scholarly journals OxyR-Like Improve Cell's Hydrogen Peroxide Tolerance via Participate in Monocyte Chemotaxis and Oxidative Phosphorylation Regulation in Magnetospirillum Gryphiswaldense MSR-1

2021 ◽  
Keyword(s):  
Hydrogen Peroxide ◽  
Oxidative Phosphorylation ◽  
Full Text ◽  
Magnetospirillum Gryphiswaldense ◽  
Monocyte Chemotaxis

Abstract The full text of this preprint has been withdrawn, as it was submitted in error. Therefore, the authors do not wish this work to be cited as a reference. Questions should be directed to the corresponding author.

scholarly journals OxyR-Like Improve Cell's Hydrogen Peroxide Tolerance via Participate in Monocyte Chemotaxis and Oxidative Phosphorylation Regulation in Magnetospirillum Gryphiswaldense MSR-1

2020 ◽  
Author(s):  
Yong Ma ◽  
Tong Wen ◽  
Yunpeng Zhang ◽  
Fangfang Guo ◽  
Xiuyu Sun ◽  
...  
Keyword(s):  
Oxidative Phosphorylation ◽  
Metabolic Regulation ◽  
Regulation System ◽  
Magnetospirillum Gryphiswaldense ◽  
System A ◽  
Complex Process ◽  
Defective Mutant ◽  
Genes Encoding ◽  
Chemotaxis Proteins ◽  
Monocyte Chemotaxis

Abstract Magnetosome formation inside magnetotactic bacteria is a complex process strictly regulated by intracellular metabolic regulation system. A series of transcriptional regulators have been proved involved in magnetosome bio-synthesis, including OxyR-Like, which is indispensable during magnetosome maturation in Magnetospirillum gryphiswaldense MSR-1. In this study, a new function of OxyR-Like was identified that it helps cell to defense reactive oxygen species (ROS). Comparison of expression profile data between wild type MSR-1 and oxyR-Like defective mutant demonstrate that after the disruption of oxyR-Like, 7 genes encoding chemotaxis proteins were down-regulated. On the contrary, the expression level of numerous genes encoding proteins which are critical for cellular aerobic respiration are increased. The result suggesting a model that OxyR-Like enhance the cell’s ROS resistant ability via increasing its environmental perception and keeping its oxidative phosphorylation in a reasonable level to avoid excessive production of endogenous ROS. This study further enriched the regulatory network of OxyR-Like and established the relationship between antioxidant metabolism pathway and magnetosome biomineralization in MSR-1.

OxyR-Like Improves Cell Hydrogen Peroxide Tolerance by Participating in Monocyte Chemotaxis and Oxidative Phosphorylation Regulation in Magnetospirillum Gryphiswaldense MSR-1

2021 ◽  
Vol 17 (12) ◽  
pp. 2466-2476
Author(s):  
Yong Ma ◽  
Fangfang Guo ◽  
Yunpeng Zhang ◽  
Xiuyu Sun ◽  
Tong Wen ◽  
...  
Keyword(s):  
Oxidative Phosphorylation ◽  
Regulatory System ◽  
Wild Type ◽  
Magnetospirillum Gryphiswaldense ◽  
System A ◽  
Complex Process ◽  
Defective Mutant ◽  
Genes Encoding ◽  
Chemotaxis Proteins ◽  
Monocyte Chemotaxis

The formation of magnetosomes inside magnetotactic bacteria is a complex process strictly controlled by the intracellular metabolic regulatory system. A series of transcriptional regulators are involved in the biosynthesis of the magnetosome, including OxyR-Like protein, which is indispensable for the maturation of magnetosomes in Magnetospirillum Gryphiswaldense MSR-1. In this study, a new function of the OxyR-Like protein that helps cells resist reactive oxygen species (ROS) was identified. A comparison of expression profile data between wild-type MSR-1 and an oxyR-Like defective mutant demonstrated that seven genes encoding chemotaxis proteins were down-regulated in the latter. On the contrary, the expression levels of numerous genes encoding proteins that are critical for cellular aerobic respiration were up-regulated. Thus, OxyR-Like enhanced the resistance of cells to ROS by increasing their environmental perception and maintaining their oxidative phosphorylation at a reasonable level to avoid the excessive production of endogenous ROS. These results increase our knowledge of the OxyR-Like regulatory network and establish a relationship between the antioxidant metabolic pathway and magnetosome biomineralization in MSR-1.

Mesosomes, Unique Membranous Structures in Bacteria

2014 ◽  
Vol 894 ◽  
pp. 316-320
Author(s):  
Xin Li ◽  
Li Peng Yang ◽  
Wen Xue Zhu ◽  
Xin Yue Pang ◽  
Han Qing Feng
Keyword(s):  
Hydrogen Peroxide ◽  
Cell Division ◽  
Oxidative Phosphorylation ◽  
Functional Properties ◽  
Cell Injury ◽  
Functional Performance ◽  
Cellular Processes

Mesosomes are unique membranous bacterial structures that actively function in cell injury and physiological cellular processes, such as replication and separation of nucleoids and oxidative phosphorylation. The structures and functions of mesosomes have been studied and identified, but the regulation of their functional properties remains still unclear. Our previous studies confirmed that hydrogen peroxide (H2O2) is involved in mesosome formation during cell injury and cell division processes. The quantity of excess H2O2accumulation is associated with the mesosome size. This observation has provided great significance in elucidating the mechanisms of maintainance of the functional performance of mesosomes. This article describes the bacterial mesosome and its functions as well as the involvement of H2O2in mediating these functions.

scholarly journals MENINGKATNYA HIDROGEN PEROKSIDA PADA VARIAN T16189C mtDNA SEMEN MANUSIA

2006 ◽  
Vol 11 (2) ◽  
pp. 173-177
Author(s):  
Sudjarwo Sudjarwo
Keyword(s):  
Reactive Oxygen Species ◽  
Hydrogen Peroxide ◽  
Oxidative Phosphorylation ◽  
Enzymatic Reaction ◽  
Cellular Respiration ◽  
Oxygen Species ◽  
Spermatozoa Motility ◽  
Significant Difference ◽  
Pcr Rflp ◽  
A Site

Mitochondria are a site of cellular respiration through oxidative phosphorylation enzymatic reaction (OXPHOS), which is producing energy in the form of ATP (Adenosine Triphosphate). If abnormalities occur along cellular respiratory chain, ATP will decrease and Reactive Oxygen Species (ROS), will increase, one of which is hydrogen peroxide. ROS is an oxidation whose targets are lipid, protein and DNA, all of which may result in the decrease of spermatozoa motility. The detection of hydrogen peroxide was conducted by means of chemiluminescence using luminol, while the detection T16189C mtDNA variant was done using PCR-RFLP with restriction enzyme MnLI. In normozoospermia, hydrogen peroxide in 16189T was 4.4 1.8 CPM/106 sp and in 16189C was 6.4 1.8 CPM/106 sp. In asthenozoospermia, hydrogen peroxide in 16189T was 20.3 8.3 CPM/106 sp while in 16189C was 62.5 9.0 CPM/106 sp. Hydrogen peroxide in normozoospermia and asthenozoospermia 16189T and 16189C showed significant difference (p less than 0.00; p less than 0.01). In normozoospermia and asthenozoospermia, 16189T and 16189C has correlation with the decrease of motile spermatozoa motility (normozoospermia, p = 0.02; p less than 0.05; asthenozoospermia p = 0.03; p less than 0.05).

Peroxidase Localization in Hartmanella Trophozoites

1971 ◽  
Vol 29 ◽  
pp. 346-347 ◽  
Author(s):  
George E. Childs ◽  
Joseph H. Miller
Keyword(s):  
Hydrogen Peroxide ◽  
Ultrastructural Localization ◽  
Pathogenic Strain ◽  
Oxidative Enzymes ◽  
Differential Centrifugation ◽  
Electron Microscopic ◽  
Microscopic Studies ◽  
The Subject ◽  
Axenic Cultures

Biochemical and differential centrifugation studies have demonstrated that the oxidative enzymes of Acanthamoeba sp. are localized in mitochondria and peroxisomes (microbodies). Although hartmanellid amoebae have been the subject of several electron microscopic studies, peroxisomes have not been described from these organisms or other protozoa. Cytochemical tests employing diaminobenzidine-tetra HCl (DAB) and hydrogen peroxide were used for the ultrastructural localization of peroxidases of trophozoites of Hartmanella sp. (A-l, Culbertson), a pathogenic strain grown in axenic cultures of trypticase soy broth.

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

Protective effect of chitooligosaccharides on hydrogen peroxide-induced PC-12 cells death by inhibition of oxidative damage

2010 ◽  
Vol 34 (8) ◽  
pp. S27-S27
Author(s):  
Xueling Dai ◽  
Ping Chang ◽  
Ke Xu ◽  
Changjun Lin ◽  
Hanchang Huang ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Oxidative Damage ◽  
Protective Effect ◽  
Pc 12 Cells ◽  
Cells Death

Signal-regulated oxidation of proteins via MICAL

2020 ◽  
Vol 48 (2) ◽  
pp. 613-620
Author(s):  
Clara Ortegón Salas ◽  
Katharina Schneider ◽  
Christopher Horst Lillig ◽  
Manuela Gellert
Keyword(s):  
Signal Transduction ◽  
Hydrogen Peroxide ◽  
Cell Death ◽  
Redox Regulation ◽  
Signal Transduction Pathways ◽  
Cellular Functions ◽  
Intracellular Signals ◽  
Amino Acid Side Chains ◽  
Specific Receptors ◽  
Sulfur Containing

Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.

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