citrulline is extracted from the blood and converted stoichiometrically into arginine by the action of ASS and ASL (Figure 2), which are localized within the proximal convoluted tubules [81,[112][113][114][115]. A tight correlation between renal citrulline uptake and renal arginine output has been elegantly demonstrated for both humans and rats [50,116].…”

Section: Renal Arginine Synthesismentioning

confidence: 99%

“…As noted in the preceding section, the renal capacity for arginine synthesis develops in late fetal stages and continues to increase after birth [81], complementing the developmental shift from release of arginine to release of citrulline by the small intestine. The kidney also expresses arginase, but expression of arginase and the arginine biosynthetic enzymes is highly segregated within different parts of the nephron, so that there is little or no coexpression of these opposing enzymic pathways within the same cell [113,119].…”

Section: Renal Arginine Synthesismentioning

confidence: 99%

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Arginine metabolism: nitric oxide and beyond

Morris

1998

Biochemical Journal

2,430

2,036

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Arginine is one of the most versatile amino acids in animal cells, serving as a precursor for the synthesis not only of proteins but also of nitric oxide, urea, polyamines, proline, glutamate, creatine and agmatine. Of the enzymes that catalyse rate-controlling steps in arginine synthesis and catabolism, argininosuccinate synthase, the two arginase isoenzymes, the three nitric oxide synthase isoenzymes and arginine decarboxylase have been recognized in recent years as key factors in regulating newly identified aspects of arginine metabolism. In particular, changes in the activities of argininosuccinate synthase, the arginases, the inducible isoenzyme of nitric oxide synthase and also cationic amino acid transporters play major roles in determining the metabolic fates of arginine in health and disease, and recent studies have identified

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Section: Arginine Synthesismentioning

confidence: 99%

Section: Arginine Synthesismentioning

confidence: 99%

Section: Renal Arginine Synthesismentioning

confidence: 99%

Section: Renal Arginine Synthesismentioning

confidence: 99%

See 2 more Smart Citations

Arginine metabolism: nitric oxide and beyond

Morris

1998

Biochemical Journal

2,430

2,036

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“…Whether the reduced in vivo activity of the eNOS reaction, which these data suggest, is due primarily to a change in the level and regulation of eNOS (8,31,32) and/or to changes in the metabolism and tissue availability of arginine (13,(33)(34)(35) cannot be determined from this study. The differences in the relative utilization of plasma arginine for NO synthesis between acute and convalescent PPHN, coupled with the intake differences mentioned above, make it relevant to recall that there is extensive compartmentation of arginine metabolism in vivo, at the intracellular, intraorgan, and interorgan levels (36)(37)(38)(39)(40), and although plasma arginine is made available during a complete turn of the urea cycle (Fig. 3), vascular endothelial cells, when stimulated, can exhibit a "direct" metabolic pathway whereby the citrulline produced by the action of the eNOS is directly converted to arginine thanks to the action of the argininosuccinate synthase and argininosuccinate lyase.…”

Section: Discussionmentioning

confidence: 99%

Whole Body Arginine Metabolism and Nitric Oxide Synthesis in Newborns with Persistent Pulmonary Hypertension

Castillo

deRojas-Walker

et al. 1995

Pediatr Res

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R A C TDespite the potential relevance of the L-arginine-nitric oxide (NO) pathway in the pathophysiology of pulmonary hypertension, no in vivo studies of the kinetics of arginine and NO have been conducted previously in this population. The terminal guanidino N-atom of L-arginine is the precursor for NO, which is oxidized to the stable inorganic nitrogen oxides, nitrite (NO,-) and nitrate (NO,-). Thus, synthesized NO is detected in serum or urine as NO,-and NO,-. The purpose of this investigation was to compare studies of whole body arginine metabolism twice in nine patients with persistent pulmonary hypertension of the newborn (PPHN), using a primed constant i.v. infusion of ~-[~uanidino-~~N,,5,5~H,]ar~inine and L- [5,5,52~,]leucine, first during acute pulmonary vasoconstriction and again during convalescence, and thereby to characterize quantitative aspects of whole body arginine kinetics and NO production, as estimated from the rate of transfer of the '5~-guanidino-label of arginine to urinary nitrate (ISNO,-). Arginine flux rates were 84.1 ? 8.6 p r n~l -k~. -~h -~ (mean ? SEM) during acute pulmonary hypertension and increased to 125 ? 13.2 ( p < 0.05) during conva-PPHN is an acute vascular maladaptation to extrauterine life, characterized by reactive pulmonary vasoconstriction, causing extrapulmonary shunting of blood across fetal channels and critical hypoxemia. Remodeling of the pulmonary arteries has been observed in some patients with PPHN (1). The etiology of this disorder is uncertain, but a role for altered NO production, a recently discovered key regulator of vascular tone (2-4), Received October 10, 1994; accepted February 27, 1995 Abbreviations PPHN, persistent pulmonary hypertension of the newborn NO, nitric oxide eNOS, nitric oxide synthase AaDO,, alveolo-arterial oxygen gradient ECMO, extracorporeal membrane oxygenation A.P.E., atom percent excess must be considered. NO is produced in the pulmonary and systemic arteries of newborn animals (5) and contributes to the postnatal vasodilation of the pulmonary circulation (6, 7). NO is synthesized in the endothelial cells, through the action of eNOS, and diffuses into subjacent vascular smooth muscle, where it binds to its molecular target, the prosthetic heme group of soluble guanylyl cyclase, forming nitrosyl proteins (8). This process activates guanylyl cyclase, augmenting levels of the second messenger, cGMP (8). Intracellular elevation of cGMP levels activates cGMP-dependent protein kinases, leading to phosphorylation of proteins and inhibition of intracellu-MA 02114. lar calcium release and/or influx through calcium channels.

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Differential expression of cytosolic proteins in the rat kidney cortex and medulla: Preliminary proteomics

Witzmann¹,

Fultz²,

Grant³

et al. 1998

Electrophoresis

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The rodent kidney is a target of many xenobiotics and is typified by regionally specific structure and function. This renders distinct regions of the kidney differentially susceptible to toxic exposure and effect. To characterize these differences at the proteome level, protein patterns from male rat kidney cortex and medulla cytosols were examined by two-dimensional electrophoresis (2-DE) and image analysis and prominent proteins identified immunologically or by matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-MS) and electrospray/ionization-tandem mass spectrometry (ESI-MS/MS) sequence tag identification. An average of 727 protein spots were resolved and matched to the cortex cytosol reference pattern, and 716 in the medulla. Of this total, 127 proteins were found to differ in abundance (86 higher in cortex; 41 higher in medulla) (P < 0.001). Of those proteins that were detectable in both cortex and medulla, the abundance of 97 differed significantly while 30 proteins were found to be unique to one region or the other (26 in cortex, 4 in medulla). Twenty protein spots were identified and their regional differences are discussed. These results both confirm and expand our understanding of the molecular heterogeneity characterizing structurally and functionally distinct regions of the kidney and serve as a useful foundation for future nephrotoxicologic studies.

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Cellular and subcellular localization of enzymes of arginine metabolism in rat kidney

Cited by 65 publications

References 40 publications

Arginine metabolism: nitric oxide and beyond

Arginine metabolism: nitric oxide and beyond

Whole Body Arginine Metabolism and Nitric Oxide Synthesis in Newborns with Persistent Pulmonary Hypertension

Differential expression of cytosolic proteins in the rat kidney cortex and medulla: Preliminary proteomics

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