Hormonal Regulation, and Intracellular Localization of a 33-kD Cationic Peroxidase in Excised Cucumber Cotyledons

Abeles, Frederick B.; Hershberger, Wilbur L.; Dunn, Linda J.

doi:10.1104/pp.89.2.664

Cited by 45 publications

(21 citation statements)

References 15 publications

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“…Levels of pI 9 and pI 4 peroxidase isolated from acetone powders of seedling tissue were measured using an RID assay described earlier (2). Acetone powders of cotyledons were used to measure the peroxidases from various species of Cucurbitaceae.…”

Section: Peroxidase Assaymentioning

confidence: 99%

Hormonal Regulation and Distribution of Peroxidase Isoenzymes in the Cucurbitaceae

Abeles

Biles²,

Dunn³

1989

Plant Physiol.

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Ethylene enhanced the levels of peroxidases in the roots, stems, leaves, and cotyledons of 2-week-old cucumber Cucumis sativus cv Poinsett 76 seedlings. Antibodies to the isoelectric point (pi) 9 and pi 4 isoenzymes were used in a radial immunodiffusion assay to demonstrate that ethylene induced similar peroxidases in other cultivars of C. sativus, other species of Cucumis and other genera of Cucurbitaceae. Examination of ethylene-induced peroxidases, using isoelectric focusing gels, demonstrated the presence of a series of other peroxidases, mostly slightly acidic, whose isoelectric focusing pH was approximately 6. These pi 6 peroxidases were partially purified on a cation exchange column. Ouchterlony double diffusion gels indicated that these proteins cross-reacted with antibodies to both the pi 9 and pi 4 peroxidase. The data presented here suggest that the induction of peroxidase isoenzymes during ethyleneinduced senescence is a common response in this family of plants. In addition, antibody and isoelectric focusing studies indicate that both acidic and basic peroxidase are highly conserved in members of this family.

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Section: Peroxidase Assaymentioning

confidence: 99%

Hormonal Regulation and Distribution of Peroxidase Isoenzymes in the Cucurbitaceae

Abeles

Biles²,

Dunn³

1989

Plant Physiol.

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“…Saunders and McClure (1976) reported that many kinds of flavonoid are present in the chloroplast of many species of vascular plants. Peroxidase activity was also found in the chloroplasts of spinach leaves (Takahama, 1984), cucumber cotyledons (Abeles et al, 1989) and barley leaves (Kuroda et al, 1990). Huff (1982) demonstrated that Chl derivatives, chlorophyllide and pheophytin, as well as…”

Section: Chlorophyll Degradation Productsmentioning

confidence: 95%

Effectiveness of Various Phenolic Compounds in Degradation of Chlorophyll by In Vitro Peroxidase-Hydrogen Peroxide System

Yamauchi

Watada

1994

Engei Gakkai zasshi

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SummaryThe effectiveness of ethanol extracts from different leafy vegetables and commercial phenolic compounds in degrading chlorophyll (Ch1) in a model system using commercial horseradish peroxidase was determined in vitro.The amount of Chl degradation ranged widely among the leafy vegetables with parsley and mitsuba ethanol extracts having 70 and 60 fold greater activity than that of the garland chrysanthemum extract respectively, which were the extremes among the eight leafy vegetables.Among sixteen commercial phenolic compounds studied, Chl degradation occurred only with apigenin (flavone), apigetrin (apigenin-7-glucoside), naringenin (flavanone), p-coumaric acid (monophenol) and resorcinol (m-diphenol). These results indicate that Chl degradation in the peroxidase-hydrogen peroxide system is dependent on the type of phenol, specifically those which have a hydroxy group at the p-position.The only degraded Chl product noted in the HPLC chromatogram, when using pcoumaric acid, was 10-hydroxychlorophyll a (Chl a-1). The amount of Chl a-1 accumulated was minimal, compared to the amount Chl degraded, and implies that most of the Chl was degraded to a colorless product without the accumulation of Chl a-1 as an intermediate.

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“…It clearly implies that ICL and SAG 281 gene are involved in cotyledon senescence at the point of chloroplast (or chlorophyll) destruction together with other senescence-related enzyme coding gene's action such as various plant peroxidases [1,8,10,16,26,34]. As discussed in earlier section, Cs1-MMP may be responsible for closing the death of a cell [43].…”

Section: One Of the Cysteine Biosynthesis Involving Sag 3-5mentioning

confidence: 99%

“…From earlier senescence study in cucumber, a plant peroxidase (33-CPO) activity was promoted by ABA and JA as ethylene but was retarded by IAA, GA and kinetin from excised cotyledon [1]. They also showed induction of the peroxidase isoenzymes by both ethylene and JA following induced senescence in cucumber cotyledon.…”

Section: One Of the Cysteine Biosynthesis Involving Sag 3-5mentioning

confidence: 99%

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Response to Plant Hormones of Senescence-related Genes for Cucumis sativus L. in Cotyledon Development

Jeong¹,

Kim²

2016

Journal of Life Science

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This study was carried out to discover the response of cucumber (Cucumis sativus L.) senescence-associated genes (SAGs) to several plant hormones in detached and developing cotyledon. Accordingly, a collection of cucumber SAGs were examined to characterize their gene expression response through semi-quantitative RT-PCR. Cotyledons were excised at day 14 after seed sowing from plantlets, then incubated in 100 μM each of IAA or zeatin solution for up to 4 days in light and darkness. They were collected at 2-day intervals and used for total RNA extraction and subjected to RT-PCR. Gene expression levels of several cucumber SAGs were significantly changed during the incubation period. More than five cucumber SAGs involving SAG 60 responded to the IAA and zeatin treatment. In the ethylene response study, cotyledons were exposed up to 10 days by ethylene gas. Most of the cucumber SAGs did not show immediate response to ethylene in green cotyledon. The exceptions were PCK, SAG 158, and SAG 288 genes, which responded after 1 day of exposure to green cotyledon, while ICL and SAG 281 revealed strong responses after 10 days of being exposed to yellowing cotyledon. These results suggest that several cucumber SAGs react actively in response to starvation or senescence against exogenously applied stimulus. This induced senescence response is able to understand the SAGs role in lipids and amino acids metabolism partly and function in organ senescence during development.

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Hormonal Regulation, and Intracellular Localization of a 33-kD Cationic Peroxidase in Excised Cucumber Cotyledons

Abstract: Ethylene enhanced chlorosis and levels of 33-kilodalton cationic peroxidase

Cited by 45 publications

References 15 publications

Hormonal Regulation and Distribution of Peroxidase Isoenzymes in the Cucurbitaceae

Hormonal Regulation and Distribution of Peroxidase Isoenzymes in the Cucurbitaceae

Effectiveness of Various Phenolic Compounds in Degradation of Chlorophyll by In Vitro Peroxidase-Hydrogen Peroxide System

Response to Plant Hormones of Senescence-related Genes for Cucumis sativus L. in Cotyledon Development

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