Hydrogen Peroxide Is Required for Poly(phenolic) Domain Formation during Wound-Induced Suberization

Razem, Fawzi A.; Bernards, Mark A.

doi:10.1021/jf0110248

Cited by 69 publications

(45 citation statements)

References 29 publications

(51 reference statements)

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“…7). It is well known that H 2 O 2 level could represent a limiting factor in the peroxidase-catalyzed reactions leading to cross-linking of lignin and suberin polyphenolic domain (Razem and Bernards, 2002). Accordingly, G3 treatment decreases the level of polymerized phenols in the wound periderm ( Fig.…”

Section: Discussionmentioning

confidence: 95%

Involvement of Polyamine Oxidase in Wound Healing

et al. 2007

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Hydrogen peroxide (H2O2) is involved in plant defense responses that follow mechanical damage, such as those that occur during herbivore or insect attacks, as well as pathogen attack. H2O2 accumulation is induced during wound healing processes as well as by treatment with the wound signal jasmonic acid. Plant polyamine oxidases (PAOs) are H2O2 producing enzymes supposedly involved in cell wall differentiation processes and defense responses. Maize (Zea mays) PAO (ZmPAO) is a developmentally regulated flavoprotein abundant in primary and secondary cell walls of several tissues. In this study, we investigated the effect of wounding on ZmPAO gene expression in the outer tissues of the maize mesocotyl and provide evidence that ZmPAO enzyme activity, protein, and mRNA levels increased in response to wounding as well as jasmonic acid treatment. Histochemically detected ZmPAO activity especially intensified in the epidermis and in the wound periderm, suggesting a tissue-specific involvement of ZmPAO in wound healing. The role played by ZmPAO-derived H2O2 production in peroxidase-mediated wall stiffening events was further investigated by exploiting the in vivo use of N-prenylagmatine (G3), a selective and powerful ZmPAO inhibitor, representing a reliable diagnostic tool in discriminating ZmPAO-mediated H2O2 production from that generated by peroxidase, oxalate oxidase, or by NADPH oxidase activity. Here, we demonstrate that G3 inhibits wound-induced H2O2 production and strongly reduces lignin and suberin polyphenolic domain deposition along the wound, while it is ineffective in inhibiting the deposition of suberin aliphatic domain. Moreover, ZmPAO ectopic expression in the cell wall of transgenic tobacco (Nicotiana tabacum) plants strongly enhanced lignosuberization along the wound periderm, providing evidence for a causal relationship between PAO and peroxidase-mediated events during wound healing.

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Section: Discussionmentioning

confidence: 95%

Involvement of Polyamine Oxidase in Wound Healing

et al. 2007

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“…Using microsomal fractions from Vicia sativa surface tissues, Kolattukudy and colleagues Kolattukudy, 1977, 1978) demonstrated that cytochrome P450 monooxygenases (P450) are involved in the ω-hydroxylation and mid-chain hydroxylation of C16 and C18 fatty acid precursors. Additionally, studies using "wound healing" potato tuber disks as a source of suberizing tissue resulted in the characterization of an NADP-dependent oxidoreductase activity that is required for the formation of diacids from ω-hydroxyacids (Agrawal and Kolattukudy, 1978) and provided evidence for the involvement of a H 2 O 2 -dependent peroxidase in the synthesis of aromatic suberin components (Razem and Bernards, 2002;Razem and Bernards, 2003). Finally, the observed properties and fatty acid elongase (FAE) activity in corn root microsomes correlated with the expected qualitative (i.e., chain-length profile) and quantitative requirements for suberin biosynthesis along the root axis (Schreiber et al, 2005a).…”

Section: The Elucidation Of Cutin and Suberin Monomer Biosynthesismentioning

confidence: 99%

Apoplastic Diffusion Barriers in Arabidopsis

Nawrath

Schreiber

Franke

et al. 2013

The Arabidopsis Book

129

143

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During the development of Arabidopsis and other land plants, diffusion barriers are formed in the apoplast of specialized tissues within a variety of plant organs. While the cuticle of the epidermis is the primary diffusion barrier in the shoot, the Casparian strips and suberin lamellae of the endodermis and the periderm represent the diffusion barriers in the root. Different classes of molecules contribute to the formation of extracellular diffusion barriers in an organ-and tissue-specific manner. Cutin and wax are the major components of the cuticle, lignin forms the early Casparian strip, and suberin is deposited in the stage II endodermis and the periderm. The current status of our understanding of the relationships between the chemical structure, ultrastructure and physiological functions of plant diffusion barriers is discussed. Specific aspects of the synthesis of diffusion barrier components and protocols that can be used for the assessment of barrier function and important barrier properties are also presented.

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“…Peroxidase enzymes, known to catalyse the dehydrogenative polymerization of phenylpropanoids, that can lead to poly(hydroxycinnamates) or lignin, have been found systematically associated with the process of suberization (Borchert 1978;Espelie and Kolattukudy 1985;Razem and Bernards 2002). Anionic peroxidases, isolated from wound-healing potato, catalysed the polymerization of ferulic acid mainly through condensation at the b position (C-8) of the propanoid side chain (Bernards et al 1999).…”

Section: Hydroxycinnamates In Suberin Structurementioning

confidence: 99%

Hydroxycinnamates in suberin formation

Graça¹

2009

Phytochem Rev

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Hydroxycinnamates are found associated with suberin in several forms: covalently linked to the aliphatic suberin; in the residue after suberinremoval; and in the non-polar extractives of suberized tissues in the form of alkyl ferulates. Suberinassociated hydroxycinnamates have been found mainly as ferulic acid-derivatives, sometimes as feruloylamides and in a lesser extent as caffeates. Ferulic acid esters of long-chain x-hydroxyacids are prevalent in the partial depolymerisation products of suberin. Also, enzymes able to catalyze the feruloylation of x-hydroxyacids were found timely-associated with the suberization process. It is proposed that ferulic acid, and its dimers, through esterification to x-hydroxyacids, covalently link the suberin aliphatic polyester to suberin-associated polyaromatics. In this case, the known role of ferulates, and related hydroxycinnamates, as cross-linkers of structurally different polymers would be enlarged to suberized cell-walls.

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Hydrogen Peroxide Is Required for Poly(phenolic) Domain Formation during Wound-Induced Suberization

Cited by 69 publications

References 29 publications

Involvement of Polyamine Oxidase in Wound Healing

Involvement of Polyamine Oxidase in Wound Healing

Apoplastic Diffusion Barriers in Arabidopsis

Hydroxycinnamates in suberin formation

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