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inos-inducible-nitric-oxide-synthase

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Meeting Abstracts
Journal: Diabetes
Diabetes 2000;49(7):1116–1122
Published: 01 July 2000
...D Liu; D Pavlovic; M C Chen; M Flodström; S Sandler; D L Eizirik Prolonged exposure of rodent beta-cells to combinations of cytokines induces the inducible form of nitric oxide synthase (iNOS) expression and Fas expression, nitric oxide (NO) production, and cell death. It also induces...
Images
Inflammatory gene expression is <span class="search-highlight">induced</span> in 3 days after HFD. C57BL/6J mice ...
Published: 16 September 2011
FIG. 4. Inflammatory gene expression is induced in 3 days after HFD. C57BL/6J mice were treated with an HFD. Mice were fed an HFD for 0 (0 or N [NCD]), 1 (1), 3 (3), or 7 days (7), or 16 weeks (H). mRNA levels of inflammatory genes from epididymal adipose tissue (WAT), brown adipose tissue (BAT), liver, and skeletal muscle were measured by quantitative real-time RT-PCR analysis. n = 10 at each time point. *P < 0.05; **P < 0.01; ***P < 0.001. iNOS, inducible nitric oxide synthase; SAA3, serum amyloid A3. FIG. 4. Inflammatory gene expression is induced in 3 days after HFD. C57BL/6J mice were treated with an HFD. Mice were fed an HFD for 0 (0 or N [NCD]), 1 (1), 3 (3), or 7 days (7), or 16 weeks (H). mRNA levels of inflammatory genes from epididymal adipose tissue (WAT), brown adipose tissue (BAT), liver, and skeletal muscle were measured by quantitative real-time RT-PCR analysis. n = 10 at each time point. *P < 0.05; **P < 0.01; ***P < 0.001. iNOS, inducible nitric oxide synthase; SAA3, serum amyloid A3. More
Images
Metabolic characterization of <em>Itch<sup>−/−</sup></em> mice. Six...
Published: 16 January 2014
Figure 1 Metabolic characterization of Itch−/− mice. Six-week-old WT and Itch−/− mice fed a ND. Weight (A) and blood glucose concentration (B) (n = 8 per group; **P < 0.005, ***P < 0.001, Student t test). Data are means ± SD. C: Peritoneal macrophage gene expression analysis. Expression of mRNA was determined by real-time PCR and normalized to β-actin (n = 4 per group; *P < 0.05, **P < 0.005, ***P < 0.001, Student t test). Data are means ± SD. iNOS, inducible nitric oxide synthase; a.u., arbitrary units. Figure 1. Metabolic characterization of Itch−/− mice. Six-week-old WT and Itch−/− mice fed a ND. Weight (A) and blood glucose concentration (B) (n = 8 per group; **P < 0.005, ***P < 0.001, Student t test). Data are means ± SD. C: Peritoneal macrophage gene expression analysis. Expression of mRNA was determined by real-time PCR and normalized to β-actin (n = 4 per group; *P < 0.05, **P < 0.005, ***P < 0.001, Student t test). Data are means ± SD. iNOS, inducible nitric oxide synthase; a.u., arbitrary units. More
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Fpr2 mediates macrophage M1 polarization. WT and Fpr2<sup>−/−</sup> BMDMs w...
Published: 12 March 2019
Figure 8 Fpr2 mediates macrophage M1 polarization. WT and Fpr2−/− BMDMs were treated with 100 ng/mL LPS and examined for expression of M1 macrophage markers (treated for 6 h) (A), production of proinflammatory cytokines in the culture supernatant (treated for 9 h) (B), and phosphorylation of NF-κB p65, MAP kinases (ET, exposure time), and TAK1 (treated for 30 min) (C) (n = 3 per group). DF: BMDMs infected with Fpr2 expressing lentiviruses (Lenti-Fpr2) or control viruses (Lenti-NC) and examined for the expression of M1 macrophage markers (iNos, inducible nitric oxide synthase) (D) and phosphorylation (p-) of NF-κB p65 and MAP kinases after stimulation with 100 ng/mL LPS for 30 min (E and F). GI: BMDMs were stimulated with 400 μmol/L palmitate (Pal) (dissolved in BSA buffer) and examined for expression of M1-related proinflammatory cytokines (stimulated for 3 h) (G), and phosphorylation of NF-κB p65 and MAP kinases (treated for 1 h) (H and I) (n = 3 per group). Values shown represent the mean ± SD. *P < 0.05, **P < 0.01, ***P < 0.001. Two-way ANOVA was used in A, B, D, F, G, and I, and two-way repeated-measures ANOVA was used in C. Veh, vehicle. Figure 8. Fpr2 mediates macrophage M1 polarization. WT and Fpr2−/− BMDMs were treated with 100 ng/mL LPS and examined for expression of M1 macrophage markers (treated for 6 h) (A), production of proinflammatory cytokines in the culture supernatant (treated for 9 h) (B), and phosphorylation of NF-κB p65, MAP kinases (ET, exposure time), and TAK1 (treated for 30 min) (C) (n = 3 per group). D–F: BMDMs infected with Fpr2 expressing lentiviruses (Lenti-Fpr2) or control viruses (Lenti-NC) and examined for the expression of M1 macrophage markers (iNos, inducible nitric oxide synthase) (D) and phosphorylation (p-) of NF-κB p65 and MAP kinases after stimulation with 100 ng/mL LPS for 30 min (E and F). G–I: BMDMs were stimulated with 400 μmol/L palmitate (Pal) (dissolved in BSA buffer) and examined for expression of M1-related proinflammatory cytokines (stimulated for 3 h) (G), and phosphorylation of NF-κB p65 and MAP kinases (treated for 1 h) (H and I) (n = 3 per group). Values shown represent the mean ± SD. *P < 0.05, **P < 0.01, ***P < 0.001. Two-way ANOVA was used in A, B, D, F, G, and I, and two-way repeated-measures ANOVA was used in C. Veh, vehicle. More
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Studies identifying unique cellular responses to physical inactivity when s...
Published: 01 November 2007
FIG. 6. Studies identifying unique cellular responses to physical inactivity when standing/ambulatory time is limited. Acute administration of the transcription blocker actinomycin D was without effect on LPL in rats with a normally higher amount of nonexercise physical activity. Administering the transcription blocker at the initiation of acute inactivity prevented the fall in LPL activity, indicating that a gene is switched on, which is responsible for the lowering of LPL activity (A). Re-initiation of intermittent standing and very slow ambulation (0.3 mph) following 12 h of inactivity restored muscle LPL completely (B). Blocking transcription did not impair this process. Lowering of plasma triglyceride and free fatty acid during inactivity with nicotinic acid (NA) completely prevented the decrease in LPL caused by physical inactivity, while having no effect on LPL activity in muscles with normal spontaneous cage activity (C). Inhibition of several signaling pathways known previously to suppress LPL activity had no effect on the decrease in LPL activity caused by physical inactivity (D). Amg, aminoguanidine; HR-LPL, heparin-releasable LPL activity, which is the functional fraction of LPL activity residing on the surface of the capillary endothelium; iNOS, inducible nitric oxide synthase; NFκB, nuclear factor-κB; Ptx, SA, pentoxifylline/salicylic acid; TNF-α, tumor necrosis factor-α. (Please see http://dx.doi.org/10.2337/db07-0882 for a high-quality digital represention of this figure.) FIG. 6. Studies identifying unique cellular responses to physical inactivity when standing/ambulatory time is limited. Acute administration of the transcription blocker actinomycin D was without effect on LPL in rats with a normally higher amount of nonexercise physical activity. Administering the transcription blocker at the initiation of acute inactivity prevented the fall in LPL activity, indicating that a gene is switched on, which is responsible for the lowering of LPL activity (A). Re-initiation of intermittent standing and very slow ambulation (0.3 mph) following 12 h of inactivity restored muscle LPL completely (B). Blocking transcription did not impair this process. Lowering of plasma triglyceride and free fatty acid during inactivity with nicotinic acid (NA) completely prevented the decrease in LPL caused by physical inactivity, while having no effect on LPL activity in muscles with normal spontaneous cage activity (C). Inhibition of several signaling pathways known previously to suppress LPL activity had no effect on the decrease in LPL activity caused by physical inactivity (D). Amg, aminoguanidine; HR-LPL, heparin-releasable LPL activity, which is the functional fraction of LPL activity residing on the surface of the capillary endothelium; iNOS, inducible nitric oxide synthase; NFκB, nuclear factor-κB; Ptx, SA, pentoxifylline/salicylic acid; TNF-α, tumor necrosis factor-α. (Please see http://dx.doi.org/10.2337/db07-0882 for a high-quality digital represention of this figure.) More
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PIAS1 in the adipocytes suppressed the chemotaxis of macrophages. On day 5 ...
Published: 31 August 2015
Figure 6 PIAS1 in the adipocytes suppressed the chemotaxis of macrophages. On day 5 after adipogenic induction, PIAS1 was silenced by siPIAS1 or ectopically expressed by Ad-PIAS1. The indicated cells were then harvested on day 8 postinduction and subjected to further studies. A: qPCR analysis of the mRNA level of inflammation-related genes. Data were normalized to the mRNA level in the cells treated with Ad-LacZ. B: qPCR analysis of the mRNA level of inflammation-related genes. Data were normalized to the mRNA level in the cells treated with siNC. C: The indicated cells were harvested, and Western blotting was conducted to measure the level of the indicated proteins. D: Cellular supernatant of the indicated cells was collected and then subjected to ELISA assay to detect the concentration of inflammatory cytokines. E: The indicated cells were harvested after stimulation with TNF-α for 12 h. ChIP qPCR assay was performed to measure binding activity of NF-κB on the promoters of TNF-α and MIP2. The data were normalized to the IgG control. F: The ACM, prepared by incubating the indicated adipocytes in DMEM supplemented with 0.2% BSA for 12 h, were added to the lower chamber. Macrophages were loaded on the upper chamber and allowed to migrate for 12 h at 37°C. The migratory cells on the lower surface of the membrane were counted manually using 5–6 randomly selected areas. ERK, extracellular signal–related kinase; iNOS, inducible nitric oxide synthase; MAPK, mitogen-activated protein kinase. *P < 0.05; **P < 0.01; ***P < 0.001. Figure 6. PIAS1 in the adipocytes suppressed the chemotaxis of macrophages. On day 5 after adipogenic induction, PIAS1 was silenced by siPIAS1 or ectopically expressed by Ad-PIAS1. The indicated cells were then harvested on day 8 postinduction and subjected to further studies. A: qPCR analysis of the mRNA level of inflammation-related genes. Data were normalized to the mRNA level in the cells treated with Ad-LacZ. B: qPCR analysis of the mRNA level of inflammation-related genes. Data were normalized to the mRNA level in the cells treated with siNC. C: The indicated cells were harvested, and Western blotting was conducted to measure the level of the indicated proteins. D: Cellular supernatant of the indicated cells was collected and then subjected to ELISA assay to detect the concentration of inflammatory cytokines. E: The indicated cells were harvested after stimulation with TNF-α for 12 h. ChIP qPCR assay was performed to measure binding activity of NF-κB on the promoters of TNF-α and MIP2. The data were normalized to the IgG control. F: The ACM, prepared by incubating the indicated adipocytes in DMEM supplemented with 0.2% BSA for 12 h, were added to the lower chamber. Macrophages were loaded on the upper chamber and allowed to migrate for 12 h at 37°C. The migratory cells on the lower surface of the membrane were counted manually using 5–6 randomly selected areas. ERK, extracellular signal–related kinase; iNOS, inducible nitric oxide synthase; MAPK, mitogen-activated protein kinase. *P < 0.05; **P < 0.01; ***P < 0.001. More
Images
Inflammation does not contribute to the KO phenotype. mRNA expression of pr...
Published: 28 May 2015
Figure 8 Inflammation does not contribute to the KO phenotype. mRNA expression of pro/anti-inflammatory genes in liver (A) and eWAT (B) of WT and KO HFD-fed mice. Data are reported as the mean ± SEM, n = 5 per group. C: Hematoxylin-eosin (H+E) staining and Oil Red O staining of hepatic sections from HFD-fed WT and KO mice. D: mRNA expression of hepatic gluconeogenic genes in HFD-fed WT and KO mice. E–J: Hematopoietic cells from GPR43-deficient mice were generated by bone marrow transplantation. E: mRNA expression of GPR43 and GPR41 in white blood cells of reconstituted mice. Data are reported as the mean ± SEM, n = 4 per group. F: Body weight of NC-diet–fed and HFD-fed reconstituted mice. Data are reported as the mean ± SEM, n = 10–12 per group. G: Intraperitoneal GTT. Data are reported as the mean ± SEM, n = 10–12 per group. H: Serum insulin concentrations during intraperitoneal GTT. Data are reported as the mean ± SEM, n = 6 per group. I: Fasting serum free fatty acid concentrations. J: Insulin tolerance test, n = 10 per group. Data are reported as the mean ± SEM. BM, bone marrow; FFA, free fatty acid; GCK, glucokinase gene; IL-1β, interleukin-1β; iNOS, inducible nitric oxide synthase; TNFα, tumor necrosis factor-α. Figure 8. Inflammation does not contribute to the KO phenotype. mRNA expression of pro/anti-inflammatory genes in liver (A) and eWAT (B) of WT and KO HFD-fed mice. Data are reported as the mean ± SEM, n = 5 per group. C: Hematoxylin-eosin (H+E) staining and Oil Red O staining of hepatic sections from HFD-fed WT and KO mice. D: mRNA expression of hepatic gluconeogenic genes in HFD-fed WT and KO mice. E–J: Hematopoietic cells from GPR43-deficient mice were generated by bone marrow transplantation. E: mRNA expression of GPR43 and GPR41 in white blood cells of reconstituted mice. Data are reported as the mean ± SEM, n = 4 per group. F: Body weight of NC-diet–fed and HFD-fed reconstituted mice. Data are reported as the mean ± SEM, n = 10–12 per group. G: Intraperitoneal GTT. Data are reported as the mean ± SEM, n = 10–12 per group. H: Serum insulin concentrations during intraperitoneal GTT. Data are reported as the mean ± SEM, n = 6 per group. I: Fasting serum free fatty acid concentrations. J: Insulin tolerance test, n = 10 per group. Data are reported as the mean ± SEM. BM, bone marrow; FFA, free fatty acid; GCK, glucokinase gene; IL-1β, interleukin-1β; iNOS, inducible nitric oxide synthase; TNFα, tumor necrosis factor-α. More
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Rag1 KO mice develop insulin resistance with increased macrophage activatio...
Published: 16 September 2011
FIG. 6. Rag1 KO mice develop insulin resistance with increased macrophage activation in 1 week of HFD. A: Macrophage infiltration and M1 polarization were increased by short-term HFD. Rag1 KO mice were treated with HFD for 1 week and killed, and epididymal adipose tissues were taken for further analyses. Total macrophages (double positive; F4/80+, CD11b+) and CD11c+ macrophages (triple positive cells; F4/80+, CD11b+, CD11c+) were increased in adipose tissue in 1 week of HFD. *P < 0.05 KO-NCD vs. KO HFD; ***P < 0.001 KO-NCD vs. KO HFD; #P < 0.05 wild-type (WT)-NCD vs. WT HFD; ##P < 0.01 WT-NCD vs. WT HFD. n = 6. B: Epididymal (Epid.) adipose tissue mass in NCD and 1-week HFD-treated Rag1 KO mice. C: Expression of inflammatory genes was promoted in 1-week HFD-fed Rag1 KO mice. mRNA levels of inflammatory genes from epididymal adipose tissue were measured by quantitative real-time RT-PCR analysis. D–F: HFD rapidly induces systemic insulin resistance in Rag1 KO mice. D: Rag1 KO mice (8 weeks old, male) were treated with NCD or HFD for 3 days (3d) (i) or 1 week (1w) (ii) and subjected to oral glucose (Glc) tolerance test. E: Serum insulin levels of Rag1 KO mice treated with NCD or HFD (for 1 week) during oral glucose tolerance. 0 min, before glucose injection; 10 min, 10 min after glucose injection. F: WT or Rag1 KO mice were treated with NCD or HFD for 1 week and subjected to insulin tolerance test with intraperitoneal injection of insulin (IP-ITT). Blood glucose levels were measured at 0, 30, 60, 90, and 120 min after insulin (0.4 unit/kg) injection. G: Glucose-uptake assays using primary adipocytes from mice treated with NCD or HFD for 1 week. iNOS, inducible nitric oxide synthase; SAA3, serum amyloid A3. *P < 0.05; **P < 0.01; ***P < 0.001. FIG. 6. Rag1 KO mice develop insulin resistance with increased macrophage activation in 1 week of HFD. A: Macrophage infiltration and M1 polarization were increased by short-term HFD. Rag1 KO mice were treated with HFD for 1 week and killed, and epididymal adipose tissues were taken for further analyses. Total macrophages (double positive; F4/80+, CD11b+) and CD11c+ macrophages (triple positive cells; F4/80+, CD11b+, CD11c+) were increased in adipose tissue in 1 week of HFD. *P < 0.05 KO-NCD vs. KO HFD; ***P < 0.001 KO-NCD vs. KO HFD; #P < 0.05 wild-type (WT)-NCD vs. WT HFD; ##P < 0.01 WT-NCD vs. WT HFD. n = 6. B: Epididymal (Epid.) adipose tissue mass in NCD and 1-week HFD-treated Rag1 KO mice. C: Expression of inflammatory genes was promoted in 1-week HFD-fed Rag1 KO mice. mRNA levels of inflammatory genes from epididymal adipose tissue were measured by quantitative real-time RT-PCR analysis. D–F: HFD rapidly induces systemic insulin resistance in Rag1 KO mice. D: Rag1 KO mice (8 weeks old, male) were treated with NCD or HFD for 3 days (3d) (i) or 1 week (1w) (ii) and subjected to oral glucose (Glc) tolerance test. E: Serum insulin levels of Rag1 KO mice treated with NCD or HFD (for 1 week) during oral glucose tolerance. 0 min, before glucose injection; 10 min, 10 min after glucose injection. F: WT or Rag1 KO mice were treated with NCD or HFD for 1 week and subjected to insulin tolerance test with intraperitoneal injection of insulin (IP-ITT). Blood glucose levels were measured at 0, 30, 60, 90, and 120 min after insulin (0.4 unit/kg) injection. G: Glucose-uptake assays using primary adipocytes from mice treated with NCD or HFD for 1 week. iNOS, inducible nitric oxide synthase; SAA3, serum amyloid A3. *P < 0.05; **P < 0.01; ***P < 0.001. More
Meeting Abstracts
Journal: Diabetes
Diabetes 1999;48(1):29–33
Published: 01 January 1999
... nitric oxide production 12-fold while stimulating mRNA expression of inducible nitric oxide synthase (iNOS). In this condition, 10-20% of cells positive for the cytokeratin-19 duct marker also stained positive for iNOS protein, whereas no positive cells were found in control preparations. Comparison...
Meeting Abstracts
Journal: Diabetes
Diabetes 1998;47(4):583–591
Published: 01 April 1998
... oxide synthase (iNOS) that generates the free radical nitric oxide. IL-1beta also induces the coexpression of the inducible isoform of cyclooxygenase (COX-2) that results in the overproduction of proinflammatory prostaglandins. The current studies were designed to characterize the involvement...
Journal Articles
Journal: Diabetes
Diabetes 2001;50(2):283–290
Published: 01 February 2001
.... This study examines the role of nuclear factor-κB (NF-κB) and the dsRNA-dependent protein kinase (PKR) in dsRNA + IFN-γ-induced nitric oxide synthase (iNOS) expression and nitric oxide production by rat, mouse,and human islets. Treatment of rat and human islets with dsRNA in the form of polyinosinic...
Journal Articles
Journal: Diabetes
Diabetes 2002;51(4):1076–1082
Published: 01 April 2002
..., Chair of Internal Medicine, University of Udine, P.le S. Maria della Misericordia, 33100 Udine, Italy. E-mail: antonio.ceriello@dpmsc.uniud.it . Received for publication 26 July 2001 and accepted in revised form 4 January 2002. CPP, coronary perfusion pressure; iNOS, inducible nitric oxide synthase...
Meeting Abstracts
Journal: Diabetes
Diabetes 2001;50(suppl_1):S70
Published: 01 February 2001
...+ on beta-cell apoptosis. We also demonstrate that IL-1beta-mediated apoptosis correlates with expression of inducible nitric oxide synthase (iNOS) and the increase in intracellular production of nitric oxide. An inhibitor of cGMP-dependent protein kinase (PKG), KT5823, suppressed IL-1beta-induced apoptosis...
Journal Articles
Journal: Diabetes
Diabetes 2002;51(2):311–316
Published: 01 February 2002
...Helen E. Thomas; Rima Darwiche; John A. Corbett; Thomas W.H. Kay Cytokines have been implicated in pancreatic β-cell destruction leading to type 1 diabetes. In vitro, a combination of γ-interferon (IFN-γ) and interleukin-1 (IL-1) stimulate inducible nitric oxide synthase (iNOS) expression in islets...
Journal Articles
Journal: Diabetes
Diabetes 1995;44(7):753–758
Published: 01 July 1995
...Allan E Karlsen; Henrik U Andersen; Henrik Vissing; Peter Mose Larsen; Stephen J Fey; Beatriz Cuartero; Ole D Madsen; Jacob S Petersen; Steen B Mortensen; Thomas Mandrup-Poulsen; Esper Boel; Jørn Nerup An inducible nitric oxide (NO) synthase isoform (iNOS) is specifically induced in the β-cells...
Meeting Abstracts
Journal: Diabetes
Diabetes 2000;49(3):346–355
Published: 01 March 2000
.... Treatment of RAW 264.7 cells and CD-1 mouse peritoneal macrophages with lipopolysaccharide (LPS) + interferon-gamma (IFN-gamma) results in inducible nitric oxide synthase (iNOS), inducible cyclooxygenase (COX-2) and interleukin-1 (IL-1) expression, increased production of nitric oxide, and the release of IL...
Journal Articles
Journal: Diabetes
Diabetes 1996;45(6):771–778
Published: 01 June 1996
..., whether these differences correlate to variations in IL-1β-induced islet inducible nitric oxide synthase (iNOS) mRNA expression and nitrite production in vitro and islet iNOS protein content in vivo. Isolated islets of Langerhans in vitro from Wistar-Kyoto/Møllegården (WK/Mol) rats were sensitive...
Journal Articles
Journal: Diabetes
Diabetes 2005;54(4):959–967
Published: 01 April 2005
...Marco A. Carvalho-Filho; Mirian Ueno; Sandro M. Hirabara; Amedea B. Seabra; José B.C. Carvalheira; Marcelo G. de Oliveira; Lício A. Velloso; Rui Curi; Mario J.A. Saad Evidence demonstrates that exogenous nitric oxide (NO) and the NO produced by inducible nitric oxide synthase (iNOS) can induce...
Journal Articles
Journal: Diabetes
Diabetes 2004;53(2):454–462
Published: 01 February 2004
...Raffaele Marfella; Clara Di Filippo; Katherine Esposito; Francesco Nappo; Elena Piegari; Salvatore Cuzzocrea; Liberato Berrino; Francesco Rossi; Dario Giugliano; Michele D’Amico We investigated the role of inducible nitric oxide synthase (iNOS) on ischemic myocardial damage and angiogenic process...
Journal Articles
Journal: Diabetes
Diabetes 2004;53(1):173–178
Published: 01 January 2004
...Bruce A. Berkowitz; Hongmei Luan; Rita R. Gupta; Daniel Pacheco; Andres Seidner; Robin Roberts; Jessica Liggett; Deborah L. Knoerzer; Jane R. Connor; Yunpeng Du; Timothy S. Kern; Yasuki Ito We aimed to test the hypothesis that the inducible form of nitric oxide synthase (iNOS) contributes...