L-Arginine-dependent formation of <i>N</i>-nitrosamines by the cytosol of macrophages activated with lipopolysaccharide and interferon-γ

Ohshima, Hiroshi; Tsuda, Mitsuhiro; Adachi, H.; Ogura, Tsutomu; Sügimura, Takashi; Esumi, Hiroyasu

doi:10.1093/carcin/12.7.1217

Cited by 59 publications

(34 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…First, it is well documented that the synthesis of nitric acid and nitrosamine(s) can be stimulated greatly by the cytosol of macrophages activated by lipopolysaccharide (LPS) and γ-interferon. 28 Second, E. coli infection accelerated urothelial proliferation. This may have augmented the mutagenic effect of the carcinogen.…”

Section: Discussionmentioning

confidence: 99%

Role of Urinary Tract Bacterial Infection in the Process of Bladder Carcinogenesis (Molecular and Biochemical Studies)

et al. 2011

View full text Add to dashboard Cite

Objective: This work is designed to study the possible role of chronic inflammation induced by E. coli in the urinary bladder of rats, the protective role of soybean flour, in addition to the role of oxidative and nitrosative stresses during bladder carcinogenesis. Material & Methods:This study was done on one hundred and fifty adult male albino rats (50 -60 gm) that divided into five groups; a) Normal control group, b) Dibutyl amine and sodium nitrate treated group, c)E.Coli treated group, d) Dibutyl amine and sodium nitrate treated group plus E. coli, and e) Dibutyl amine and sodium nitrate treated group plus soy bean flour. Survival rate and histopatholgical changes during the period of treatment were recorded. Level of malondialdhyde, glutathione, catalase, hydrogen peroxide, Total anti-oxidant capacity and nitric oxide were measured. RNA extracted from bladder tissues was determined in addition to P16 level and caspase-3 expression.Results: Survival analysis showed a significant decrease (p< 0.001) in E.Coli and dibutyl amine plus sodium nitrate treated groups in comparing with the normal and other treated groups. Also, E. coli infection in the bladder tissues increases the carcinogenic ability of nitrosamine precursors, and enhances oxidative and nitrosative stresses via increasing levels of nitric acid, hydrogen peroxide and malondialdhyde. Regarding the molecular changes, extra bands have been found in E. coli and E. coli + carcinogen treated groups approximately at 16-18KD which are not present in the other groups. Conclusion:Bacterial infection of the urinary bladder may play a major additive and synergistic role in bladder carcinogenesis. Our results have also shown that soy bean flour may have a protective action during induction of urinary tumors.

show abstract

Section: Discussionmentioning

confidence: 99%

Role of Urinary Tract Bacterial Infection in the Process of Bladder Carcinogenesis (Molecular and Biochemical Studies)

et al. 2011

View full text Add to dashboard Cite

show abstract

“…Primary MLFs were isolated from adult lungs (48) and were cultured in complete DMEM medium. For NO production, macrophages were stimulated with 1 μg/ml LPS, and nitrite was measured using the Griess reagent (49).…”

Section: Methodsmentioning

confidence: 99%

Noncleavable poly(ADP-ribose) polymerase-1 regulates the inflammation response in mice

Pétrilli¹,

Herceg²,

Hassa³

et al. 2004

J. Clin. Invest.

View full text Add to dashboard Cite

Poly(ADP-ribosyl)ation is rapidly formed in cells following DNA damage and is regulated by poly(ADPribose) polymerase-1 (PARP-1). PARP-1 is known to be involved in various cellular processes, such as DNA repair, genomic stability, transcription, and cell death. During apoptosis, PARP-1 is cleaved by caspases to generate 89-kDa and 24-kDa fragments, a hallmark of apoptosis. This cleavage is thought to be a regulatory event for cellular death. In order to understand the biological significance of PARP-1 cleavage, we generated a PARP-1 knockin (PARP-1 KI/KI ) mouse model, in which the caspase cleavage site of PARP-1, DEVD 214 , was mutated to render the protein resistant to caspases during apoptosis. While PARP-1 KI/KI mice developed normally, they were highly resistant to endotoxic shock and to intestinal and renal ischemia-reperfusions, which were associated with reduced inflammatory responses in the target tissues and cells due to the compromised production of specific inflammatory mediators. Despite normal binding of NF-κB to DNA, NF-κB-mediated transcription activity was impaired in the presence of caspase-resistant PARP-1. This study provides a novel insight into the function of PARP-1 in inflammation and ischemia-related pathophysiologies. IntroductionUpon DNA damage, poly(ADP-ribose) polymerase-1 (PARP-1, EC 2.4.2.30) is activated and catalyzes the formation of poly(ADPribose) (PAR) chains by transferring (ADP-ribose) from β-NAD + onto itself and nuclear acceptor proteins (1). PARP-1 is known to be involved in various cellular processes including DNA repair, recombination, genomic stability, transcription regulation, and cell death (1-3). In addition, massive poly(ADP-ribosyl)ation induced by acute DNA damage results in rapid depletion of cellular NAD + and ATP pools, which, if not regulated, can lead to cellular dysfunction and cell death (4). Involvement of PARP-1 in cell death is also speculated based on the prominent phenomenon that during apoptosis, PARP-1 is cleaved by caspases at the conserved site DEVD 214 , generating 24-kDa and 89-kDa fragments, a hallmark of apoptosis.Mice lacking PARP-1 develop normally and PARP-1 -/-fibroblasts and lymphoid cells display a normal apoptotic response after treatment with various apoptotic inducers, such as anti-Fas antibody, TNF-α, γ-radiation, and dexamethasone, which demonstrates that PARP-1 per se is dispensable for apoptosis, at least in these cell types (5, 6). However, inactivation of PARP-1 by chemical inhibitors and genetic means protects mice from endotoxic shock and other disease models related to inflammation, such as diabetes, stroke, and myocardial reperfusion (7-12). In addition, PARP inhibitors protect rats from renal and intestinal ischemia-

show abstract

“…Discrepancies between previous results and ours might be attributed to the cotreatment of IFN-␥. IFN-␥ strongly enhanced induction of NO by LPS stimulation in macrophages (14,41,51). Thus, LPS with IFN-␥ led to the production of excess NO, resulting in nitrosylation of the complexes, while NO induced by LPS alone might not be enough to repress complexes in the cells.…”

Section: Effect Of Lps On Translation In Macrophagesmentioning

confidence: 99%

Genome-wide identification and characterization of transcripts translationally regulated by bacterial lipopolysaccharide in macrophage-like J774.1 cells

Kitamura

Ito²,

Yuasa³

et al. 2008

Physiological Genomics

View full text Add to dashboard Cite

Although Escherichia coli LPS is known to elicit various proinflammatory responses in macrophages, its effect on the translational states of transcripts has not yet been explored on a genome-wide scale. To address this, we investigated the mRNA profiles in polysomal and free messenger ribonucleoprotein particle (mRNP) fractions of mouse macrophage-like J774.1 cells, using Affymetrix Mouse Genome 430 2.0 GeneChips. Comparison of the mRNA profiles in total cellular, polysomal, and free mRNP fractions enabled us to identify transcripts that were modulated at the translational level by LPS: among 19,791 transcripts, 115 and 418 were up- and downregulated at 1, 2, or 4 h after LPS stimulation (100 ng/ml) in a translation-dependent manner. Interestingly, gene ontology-based analysis suggested that translation-dependent downregulated genes frequently include those encoding proteins in the mitochondrial respiratory chain. In fact, the mRNA levels of some transcripts for complexes I, IV, and V in the mitochondrial respiratory chain were translationally downregulated, eventually contributing to the decline of their protein levels. Moreover, the amount of metabolically labeled cytochrome oxidase subunit Va in complex IV was decreased without any change of its mRNA level in total cellular fraction after LPS stimulation. Consistently, the total amounts and activities of complexes I and IV were attenuated by LPS stimulation, and the attenuation was independent of nitric oxide. These results demonstrated that translational suppression may play a critical role in the LPS-mediated attenuation of mitochondrial oxidative phosphorylation in a nitric oxide-independent manner in J774.1 cells.

show abstract

L-Arginine-dependent formation of N-nitrosamines by the cytosol of macrophages activated with lipopolysaccharide and interferon-γ

Cited by 59 publications

References 0 publications

Role of Urinary Tract Bacterial Infection in the Process of Bladder Carcinogenesis (Molecular and Biochemical Studies)

Role of Urinary Tract Bacterial Infection in the Process of Bladder Carcinogenesis (Molecular and Biochemical Studies)

Noncleavable poly(ADP-ribose) polymerase-1 regulates the inflammation response in mice

Genome-wide identification and characterization of transcripts translationally regulated by bacterial lipopolysaccharide in macrophage-like J774.1 cells

Contact Info

Product

Resources

About