The Generation of Active Oxygen Species Differs in Tobacco and Grapevine Mesophyll Protoplasts

Papadakis, Anastasia K.; Roubelakis‐Angelakis, Kalliopi A.

doi:10.1104/pp.121.1.197

Cited by 91 publications

(60 citation statements)

References 63 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…DPI has been reported to inhibit the oxidative burst in plants (Levine et al, 1994;Cazalé et al, 1998;Papadakis and Roubelakis-Angelakis, 1999). We find that 5 m DPI effectively inhibited the deposition of GvP1 in response to Pmg, and partial inhibition was observed with 1 m. This inhibitory effect appears to be due to the supression of H 2 O 2 formation because DPI had no effect on GvP1 deposition in response to the addition of exogenous H 2 O 2 .…”

Section: Discussionmentioning

confidence: 56%

“…However, different plant species can place emphasis on different mechanisms for the production of active oxygen species in response to elicitation (Bolwell et al, 1998;Papadakis and Roubelakis-Angelakis, 1999). Our results indicate that increases in either GSH or salicylic acid are insufficient for the propagation of an oxidative burst in grapevine callus cultures.…”

Section: Discussionmentioning

confidence: 62%

See 1 more Smart Citation

Rapid Deposition of Extensin during the Elicitation of Grapevine Callus Cultures Is Specifically Catalyzed by a 40-Kilodalton Peroxidase

et al. 2001

View full text Add to dashboard Cite

Elicitation or peroxide stimulation of grape (Vitis vinifera L. cv Touriga) vine callus cultures results in the rapid and selective in situ insolubilization of an abundant and ionically bound cell wall protein-denominated GvP1. Surface-enhanced laser desorption/ionization/time of flight-mass spectrometry analysis, the amino acid composition, and the N-terminal sequence of purified GvP1 identified it as an 89.9-kD extensin. Analysis of cell walls following the in situ insolubilization of GvP1 indicates large and specific increases in the major amino acids of GvP1 as compared with the amino acids present in salt-eluted cell walls. We calculate that following deposition, covalently bound GvP1 contributes up to 4% to 5% of the cell wall dry weight. The deposition of GvP1 in situ requires peroxide and endogenous peroxidase activity. Isoelectric focusing of saline eluates of callus revealed only a few basic peroxidases that were all isolated or purified to electrophoretic homogeneity. In vitro and in situ assays of extensin cross-linking activity using GvP1 and peroxidases showed that a 40-kD peroxidase cross-linked GvP1 within minutes, whereas other grapevine peroxidases had no significant activity with GvP1. Internal peptide sequences indicated this extensin peroxidase (EP) is a member of the class III peroxidases. We conclude that we have identified and purified an EP from grapevine callus that is responsible for the catalysis of GvP1 deposition in situ during elicitation. Our results suggest that GvP1 and this EP play an important combined role in grapevine cell wall defense.

show abstract

Section: Discussionmentioning

confidence: 56%

Section: Discussionmentioning

confidence: 62%

Rapid Deposition of Extensin during the Elicitation of Grapevine Callus Cultures Is Specifically Catalyzed by a 40-Kilodalton Peroxidase

et al. 2001

View full text Add to dashboard Cite

show abstract

“…The ammonium was quantified by preparing a standard curve with ammonium nitrate. The production of O 2 .ÿ and H 2 O 2 from V. vinifera cv Sultanina cell cultures was determined by the chemiluminescence assay of luminol and lucigenin, respectively, in cells and in the culture medium as already described (Papadakis and Roubelakis-Angelakis, 1999). Three independent experiments, with three replicates each, were performed.…”

Section: Ammonia Extraction and Determinationmentioning

confidence: 99%

Abiotic Stress Generates ROS That Signal Expression of Anionic Glutamate Dehydrogenases to Form Glutamate for Proline Synthesis in Tobacco and Grapevine

et al. 2006

Self Cite

View full text Add to dashboard Cite

Glutamate dehydrogenase (GDH) may be a stress-responsive enzyme, as GDH exhibits considerable thermal stability, and de novo synthesis of the a-GDH subunit is induced by exogenous ammonium and senescence. NaCl treatment induces reactive oxygen species (ROS), intracellular ammonia, expression of tobacco (Nicotiana tabacum cv Xanthi) gdh-NAD;A1 encoding the a-subunit of GDH, increase in immunoreactive a-polypeptide, assembly of the anionic isoenzymes, and in vitro GDH aminating activity in tissues from hypergeous plant organs. In vivo aminating GDH activity was confirmed by gas chromatorgraphy-mass spectrometry monitoring of 15 N-Glu, 15 N-Gln, and 15 N-Pro in the presence of methionine sulfoximine and amino oxyacetic acid, inhibitors of Gln synthetase and transaminases, respectively. Along with upregulation of a-GDH by NaCl, isocitrate dehydrogenase genes, which provide 2-oxoglutarate, are also induced. Treatment with menadione also elicits a severalfold increase in ROS and immunoreactive a-polypeptide and GDH activity. This suggests that ROS participate in the signaling pathway for GDH expression and protease activation, which contribute to intracellular hyperammonia. Ammonium ions also mimic the effects of salinity in induction of gdh-NAD;A1 expression. These results, confirmed in tobacco and grape (Vitis vinifera cv Sultanina) tissues, support the hypothesis that the salinity-generated ROS signal induces a-GDH subunit expression, and the anionic isoGDHs assimilate ammonia, acting as antistress enzymes in ammonia detoxification and production of Glu for Pro synthesis.

show abstract

“…Lucigenin-based luminescence assays were adapted from Papadakis and RoubelakisAngelakis (Papadakis and Roubelakis-Angelakis, 1999). Six to 7 cmlong (from the apex) pieces were placed in the recording cuvette with 2 ml of control assay solution (mM: 0.5 CaCl2, 1 EDTA, 10 Tris, pH 8.7).…”

Section: Luminometrymentioning

confidence: 99%

Free oxygen radicals regulate plasma membrane Ca2+- and K+-permeable channels in plant root cells

Demidchik

Shabala

Coutts

et al. 2003

Journal of Cell Science

327

265

View full text Add to dashboard Cite

Free oxygen radicals are an irrefutable component of life, underlying important biochemical and physiological phenomena in animals. Here it is shown that free oxygen radicals activate plasma membrane Ca2+- and K+-permeable conductances in Arabidopsis root cell protoplasts, mediating Ca2+ influx and K+ efflux,respectively. Free oxygen radicals generate increases in cytosolic Ca2+ mediated by a novel population of nonselective cation channels that differ in selectivity and pharmacology from those involved in toxic Na+ influx. Analysis of the free oxygen radical-activated K+ conductance showed its similarity to the Arabidopsisroot K+ outward rectifier. Significantly larger channel activation was found in cells responsible for perceiving environmental signals and undergoing elongation. Quenching root free oxygen radicals inhibited root elongation, confirming the role of radical-activated Ca2+ influx in cell growth. Net free oxygen radical-stimulated Ca2+ influx and K+ efflux were observed in root cells of monocots, dicots, C3 and C4 plants, suggesting conserved mechanisms and functions. In conclusion, two functions for free oxygen radical cation channel activation are proposed:initialization/amplification of stress signals and control of cell elongation in root growth.

show abstract

The Generation of Active Oxygen Species Differs in Tobacco and Grapevine Mesophyll Protoplasts

Cited by 91 publications

References 63 publications

Rapid Deposition of Extensin during the Elicitation of Grapevine Callus Cultures Is Specifically Catalyzed by a 40-Kilodalton Peroxidase

Rapid Deposition of Extensin during the Elicitation of Grapevine Callus Cultures Is Specifically Catalyzed by a 40-Kilodalton Peroxidase

Abiotic Stress Generates ROS That Signal Expression of Anionic Glutamate Dehydrogenases to Form Glutamate for Proline Synthesis in Tobacco and Grapevine

Free oxygen radicals regulate plasma membrane Ca2+- and K+-permeable channels in plant root cells

Contact Info

Product

Resources

About