Inhibition by Salicylhydroxamic Acid, BW755C, Eicosatetraynoic Acid, and Disulfiram of Hypersensitive Resistance Elicited by Arachidonic Acid or Poly-l-Lysine in Potato Tuber

Preisig, Carol L.; Kúc, J.

doi:10.1104/pp.84.3.891

Cited by 51 publications

(24 citation statements)

References 21 publications

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“…syringae pv phaseolicola (5), et al). Preisig and Kuc (19) suggested that LOX plays a role in the hypersensitive reaction of potato to Phytophthora infestans induced by arachidonic acid. The present study provides correlative evidence for an important role of LOX in plant disease resistance.…”

Section: Antifungal Activities Of Hydroperoxy and Hydroxy Fatty Acidsmentioning

confidence: 99%

A Lipoxygenase Pathway Is Activated in Rice after Infection with the Rice Blast Fungus Magnaporthe grisea

Ohta¹,

Shida²,

Peng³

et al. 1991

Plant Physiol.

111

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Lipoxygenase (LOX) and lipid hydroperoxide-decomposing activity (LHDA) markedly increased in the fifth leaves of rice (Oryza sativa cv Aichiasahi) after infection with the rice blast fungus, Magnaporthe grisea. The increases in the enzyme activities were significantly higher in response to infection with an incompatible strain (race 131) compared with infection with a compatible strain (race 007) of the fungus. Using ion-exchange chromatography, we isolated three LOX activities (leaf LOX-1, -2, -3) from both uninoculated and infected leaves. The activity of leaf LOX-3, in particular, increased in the incompatible race-infected leaves. The leaf LOX-3 had a pH optimum of 5.0 and produced preferentially 13-L-hydroperoxy-9,11 (Z,E)-octadecadienoic acid (13-HPODD) from linoleic acid. 13-HPODD and 13-L-hydroxy-9,11 (Z,E)-octadecadienoic acid, one of the reaction products from 13-HPODD by LHDA, were highly inhibitory to the germination of conidia of the fungus. The present study provides correlative evidence for important roles of LOX and LHDA in the resistance response of rice against the blast fungus.Rice (Oryza sativa) blast, caused by Magnaporthe grisea, is one of the most destructive rice diseases. Many studies have been concerned with resistance mechanisms of rice to the blast fungus, and, thus, several antifungal substances have been isolated from rice leaves (1, 4, 9-1 1, 14). However, the biosynthetic mechanisms of these substances in fungal-infected leaves have not been established. Therefore, it is not known whether the antifungal substances isolated from rice leaves are actually involved in the defense response of rice against the fungus.We recently found an activity that decomposed lipid hy-

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Section: Antifungal Activities Of Hydroperoxy and Hydroxy Fatty Acidsmentioning

confidence: 99%

A Lipoxygenase Pathway Is Activated in Rice after Infection with the Rice Blast Fungus Magnaporthe grisea

Ohta¹,

Shida²,

Peng³

et al. 1991

Plant Physiol.

111

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“…Firstly, arachidonic acid induces phytoalexin biosynthesis (Bloch et al, 1984) and hypersensitive cell death (Davis and Currier, 1988) in potato tubers. It has been proposed that the elicitor activity of arachidonic acid occurs through the action of lipoxygenase on this exogenous PUFA (Preisig and Kuc, 1987). Indeed, lipid hydroperoxides and their secondary derivatives such as free radicals, can exert deleterious effects on membranes, leading to cell death.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of elicitor‐induced lipoxygenase in tobacco cells

et al. 1993

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SummaryLipoxygenase activity was induced in a tobacco cell suspension culture by treatment with glycopeptide elicitors prepared from the cell walls of Phytophthora parasitica var, nicotianae, and in tobacco seedlings infected by this fungal pathogen. Upon purification and characterization, the enzyme appeared to have a molecular weight of 96000, a pl of 5.1 and a Km of 20.9 μM with linoleic acid as substrate. According to its acidic optimum pH, it belongs to type‐2 lipoxygenases. Using linoleic, linolenic and arachidonic acids as substrates, the products formed in vitro by lipoxygenase were characterized. 9‐ and 5‐hydroperoxides were the main products obtained from the C18 and C20 fatty acids, respectively, thereby indicating that a 5‐lipoxygenase accounts for most of the elicitor‐induced activity, since the main site of insertion of molecular oxygen is on C‐5 of arachidonic acid. Small amounts of 13‐hydroperoxides were also formed from the C18 fatty acids. In vitro, the strongest inhibitors of tobacco lipoxygenase were n‐propylgallate and nordihydroguaiaretic acid. The possible involvement of this enzyme in signaling phenomena leading to defense induction in plants via jasmonic acid and other fatty acid‐derived products is discussed.

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“…Plants have different LOX isoforms with different catalytic specificities, but the factors that regulate the expression of these isoforms are largely unknown (12,18,34). Various roles have been proposed for LOXs that include a role in plant growth and development, senescence, and defense against insects and pathogens (7,17,18,28,34), although definitive proof for any of these is lacking. The normal substrates for plant LOXs are linoleic and linolenic acids, and LOX products of these fatty acids are metabolized to compounds that may function as signal molecules.…”

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confidence: 99%

Rapid Stimulation of 5-Lipoxygenase Activity in Potato by the Fungal Elicitor Arachidonic Acid

Bostock¹,

Yamamoto²,

Choi³

et al. 1992

Plant Physiol.

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The activity of lipoxygenase (LOX) in aged potato tuber discs increased by almost 2-fold following treatment of the discs with the fungal elicitor arachidonic acid (AA). Enzyme activity increased above that in untreated discs within 30 min after AA treatment, peaked at 1 to 3 h, and returned to near control levels by 6 h. The majority of the activity was detected in a soluble fraction (105,000g supernatant), but a minor portion was also associated with a particulate fraction enriched in microsomal membranes (105,000g pellet); both activities were similarly induced. 5-Hydroperoxyeicosatetraenoic acid was the principal product following incubation of these extracts with AA. Antibodies to soybean LOX strongly reacted with a protein with a molecular mass of approximately 95-kD present in both soluble and particulate fractions whose abundance generally corresponded with LOX activity in extracts. LOX activity was not enhanced by treatment of the discs with nonelicitor fatty acids or by branched ,-glucans from the mycelium of Phytophthora infestans. Prior treatment of the discs with abscisic acid, salicylhydroxamic acid, or n-propyl gallate, all of which have been shown to suppress AA induction of the hypersensitive response, inhibited the AA-induced increment in LOX activity. Cycloheximide pretreatment, which abolishes AA elicitor activity for other responses such as phytoalexin induction, did not inhibit LOX activity in water-or elicitor-treated discs but enhanced activity similar to that observed by AA treatment. The elicitor-induced increase in 5-LOX activity preceded or temporally paralleled the induction of other studied responses to AA, including the accumulation of mRNAs for 3-hydroxy-3-methylglutaryl coenzyme A reductase and phenylalanine ammonia lyase reported here. The results are discussed in relation to the proposed role of the 5-LOX in signalresponse coupling of arachidonate elicitation of the hypersensitive response.During the past several years, considerable progress has been made in the molecular characterization of plant LOXs3

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Inhibition by Salicylhydroxamic Acid, BW755C, Eicosatetraynoic Acid, and Disulfiram of Hypersensitive Resistance Elicited by Arachidonic Acid or Poly-l-Lysine in Potato Tuber

Cited by 51 publications

References 21 publications

A Lipoxygenase Pathway Is Activated in Rice after Infection with the Rice Blast Fungus Magnaporthe grisea

A Lipoxygenase Pathway Is Activated in Rice after Infection with the Rice Blast Fungus Magnaporthe grisea

Purification and characterization of elicitor‐induced lipoxygenase in tobacco cells

Rapid Stimulation of 5-Lipoxygenase Activity in Potato by the Fungal Elicitor Arachidonic Acid

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