scholarly journals Pulsed EPR Determination of the Distance between Heme Iron and FMN Centers in a Human Inducible Nitric Oxide Synthase

2010 ◽  
Vol 132 (34) ◽  
pp. 12059-12067 ◽  
Author(s):  
Andrei V. Astashkin ◽  
Bradley O. Elmore ◽  
Weihong Fan ◽  
J. Guy Guillemette ◽  
Changjian Feng
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Inducible Nitric Oxide Synthase ◽  
Heme Iron ◽  
Pulsed Epr ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide

scholarly journals Plaunol A from Croton stellatopilosus Inhibits Inducible Nitric Oxide Synthase and Cyclooxygenase-2 in Macrophage RAW264.7 Cells

2018 ◽  
Vol 13 (7) ◽  
pp. 1934578X1801300
Author(s):  
Charoenwong Premprasert ◽  
Supinya Tewtrakul ◽  
Juraithip Wungsintaweekul
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Inducible Nitric Oxide Synthase ◽  
Cyclooxygenase 2 ◽  
Raw264.7 Cells ◽  
Mrna Levels ◽  
Chromatographic Techniques ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide

A clerodane diterpene (plaunol A) and three flavonoids (vitexin; luteolin-7-O-β-D-glucoside and luteolin-4'-O-glucoside) were isolated from stems and leaves of Croton stellatoliosus Ohba, using series of chromatographic techniques. Evaluation for anti-inflammatory activity in LPS-induced RAW264.7 cells revealed that, only plaunol A exhibited the inhibitory activity on nitric oxide production with the IC50 of 11.69 μM. This was no cytotoxic effect to the cells at a concentration of 100 μM, by MTT assay. Determination of mRNA levels by qRT-PCR, indicated that plaunol A suppressed the expressions of inducible nitric oxide synthase and cyclooxygenase-2 in lipopolysaccharide-induced RAW264.7 cells.

scholarly journals Briaviolide Q, a New Briarane from the Cultured Briareum violaceum

2018 ◽  
Vol 13 (10) ◽  
pp. 1934578X1801301 ◽  
Author(s):  
Tsung-Chang Tsai ◽  
Jing-Hao Xu ◽  
Mu-Jang Li ◽  
Jih-Jung Chen ◽  
Jui-Hsin Su ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Protein Expression ◽  
Inducible Nitric Oxide Synthase ◽  
Structure Determination ◽  
Spectroscopic Data ◽  
Murine Cell Line ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide

A new briarane-type diterpenoid, briaviolide Q (1), along with a known analogue, excavatolide Z (2), were obtained from a cultured octocoral Briareum violaceum. Details of the isolation and structure determination of briarane 1 from spectroscopic data are presented in this paper. In RAW264.7 cells, a macrophage-like murine cell line, briarane 1 was found to inhibit the protein expression of pro-inflammatory inducible nitric oxide synthase (iNOS) in cells stimulated by lipopolysaccharide (LPS).

scholarly journals Fourier transform infrared spectroscopy study of ligand photodissociation and migration in inducible nitric oxide synthase

F1000Research ◽  
2014 ◽  
Vol 3 ◽  
pp. 290 ◽  
Author(s):  
Michael Horn ◽  
Karin Nienhaus ◽  
Gerd Ulrich Nienhaus
Keyword(s):  
Nitric Oxide ◽  
Carbon Monoxide ◽  
Fourier Transform ◽  
Nitric Oxide Synthase ◽  
Inducible Nitric Oxide Synthase ◽  
Fourier Transform Infrared ◽  
Heme Iron ◽  
Cryogenic Temperatures ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide

Inducible nitric oxide synthase (iNOS) is a homodimeric heme enzyme that catalyzes the formation of nitric oxide (NO) from dioxygen and L-arginine (L-Arg) in a two-step process. The produced NO can either diffuse out of the heme pocket into the surroundings or it can rebind to the heme iron and inhibit enzyme action. Here we have employed Fourier transform infrared (FTIR) photolysis difference spectroscopy at cryogenic temperatures, using the carbon monoxide (CO) and NO stretching bands as local probes of the active site of iNOS. Characteristic changes were observed in the spectra of the heme-bound ligands upon binding of the cofactors. Unlike photolyzed CO, which becomes trapped in well-defined orientations, as indicated by sharp photoproduct bands, photoproduct bands of NO photodissociated from the ferric heme iron were not visible, indicating that NO does not reside in the protein interior in a well-defined location or orientation. This may be favorable for NO release from the enzyme during catalysis because it reduces self-inhibition. Moreover, we used temperature derivative spectroscopy (TDS) with FTIR monitoring to explore the dynamics of NO and carbon monoxide (CO) inside iNOS after photodissociation at cryogenic temperatures. Only a single kinetic photoproduct state was revealed, but no secondary docking sites as in hemoglobins. Interestingly, we observed that intense illumination of six-coordinate ferrous iNOSoxy-NO ruptures the bond between the heme iron and the proximal thiolate to yield five-coordinate ferric iNOSoxy-NO, demonstrating the strong trans effect of the heme-bound NO.

scholarly journals Fourier transform infrared spectroscopy study of ligand photodissociation and migration in inducible nitric oxide synthase

F1000Research ◽  
2014 ◽  
Vol 3 ◽  
pp. 290 ◽  
Author(s):  
Michael Horn ◽  
Karin Nienhaus ◽  
Gerd Ulrich Nienhaus
Keyword(s):  
Nitric Oxide ◽  
Carbon Monoxide ◽  
Fourier Transform ◽  
Nitric Oxide Synthase ◽  
Inducible Nitric Oxide Synthase ◽  
Fourier Transform Infrared ◽  
Heme Iron ◽  
Cryogenic Temperatures ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide

Inducible nitric oxide synthase (iNOS) is a homodimeric heme enzyme that catalyzes the formation of nitric oxide (NO) from dioxygen and L-arginine (L-Arg) in a two-step process. The produced NO can either diffuse out of the heme pocket into the surroundings or it can rebind to the heme iron and inhibit enzyme action. Here we have employed Fourier transform infrared (FTIR) photolysis difference spectroscopy at cryogenic temperatures, using the carbon monoxide (CO) and NO stretching bands as local probes of the active site of iNOS. Characteristic changes were observed in the spectra of the heme-bound ligands upon binding of the cofactors. Unlike photolyzed CO, which becomes trapped in well-defined orientations, as indicated by sharp photoproduct bands, photoproduct bands of NO photodissociated from the ferric heme iron were not visible, indicating that NO does not reside in the protein interior in a well-defined location or orientation. This may be favorable for NO release from the enzyme during catalysis because it reduces self-inhibition. Moreover, we used temperature derivative spectroscopy (TDS) with FTIR monitoring to explore the dynamics of NO and carbon monoxide (CO) inside iNOS after photodissociation at cryogenic temperatures. Only a single kinetic photoproduct state was revealed, but no secondary docking sites as in hemoglobins. Interestingly, we observed that intense illumination of six-coordinate ferrous iNOSoxy-NO ruptures the bond between the heme iron and the proximal thiolate to yield five-coordinate ferric iNOSoxy-NO, demonstrating the strong trans effect of the heme-bound NO.

Helicobacter pylori enhances an expression of inducible nitric oxide synthase (iNOS) in human gastric epithelium

2001 ◽  
Vol 120 (5) ◽  
pp. A653-A654
Author(s):  
Q SONG ◽  
M OWENS ◽  
D SMOOT ◽  
H ASHKTORAB ◽  
B GOLD
Keyword(s):  
Nitric Oxide ◽  
Helicobacter Pylori ◽  
Nitric Oxide Synthase ◽  
Inducible Nitric Oxide Synthase ◽  
Gastric Epithelium ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide

289: Roles of Inducible Nitric Oxide Synthase in Voiding Function and Bladder Pain During Experimental Cystitis

2006 ◽  
Vol 175 (4S) ◽  
pp. 96-96
Author(s):  
Masayoshi Nomura ◽  
Hisae Nishii ◽  
Masato Tsutsui ◽  
Naohiro Fujimoto ◽  
Tetsuro Matsumoto
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Inducible Nitric Oxide Synthase ◽  
Voiding Function ◽  
Bladder Pain ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide

Search for Potential Inducible Nitric Oxide Synthase Inhibitors with Favorable ADMET Profiles for the Therapy of Helicobacter pylori Infections

2020 ◽  
Vol 19 (30) ◽  
pp. 2795-2804 ◽  
Author(s):  
Ricardo Pereira Rodrigues ◽  
Juliana Santa Ardisson ◽  
Rita de Cássia Ribeiro Gonçalves ◽  
Tiago Branquinho Oliveira ◽  
Vinicius Barreto da Silva ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Helicobacter Pylori ◽  
Nitric Oxide Synthase ◽  
Inducible Nitric Oxide Synthase ◽  
Crucial Role ◽  
Chemical Space ◽  
Target Selection ◽  
Oxide Synthase ◽  
Inos Inhibition ◽  
Inducible Nitric Oxide

Background: Helicobacter pylori is a gram-negative bacterium related to chronic gastritis, peptic ulcer and gastric carcinoma. During its infection process, promotes excessive inflammatory response, increasing the release of reactive species and inducing the production of pro-inflammatory mediators. Inducible Nitric Oxide Synthase (iNOS) plays a crucial role in the gastric carcinogenesis process and a key mediator of inflammation and host defense systems, which is expressed in macrophages induced by inflammatory stimuli. In chronic diseases such as Helicobacter pylori infections, the overproduction of NO due to the prolonged induction of iNOS is of major concern. Objective: In this sense, the search for potential iNOS inhibitors is a valuable strategy in the overall process of Helicobacter pylori pathogeny. Method: In silico techniques were applied in the search of interesting compounds against Inducible Nitric Oxide Synthase enzyme in a chemical space of natural products and derivatives from the Analyticon Discovery databases. Results: The five compounds with the best iNOS inhibition profile were selected for activity and toxicity predictions. Compound 9 (CAS 88198-99-6) displayed significant potential for iNOS inhibition, forming hydrogen bonds with residues from the active site and an ionic interaction with heme. This compound also displayed good bioavailability and absence of toxicity/or from its probable metabolites. Conclusion: The top-ranked compounds from the virtual screening workflow show promising results regarding the iNOS inhibition profile. The results evidenced the importance of the ionic bonding during docking selection, playing a crucial role in binding and positioning during ligand-target selection for iNOS.

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