L arginine

Manufactured by Merck Group

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L-arginine is an amino acid that plays a crucial role in various physiological processes. It serves as a substrate for the production of nitric oxide, which is essential for maintaining healthy blood flow and cardiovascular function. This lab equipment product can be utilized for research and scientific applications related to the study of L-arginine and its associated biological functions.

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Lab products found in correlation

Close spelling variants of this product

L-Arginine 13C615N4 hydrochloride (5 citations) N-nitro-L-arginine methyl ester (3 citations) Nw-nitro-L-arginine methylester hydrochloride (L-NAME), (3 citations) [13C6,15N4]L-arginine-HCl (2 citations) Poly-L-Arginine (13 citations) L-NG-monomethyl-arginine-citrate (L-NMMA) (4 citations) NG-monomethyl-l-arginine (NGMMA) (2 citations) L-Arginine 12C614N4 hydrochloride (3 citations) Nitro-L-arginine methyl ester hydrochloride (L-NAME) (2 citations) L-13C615N4-arginine (Arg-10, (2 citations)

442 protocols using l arginine

L-arginine Modulation of Leishmania Viability

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The effect of L-arginine on the viability of L. donovani promastigotes were analyzed by 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenylterazolium bromide (MTT) assay as described previously [34 (link), 35 (link)]. Leishmania promastigotes of the exponential phase were grown in complete RPMI media (Invitrogen), RPMI media with different concentrations (0–200 mg/L) of L-arginine (Sigma-Aldrich), single amino acid free or supplemented RPMI media as well as complete amino acid free RPMI media for 0–120 hrs. The OD was recorded on an ELISA reader (Multiskan EX; Thermo Fisher Scientific, Waltham, MA) at 570 nm and percent cell viability was determined. The growth of the parasite in absence of L-arginine but presence of L-lysine, glutamine, proline (all from Sigma-Aldrich) or L-ornithine, putrescine, spermidine, spermine (all from Merck-Millipore) as well as in presence of L-arginine was assessed by trypan blue dye exclusion method. Viable cells were quantified by counting the number of non-stained cells. Results were expressed as mean±SD for three independent experiments performed in triplicate.

Mandal A., Das S., Roy S., Ghosh A.K., Sardar A.H., Verma S., Saini S., Singh R., Abhishek K., Kumar A., Mandal C, & Das P. (2016). Deprivation of L-Arginine Induces Oxidative Stress Mediated Apoptosis in Leishmania donovani Promastigotes: Contribution of the Polyamine Pathway. PLoS Neglected Tropical Diseases, 10(1), e0004373.

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Ibuprofen and L-arginine Modulate Inflammatory Responses

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RAW264.7 cells and A549 cells were purchased from American Type Culture Collection (Manassas, VA, USA) and cultured in either arginine-free DMEM (Thermo Fisher Scientific Life Sciences, Waltham, MA, USA) or standard DMEM (containing 400 µM l-arginine; Sigma-Aldrich, St. Louis, MO, USA), both supplemented with fetal calf serum (10%; LabTech, Uckfield, United Kingdom). Confluent cultures were treated with LPS (RAW264.7 cells; 1 μg/ml; Sigma-Aldrich) or IL-1β (A549 cells; 10 ng/ml; R&D Systems, Minneapolis, MN, USA) for 24 h to induce iNOS and COX-2, in some cases in the presence of the NOS inhibitors, l-NAME (300 μM; Sigma-Aldrich) or ADMA (1 mM; Sigma-Aldrich). Increasing concentrations of ibuprofen arginate (Zambon Pharma), ibuprofen sodium (Sigma-Aldrich), l-arginine free base (Sigma-Aldrich), or the combination of ibuprofen sodium and l-arginine were also added such that the molar concentration of l-arginine present in each preparation was the same, or for ibuprofen sodium, the molar concentration of ibuprofen. After 24 h, media were collected for measurement of nitrite accumulation using the Griess reaction (Sigma-Aldrich) or PGE₂ using immunoassay (Cisbio, Codolet, France). Cell viability was assessed using the alamarBlue metabolic activity assay (Thermo Fisher Scientific).

Kirkby N.S., Tesfai A., Ahmetaj-Shala B., Gashaw H.H., Sampaio W., Etelvino G., Leão N.M., Santos R.A, & Mitchell J.A. (2016). Ibuprofen arginate retains eNOS substrate activity and reverses endothelial dysfunction: implications for the COX-2/ADMA axis. The FASEB Journal, 30(12), 4172-4179.

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CD8 ζ Expression Modulation by L-arginine

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Detection of CD8 ζ after culture in medium with or without L-arginine was performed according to previously described protocols (Das et al., 2008 (link)). PBMCs were incubated at 37°C overnight in either L-arginine-free medium or L-arginine-free medium supplemented with L-arginine (0.2 g/L, Sigma-Aldrich, USA). Then the cells were surface stained with anti-CD3-FITC and anti-CD8-APC and intracellularly stained with the anti-TCR ζ-PE mAb or its corresponding isotype control (IgG1-PE mAb), and finally analyzed using the FACSCalibur and FlowJo software.

Zeng Q.L., Yang B., Sun H.Q., Feng G.H., Jin L., Zou Z.S., Zhang Z., Zhang J.Y, & Wang F.S. (2014). Myeloid-Derived Suppressor Cells Are Associated with Viral Persistence and Downregulation of TCR ζ Chain Expression on CD8+ T Cells in Chronic Hepatitis C Patients. Molecules and Cells, 37(1), 66-73.

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Vascular Reactivity Modulation by AMP and L-Arginine

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Phenylephrine (PE) (Sigma, Saint-Louis, MO, USA) precontraction was achieved by the addition of 8 or 20 μM (as indicated by the manufacturer) to each bath in order to reach a stable strip contracting effect. Although 8 μM PE was generally considered sufficient with no detectable change at 20 μM PE, we preferred to use the 20 μM dosage in order to obtain the highest possible precontraction effect. Drugs AMP (Interchemica S.r.l., Strambino, Italy) and L-Arginine (Sigma-Aldrich, Saint-Quentin-Fallavier, France) were administered either independently or in sequential combinations (AMP at different doses, then L-Arginine at different doses, then the combination AMP–L-Arginine) to the strips under precontracted conditions. The final bath concentrations were between 10⁻⁴ M and 10⁻³ M. Nitric oxide (NO) synthase inhibitor N-nitro-L-Arginine (L-NNA) at the dose of 5.10⁻⁴ M was also administered to the strips before treatment with AMP.

Stücker O., Pons C., Neuzillet Y., Laemmel E, & Lebret T. (2014). Effects of Adenosine Monophosphate Used in Combination with L-Arginine on Female Rabbit Corpus Cavernosum Tissue. Sexual Medicine, 2(1), 1-7.

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Arginase Activity Assay in BV-2 Cells

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Arginase activity was evaluated according to the method described by Corraliza et al. [24 (link)]. BV-2 cells (1 × 10⁶ cells/mL) were pretreated with DEAC or CM (100 μg/mL) or 0.1% DMSO (drug vehicle), for 1 h before the addition of LPS (0.5 μg/mL), or vehicle. After 24 h, cells were lysed with buffer containing 0.1% Triton X-100. The enzyme was activated by heating the plates for 10 minutes at 55°C, using enzyme activation buffer (10 mM MnCl₂, 25 mM Tris-HCl). The hydrolysis of L-arginine (25 μL, 0.5 M, pH 9.7) was induced through the incubation of lysate (50 μL) with 25 μL of L-arginine (Sigma-Aldrich, USA) 0.5 M (pH 9.7) during 60 min at 37°C. The reaction was stopped with 400 μL of buffer containing H₂SO₄/H₃PO₄/H₂O (1/3/7, v/v/v). After the addition of α-isonitrosopropiophenone (25 μL, 9%) and heating for 30 minutes at 95°C, the concentration of urea (final product of the reaction) was determined by spectrophotometric analysis (540 nm). The concentrations of urea were interpolated from the linear equation obtained from the standard curve generated by known concentrations of urea (1.5 to 300 μg/mL).

de Araújo A.B., Azul F.V., Silva F.R., de Almeida T.S., Oliveira J.V., Pimenta A.T., Bezerra A.M., Machado N.J, & Leal L.K. (2022). Antineuroinflammatory Effect of Amburana cearensis and Its Molecules Coumarin and Amburoside A by Inhibiting the MAPK Signaling Pathway in LPS-Activated BV-2 Microglial Cells. Oxidative Medicine and Cellular Longevity, 2022, 6304087.

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Coenzyme Q10 Ameliorates Pancreatitis

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Rats were randomly divided into 4 groups (n = 8). Control group received intraperitoneal (IP) injections of normal saline. In sham and experimental groups, pancreatitis was induced with 3.2 g/kg bodyweight L-arginine (Sigma-Aldrich, Germany) IP, twice at an interval of 1 hour. Rats in E1 and E2 groups were, respectively, treated with a single dose of 100 and 200 mg/kg bodyweight Q10 (Sigma-Aldrich, Germany) IP, 30 minutes prior to L-arginine administration.

Mirmalek S.A., Gholamrezaei Boushehrinejad A., Yavari H., Kardeh B., Parsa Y., Salimi-Tabatabaee S.A., Yadollah-Damavandi S., Parsa T., Shahverdi E, & Jangholi E. (2016). Antioxidant and Anti-Inflammatory Effects of Coenzyme Q10 on L-Arginine-Induced Acute Pancreatitis in Rat. Oxidative Medicine and Cellular Longevity, 2016, 5818479.

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Whole Blood Stimulation for Leishmania Antigen

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Three x 2ml of blood were collected in EDTA tubes and 3 x 2ml in heparin tubes (BD). Soluble Leishmania antigen (SLA) was prepared from stationary-PHAse L. donovani promastigotes isolated from 5 patients as described in [14 (link)], and was added immediately after blood collection at a concentration of 5μg/mL and phytohaemagglutinin (PHA, Sigma) at 10 μg/mL. For the stimulation in the presence of L-arginine, two x 2ml tubes of blood were collected and 1mM L-arginine (Sigma) was added directly in the tubes. Unstimulated blood was used as negative control (nil). Plasma from activated blood samples and negative controls was collected after 24 hours of incubation at 37°C and stored at -20°C for further analysis.

Adem E., Tajebe F., Getahun M., Kiflie A., Diro E., Hailu A., Shkedy Z., Mengesha B., Mulaw T., Atnafu S., Deressa T., Mathewos B., Abate E., Modolell M., Munder M., Müller I., Takele Y, & Kropf P. (2016). Successful Treatment of Human Visceral Leishmaniasis Restores Antigen-Specific IFN-γ, but not IL-10 Production. PLoS Neglected Tropical Diseases, 10(3), e0004468.

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Quantification of Arginase Activity

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Arginase activity was measured as previously reported (47 (link)). Briefly, rat alveolar macrophages were lysed with 50 μl of 50 mM Tris–HCl pH 7.5, Triton X-100 0.1 %, 1 mM benzamidine, 200 μg/ml aprotinin, and 200 μg/ml leupeptin. After 30 min shaking at 4ºC, arginase was activated with 50 μl of 10 mM MnCl₂ and 50 mM Tris-HCl, pH 7.5, for 10 min at 55º C. L-arginine hydrolysis was measured by incubating the cell lysate with 25 μl of 0.5 M L-arginine (Sigma) (pH 9.7) at 37ºC for 1 h. The reaction was stopped by addition of 200 μl H₂SO₄ /H₃PO₄ /H₂O (1:3:7 v/v). The produced urea was quantified at 570 nm after addition of 25 μl of α-isonitrosopropiophenone (dissolved in 100% ethanol) followed by heating at 99ºC for 45 min. Urea production was normalized to cell number for each treatment by quantifying cells with the WST-1 reagent (Roche), following manufacturer’ instructions. One unit of arginase activity is defined as the amount of enzyme that catalyses the formation of 1 μmol urea per min.

Minutti C.M., Jackson-Jones L.H., García-Fojeda B., Knipper J.A., Sutherland T.E., Logan N., Rinqvist E., Guillamat-Prats R., Ferenbach D.A., Artigas A., Stamme C., Chroneos Z.C., Zaiss D.M., Casals C, & Allen J.E. (2017). Local enhancers of Type 2-mediated macrophage activation and proliferation promote tissue repair. Science (New York, N.Y.), 356(6342), 1076-1080.

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Colorimetric Assay for Arg1 Activity

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Arg1 activity was determined by a standard colorimetric method⁶⁰ in cell lysates. Briefly, cells were lysed by adding 0.1% Triton X-100 (Sigma) and 50 mM Tris-HCl (pH 7.5). 10 mM MnCl₂ (Sigma) to cell samples, then heated at 56°C for 7 min to activate the enzyme. Hydrolysis of L-arginine by Arg1 was performed by incubating the mixture with 50 µmol of L-arginine (pH 9.7; Sigma) at 37°C for 2 h, and the reaction was stopped by adding an acid solution (H₂SO₄; H₃PO₄; H₂O). For the determination of urea production, α-isonitrosopropiophenone (Sigma) was added and the mixture was incubated at 95°C for 30 min and then 4°C for 30 min. Each sample was assayed in duplicate, the absorbance was measured at 540 nm and urea production was determined with urea as a standard.

Leblond M.M., Gérault A.N., Corroyer-Dulmont A., MacKenzie E.T., Petit E., Bernaudin M, & Valable S. (2015). Hypoxia induces macrophage polarization and re-education toward an M2 phenotype in U87 and U251 glioblastoma models. Oncoimmunology, 5(1), e1056442.

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Modulation of MDSC-Mediated T Cell Suppression

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MDSC were co-cultured with CD3/CD28 activated splenocytes for 4 days in the presence of Arginase-1 inhibitor N^ω-hydroxy-nor-Arginine (nor-NOHA) (Cayman Chemical, 300μM) or neutralization antibodies against IL-4, IL-6, IL-10 and GM-CSF (20 μg/ml each) to suppress arginase-1 function or expression in MDSC, followed by T cell proliferation assay as described above. To supplement L-arginine in the co-culture system, cell culture medium was replenished with excess L-arginine (10 mM, Sigma) on day 1 and day 3 and then assayed for T cell proliferation as described.

Bian Z., Abdelaal A.M., Shi L., Liang H., Xiong L., Kidder K., Venkataramani M., Culpepper C., Zen K, & Liu Y. (2018). Arginase-1 is neither constitutively expressed in nor required for myeloid-derived suppressor cell (MDSC)-mediated inhibition of T cell proliferation. European journal of immunology, 48(6), 1046-1058.

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