Hydrogen peroxide affects ion channels in lily pollen grain protoplasts

Plant Biology ◽  
2016 ◽  
Vol 18 (5) ◽  
pp. 761-767 ◽  
Author(s):  
M. A. Breygina ◽  
D. V. Abramochkin ◽  
N. M. Maksimov ◽  
I. P. Yermakov
Keyword(s):  
Hydrogen Peroxide ◽  
Ion Channels ◽  
Pollen Grain ◽  
Lily Pollen

Changes in the composition of ionogenic groups of the wall of the lily pollen grain during germination

2009 ◽  
Vol 56 (2) ◽  
pp. 211-218 ◽  
Author(s):  
N. R. Meychik ◽  
A. V. Smirnova ◽  
N. P. Matveeva ◽  
Yu. I. Nikolaeva ◽  
I. P. Ermakov
Keyword(s):  
Pollen Grain ◽  
Ionogenic Groups ◽  
Lily Pollen

Molecular and physiological characterisation of a 14-3-3 protein from lily pollen grains regulating the activity of the plasma membrane H + ATPase during pollen grain germination and tube growth

Planta ◽  
2001 ◽  
Vol 213 (1) ◽  
pp. 132-141 ◽  
Author(s):  
Heidi Pertl ◽  
Martin Himly ◽  
Renate Gehwolf ◽  
Rosa Kriechbaumer ◽  
Doris Strasser ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Pollen Grains ◽  
Pollen Grain ◽  
Tube Growth ◽  
Pollen Grain Germination ◽  
Lily Pollen

scholarly journals TRPM2 ion channels steer neutrophils towards a source of hydrogen peroxide

2021 ◽  
Author(s):  
Hassan Morad ◽  
Suaib Luqman ◽  
Chun-Hsiang Tan ◽  
Victoria Swann ◽  
Peter A. McNaughton
Keyword(s):  
Hydrogen Peroxide ◽  
Ion Channels ◽  
Calcium Influx ◽  
Thermal Sensitivity ◽  
Leading Edge ◽  
Neutrophil Chemotaxis ◽  
Small Temperature

AbstractNeutrophils must navigate accurately towards pathogens in order to destroy invaders and thus defend our bodies against infection. Here we show that hydrogen peroxide, a potent neutrophil chemoattractant, guides chemotaxis by activating calcium-permeable TRPM2 ion channels and thus generating an intracellular leading-edge calcium “pulse”. The thermal sensitivity of TRPM2 activation means that chemotaxis towards hydrogen peroxide is strongly promoted by small temperature elevations, suggesting that an important function of fever may be to enhance neutrophil chemotaxis by facilitating calcium influx through TRPM2. Chemotaxis towards conventional chemoattractants such as LPS, CXCL2 and C5a does not depend on TRPM2 but is driven in a similar way by leading-edge calcium pulses. Other proposed initiators of neutrophil movement, such as PI3K, Rac and lyn, influence chemotaxis by modulating the amplitude of calcium pulses. We propose that intracellular leading-edge calcium pulses are universal drivers of the motile machinery involved in neutrophil chemotaxis.

scholarly journals TRPM2 ion channels steer neutrophils towards a source of hydrogen peroxide

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Hassan Morad ◽  
Suaib Luqman ◽  
Chun-Hsiang Tan ◽  
Victoria Swann ◽  
Peter A. McNaughton
Keyword(s):  
Hydrogen Peroxide ◽  
Ion Channels ◽  
Calcium Influx ◽  
Thermal Sensitivity ◽  
Leading Edge ◽  
Neutrophil Chemotaxis ◽  
Small Temperature

AbstractNeutrophils must navigate accurately towards pathogens in order to destroy invaders and thus defend our bodies against infection. Here we show that hydrogen peroxide, a potent neutrophil chemoattractant, guides chemotaxis by activating calcium-permeable TRPM2 ion channels and generating an intracellular leading-edge calcium “pulse”. The thermal sensitivity of TRPM2 activation means that chemotaxis towards hydrogen peroxide is strongly promoted by small temperature elevations, suggesting that an important function of fever may be to enhance neutrophil chemotaxis by facilitating calcium influx through TRPM2. Chemotaxis towards conventional chemoattractants such as LPS, CXCL2 and C5a does not depend on TRPM2 but is driven in a similar way by leading-edge calcium pulses. Other proposed initiators of neutrophil movement, such as PI3K, Rac and lyn, influence chemotaxis by modulating the amplitude of calcium pulses. We propose that intracellular leading-edge calcium pulses are universal drivers of the motile machinery involved in neutrophil chemotaxis.

scholarly journals Control of Guard Cell Ion Channels by Hydrogen Peroxide and Abscisic Acid Indicates Their Action through Alternate Signaling Pathways

2003 ◽  
Vol 131 (2) ◽  
pp. 385-388 ◽  
Author(s):  
Barbara Köhler ◽  
Adrian Hills ◽  
Michael R. Blatt
Keyword(s):  
Hydrogen Peroxide ◽  
Abscisic Acid ◽  
Ion Channels ◽  
Signaling Pathways ◽  
Guard Cell

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.

An Electrophysiological Study Of The Effects Of Propofol On Native Neuronal Ligand-Gated Ion Channels

2001 ◽  
Vol 28 (5-6) ◽  
pp. 451-458 ◽  
Author(s):  
Debra Patten ◽  
Graham R Foxon ◽  
Keith F Martin ◽  
Robert F Halliwell
Keyword(s):  
Ion Channels ◽  
Electrophysiological Study ◽  
Gated Ion Channels ◽  
Ligand Gated Ion Channels
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