Inhibition of pectin methyl esterase activity by green tea catechins

Lewis, Kristin C.; Selzer, Tzvia; Shahar, Chen; Udi, Yael; Tworowski, Dmitry; Sagi, Irit

doi:10.1016/j.phytochem.2008.08.012

Cited by 77 publications

(60 citation statements)

References 40 publications

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“…We did not observe any phenotypic variation in the transfer (T)-DNA insertional mutants of the respective PME genes compared with the phenotype of wild-type plants, and one probable explanation for this is the known high level of genetic redundancy of PMEs (Pelloux et al, 2007;Wolf et al, 2009). To overcome this, we employed a systemic chemical inhibitor of PMEs, (-)-epigallocatechin gallate (EGCG) (Lewis et al, 2008;Wolf et al, 2012), which targets PME activity in vivo. We treated seedlings with EGCG for 4 h at a concentration of 200 μM (this concentration did not completely inhibit root growth) or by directly supplementing EGCG to Murashige-Scoog agar plates at a concentration of 100 μM for continuous growth inhibition.…”

Section: Consequences Of the Loss Of Cos 488 Binding Sites In Mature mentioning

confidence: 95%

Tracking developmentally regulated post-synthetic processing of homogalacturonan and chitin using reciprocal oligosaccharide probes

et al. 2014

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Polysaccharides are major components of extracellular matrices and are often extensively modified post-synthetically to suit local requirements and developmental programmes. However, our current understanding of the spatiotemporal dynamics and functional significance of these modifications is limited by a lack of suitable molecular tools. Here, we report the development of a novel non-immunological approach for producing highly selective reciprocal oligosaccharide-based probes for chitosan (the product of chitin deacetylation) and for demethylesterified homogalacturonan. Specific reciprocal binding is mediated by the unique stereochemical arrangement of oppositely charged amino and carboxy groups. Conjugation of oligosaccharides to fluorophores or gold nanoparticles enables direct and rapid imaging of homogalacturonan and chitosan with unprecedented precision in diverse plant, fungal and animal systems. We demonstrated their potential for providing new biological insights by using them to study homogalacturonan processing during Arabidopsis thaliana root cap development and by analyzing sites of chitosan deposition in fungal cell walls and arthropod exoskeletons.

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Section: Consequences Of the Loss Of Cos 488 Binding Sites In Mature mentioning

confidence: 95%

Tracking developmentally regulated post-synthetic processing of homogalacturonan and chitin using reciprocal oligosaccharide probes

et al. 2014

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“…Epigallocatechin gallate (EGCG) is reported to act as a competitive inhibitor to tomato PME, and the inhibitory interaction occurs at the catalytic binding site of PME via a hydrophobic interaction 23 . In this study, gallic acid and coumaric acid exhibited a mixed inhibition pattern on the PME from S. cerevisiae.…”

Section: Inhibition Kinetics Of Phenolic Acids On Pectin Methyl Esterasementioning

confidence: 99%

“…It increased from 17.8 mM to 21.0 mM in the presence of 0.1% and 0.5% coumaric acid respectively (Table IV). Ki values of EGCG and PME inhibitor (PMEI) from kiwi to tomato PME were 420 μM (measured by cyano-acetate substrate) and 0.053 μM (using citrus pectin as the substrate) respectively 9,23 and to kiwi PME with an Ki of 0.22 μM (using citrus pectin as the substrate) 3 . The Ki values of gallic acid and coumaric acid were higher than that of EGCG and kiwi PMEI.…”

Section: Inhibition Kinetics Of Phenolic Acids On Pectin Methyl Esterasementioning

confidence: 99%

Effect of Phenolic Acid on Antioxidant Activity of Wine and Inhibition of Pectin Methyl Esterase

Chen

Hou

et al. 2009

Journal of the Institute of Brewing

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Antioxidant activity, malolactic fermentation and sensory evaluation of the grape must after fermentation in the presence of gallic acid and coumaric acid, as well as the inhibitory mechanism of gallic acid and coumaric acid on pectin methyl esterase (PME), were investigated. The content of malic acid and lactic acid increased 40.4% and 36.9% compared to the control when commercial pectic enzyme (CPE) was used. The increase in malic acid content was enhanced by 64.8% and 83.4%, compared to the control in the presence of CPE + Gallic acid and CPE + Coumaric acid respectively. Ferric reducing/antioxidant power (FRAP) increased in the samples with added CPE. In addition to an increase in the FRAP, antioxidant capacity was enhanced in the CPE + Gallic acid and CPE + Coumaric acid samples. No significant differences were found in the content of total anthocyanin and in the value of sensory characteristics. The content of total flavanols increased significantly in the samples with added CPE. Lineweaver-Burk plots of PME, with gallic acid or coumaric acid, indicated that gallic acid and coumaric acid were mixed inhibitors of PME.

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“…6B3). To further demonstrate that the polar exocytosis and targeting of NtPPME1 to cell plate is ROP1-dependent, we treated BY2 cells expressing NtPPME1-GFP with 50 mM catechin-derivative (2)-epigallocatechin gallate (EGCG), a PME inhibitor (Lewis et al, 2008;Wolf et al, 2012), or coexpressed with CA-rop1 or DN-rop1, followed by confocal imaging. As shown in Supplemental Figure S8, the cell plate formation was strongly inhibited by treatment of the PME activity inhibitor EGCG, as well as by coexpression of DN-rop1 or CA-rop1.…”

Section: Rop1 Activity Controls Ntppme1 Polar Exocytic Secretion and mentioning

confidence: 99%

A Distinct Pathway for Polar Exocytosis in Plant Cell Wall Formation

et al. 2016

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Post-Golgi protein sorting and trafficking to the plasma membrane (PM) is generally believed to occur via the trans-Golgi network (TGN). In this study using Nicotiana tabacum pectin methylesterase (NtPPME1) as a marker, we have identified a TGN-independent polar exocytosis pathway that mediates cell wall formation during cell expansion and cytokinesis. Confocal immunofluorescence and immunogold electron microscopy studies demonstrated that Golgi-derived secretory vesicles (GDSVs) labeled by NtPPME1-GFP are distinct from those organelles belonging to the conventional post-Golgi exocytosis pathway. In addition, pharmaceutical treatments, superresolution imaging, and dynamic studies suggest that NtPPME1 follows a polar exocytic process from Golgi-GDSV-PM/cell plate (CP), which is distinct from the conventional Golgi-TGN-PM/CP secretion pathway. Further studies show that ROP1 regulates this specific polar exocytic pathway. Taken together, we have demonstrated an alternative TGN-independent Golgi-to-PM polar exocytic route, which mediates secretion of NtPPME1 for cell wall formation during cell expansion and cytokinesis and is ROP1-dependent.

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Inhibition of pectin methyl esterase activity by green tea catechins

Cited by 77 publications

References 40 publications

Tracking developmentally regulated post-synthetic processing of homogalacturonan and chitin using reciprocal oligosaccharide probes

Tracking developmentally regulated post-synthetic processing of homogalacturonan and chitin using reciprocal oligosaccharide probes

Effect of Phenolic Acid on Antioxidant Activity of Wine and Inhibition of Pectin Methyl Esterase

A Distinct Pathway for Polar Exocytosis in Plant Cell Wall Formation

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