Impact of Mycoplasma hyorhinis infection on l-arginine metabolism: differential regulation of the human and murine iNOS gene
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Guido Kagemann
Abstract
Infection with mycoplasma is a common problem in cell cultures, with Mycoplasma hyorhinis being the predominant species. Here we investigate the effect of M. hyorhinis infection on L-arginine metabolism, with focus on iNOS-mediated NO synthesis in murine keratinocytes and the human colon cancer cell line DLD-1. iNOS and arginase are L-arginine-metabolizing enzymes involved in the regulation of inflammatory processes, with NO contributing to innate immunity. In murine cells, M. hyorhinis infection enhances cytokine-induced iNOS expression and augments iNOS activity, whereas in the absence of cytokines it causes de novo induction of iNOS mRNA without subsequent translation into iNOS protein. In turn, arginase-1 mRNA expression is diminished in M. hyorhinis-infected murine keratinocytes, resulting in decreased arginase activity. One of the underlying upstream mechanisms is NF-κB activation. In contrast, in human cells neither iNOS mRNA nor protein expression is affected by M. hyorhinis infection, but NO synthesis is enhanced, which may be caused by increased L-arginine import. This demonstrates that infection with M. hyorhinis leads to different effects on gene regulation of the murine and human iNOS gene. Our study underlines the importance of routine checking of cell cultures for mycoplasma contamination, particularly in studies on NO-mediated effects or inflammatory processes.
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Articles in the same Issue
- Highlight: Radicals in Enzymatic Catalysis
- Radical-mediated dehydration reactions in anaerobic bacteria
- Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster
- Structural and functional comparison of HemN to other radical SAM enzymes
- New glycyl radical enzymes catalysing key metabolic steps in anaerobic bacteria
- Unusual reactions involved in anaerobic metabolism of phenolic compounds
- Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism
- Spectroscopic and theoretical approaches for studying radical reactions in class I ribonucleotide reductase
- Biomimetic metal-radical reactivity: aerial oxidation of alcohols, amines, aminophenols and catechols catalyzed by transition metal complexes
- Combinatorial approaches to functional models for galactose oxidase
- Spectroscopic characterization of the iron-oxo intermediate in cytochrome P450
- Impact of Mycoplasma hyorhinis infection on l-arginine metabolism: differential regulation of the human and murine iNOS gene
- Degradation of the sodium taurocholate cotransporting polypeptide (NTCP) by the ubiquitin-proteasome system
- Identification of three novel mutations in the dihydropyrimidine dehydrogenase gene associated with altered pre-mRNA splicing or protein function
Articles in the same Issue
- Highlight: Radicals in Enzymatic Catalysis
- Radical-mediated dehydration reactions in anaerobic bacteria
- Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster
- Structural and functional comparison of HemN to other radical SAM enzymes
- New glycyl radical enzymes catalysing key metabolic steps in anaerobic bacteria
- Unusual reactions involved in anaerobic metabolism of phenolic compounds
- Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism
- Spectroscopic and theoretical approaches for studying radical reactions in class I ribonucleotide reductase
- Biomimetic metal-radical reactivity: aerial oxidation of alcohols, amines, aminophenols and catechols catalyzed by transition metal complexes
- Combinatorial approaches to functional models for galactose oxidase
- Spectroscopic characterization of the iron-oxo intermediate in cytochrome P450
- Impact of Mycoplasma hyorhinis infection on l-arginine metabolism: differential regulation of the human and murine iNOS gene
- Degradation of the sodium taurocholate cotransporting polypeptide (NTCP) by the ubiquitin-proteasome system
- Identification of three novel mutations in the dihydropyrimidine dehydrogenase gene associated with altered pre-mRNA splicing or protein function
