Regulation of arginase levels by urea and intermediates of the Krebs‐Henseleit cycle in <i>Saccharomyces cerevisiae</i>

Chan, Patrick Y.; Cossins, Edwin A.

doi:10.1016/0014-5793(72)80074-7

Cited by 6 publications

(6 citation statements)

References 19 publications

(2 reference statements)

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“…As mentioned above, in the urea cycle arginine is converted by arginase, a manganese metalloenzyme, in ornithine and urea; this cycle is crucial not only for allowing urea excretion, but also for producing bicarbonate, which is critical for maintaining acid/base homeostasis [ 59 , 60 , 61 , 62 , 63 ]. Arginase exists in two distinct isoforms, arginase I and II, that share ~60% sequence homology; arginase I is a cytosolic enzyme mainly localized in the liver, whereas arginase II is a mitochondrial enzyme with a wide distribution and is expressed in the kidney, prostate, gastrointestinal tract, and the vasculature [ 64 , 65 , 66 , 67 ].…”

Section: Pleiotropic Effects Of Argininementioning

confidence: 99%

Arginine and Endothelial Function

et al. 2020

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Arginine (L-arginine), is an amino acid involved in a number of biological processes, including the biosynthesis of proteins, host immune response, urea cycle, and nitric oxide production. In this systematic review, we focus on the functional role of arginine in the regulation of endothelial function and vascular tone. Both clinical and preclinical studies are examined, analyzing the effects of arginine supplementation in hypertension, ischemic heart disease, aging, peripheral artery disease, and diabetes mellitus.

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Section: Pleiotropic Effects Of Argininementioning

confidence: 99%

Arginine and Endothelial Function

et al. 2020

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“…However, the effects of changes in the SLC14A1 protein level on the NOS pathway are unknown. The nitric oxide synthase pathway might be involved in the SLC14A1 regulation [51,52], but under our experimental conditions, no mRNA expression of arginase 1 (enzyme of the urea cycle) or eNOS1 (enzyme of NO pathway) was detectable by qPCR in our experiments.…”

Section: Discussionmentioning

confidence: 64%

Decreased Expression of the Human Urea Transporter SLC14A1 in Bone is Induced by Cytokines and Stimulates Adipogenesis of Mesenchymal Progenitor Cells

Komrakova

Blaschke

Ponce

et al. 2020

Exp Clin Endocrinol Diabetes

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The human urea transporter SLC14A1 (HUT11/UT-B) has been suggested as a marker for the adipogenic differentiation of bone cells with a relevance for bone diseases. We investigated the function of SLC14A1 in different cells models from bone environment. SLC14A1 expression and cytokine production was investigated in bone cells obtained from patients with osteoporosis. Gene and protein expression of SLC14A1 was studied during adipogenic or osteogenic differentiation of human mesenchymal progenitor cells (hMSCs) and of the single-cell–derived hMSC line (SCP-1), as well as in osteoclasts and chondrocytes. Localization was determined by histochemical methods and functionality by urea transport experiments. Expression of SLC14A1 mRNA was lower in cells from patients with osteoporosis that produced high levels of cytokines. Accordingly, when adding a combination of cytokines to SCP-1 SLC14A1 mRNA expression decreased. SLC14A1 mRNA expression decreased after both osteogenic and more pronounced adipogenic stimulation of hMSCs and SCP-1 cells. The highest SLC14A1 expression was determined in undifferentiated cells, lowest in chondrocytes and osteoclasts. Downregulation of SLC14A1 by siRNA resulted in an increased expression of interleukin-6 and interleukin-1 beta as well as adipogenic markers. Urea influx through SLC14A1 increased expression of osteogenic markers, adipogenic markers were suppressed. SLC14A1 protein was localized in the cell membrane and the cytoplasm. Summarizing, the SLC14A1 urea transporter affects early differentiation of hMSCs by diminishing osteogenesis or by favoring adipogenesis, depending on its expression level. Therefore, SLC14A1 is not unequivocally an adipogenic marker in bone. Our findings suggest an involvement of SLC14A1 in bone metabolism and inflammatory processes and disease-dependent influences on its expression.

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“…transferred from agar slants to a basal medium which had been supplemented with L-methionine (2.5,umol/ ml). The basal medium (Combepine et al, 1971;Chan & Cossins, 1972) contained (per 100ml): 50,ug of thiamin, 5mg of inositol, 500,ug each of calcium pantothenate and nicotinic acid, 2,ug of biotin, 85mg of KCI, 1.5mg of MgSO4,7H20, 500,ug each of FeCl3,6H20 and MnSO4,H20,25mg of CaCl2,2H20,110mg of KH2PO4,200mg of (NH4)2HP04, 10g of glucose, 40mg each of DL-leucine, DL-valine, Lcysteine, DL-phenylalanine, DL-threonine, DL-alanine, L-aspartic acid, L-lysine-HCl and DL-serine, 50mg of L-glutamic acid, 20mg each of L-isoleucine, L-tryptophan, L-tyrosine, L-arginine-HCl, L-histidine-HCl-H20 and glycine, and 10mg of L-proline. The final pH of the medium was adjusted to pH4.5 with 50% (w/v) (NH4)2HP04 solution.…”

Section: Methodsmentioning

confidence: 99%

“…The final pH of the medium was adjusted to pH4.5 with 50% (w/v) (NH4)2HP04 solution. Cells were subcultured aerobically (Chan & Cossins, 1972) in the basal medium at 30°C for 24h and harvested by centrifugation (4000g for 10min at 2°C). After washing three times with sterile demineralized water the cells were used to inoculate fresh basal medium, which in some cases was supplemented with L-methionine.…”

Section: Methodsmentioning

confidence: 99%

Regulation of C1 metabolism by l-methionine in Saccharomyces cerevisiae

Lor

Cossins

1972

Biochemical Journal

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1. The concentrations of folate derivatives in aerobic cultures of Saccharomyces cerevisiae (A.T.C.C. 9763) were determined by microbiological assay employing Lactobacillus casei (A.T.C.C. 7469) and Pediococcus cerevisiae (A.T.C.C. 8081). Cells cultured in media lacking l-methionine contained higher concentrations of folate derivatives than cells grown in the same media supplemented with 2.5mumol of l-methionine/ml. The concentrations of highly conjugated derivatives were also decreased by supplementing the growth medium with l-methionine. 2. DEAE-cellulose column chromatography of extracts prepared from cells grown under these conditions revealed that the concentrations of methylated tetrahydrofolates were drastically decreased by the methionine supplement. Smaller decreases were also observed in the concentrations of formylated and unsubstituted derivatives. 3. The concentrations of four enzymes of C(1) metabolism were compared after 6h of growth in the presence and in the absence of l-methionine (2.5mumol/ml). The specific activities of formyltetrahydrofolate synthetase, methylenetetrahydrofolate reductase and serine hydroxymethyltransferase were not altered by this treatment but that of 5-methyltetrahydrofolate-homocysteine methyltransferase was decreased by approx. 65% when l-methionine was supplied. The activities of 5-methyltetrahydrofolate-homocysteine methyltransferase, serine hydroxymethyltransferase and formyltetrahydrofolate synthetase were not appreciably altered by l-methionine in vitro. In contrast this amino acid was found to inhibit the activity of methylenetetrahydrofolate reductase. 4. Feeding experiments employing sodium [(14)C]formate indicated that cells grown in the presence of exogenous methionine, although having less ability to convert formate into methionine, readily incorporated (14)C into serine and the adenosyl moiety of S-adenosylmethionine. 5. It is suggested that exogenous l-methionine controls C(1) metabolism in Saccharomyces principally by regulation of methyl-group biogenesis within the folate pool.

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Regulation of arginase levels by urea and intermediates of the Krebs‐Henseleit cycle in Saccharomyces cerevisiae

Cited by 6 publications

References 19 publications

Arginine and Endothelial Function

Arginine and Endothelial Function

Decreased Expression of the Human Urea Transporter SLC14A1 in Bone is Induced by Cytokines and Stimulates Adipogenesis of Mesenchymal Progenitor Cells

Regulation of C1 metabolism by l-methionine in Saccharomyces cerevisiae

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