Green tea polyphenol epigallocatechin-3-gallate (EGCG) induced intermolecular cross-linking of membrane proteins

Chen, Rong; Wang, Jianbo; Zhang, Xianqing; Ren, Jing; Zeng, Cheng-Ming

doi:10.1016/j.abb.2010.12.033

Cited by 85 publications

(66 citation statements)

References 35 publications

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“…Production of quinoproteins may inhibit plant growth through cross linking of membrane proteins, deactivation of enzymes, mitochondrial dysfunction, disrupting homeostasis and DNA fragmentation leading to apoptosis. [12][13][14]23) Previously, it has been reported that l-DOPA inhibited mitochondrial complex I (NADH dehydrogenase) and complex IV (cytochrome c oxidase) activities in rat and human mitochondria, respectively. 24,25) Moreover, quinoproteins from dopaminequinone induced mitochondrial swelling and permeability transition of the mitochondrial membrane and reduced complex I activity and electron transport leading to dysfunction of mitochondria in human and rat brains.…”

Section: Discussionmentioning

confidence: 99%

Bioactive l-DOPA induced quinoprotein formation to inhibit root growth of cucumber seedlings

2013

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l-DOPA (l-3,4-dihydroxyphenylalanine) is a bioactive secondary metabolite which inhibits growth of many weed species. However, its mode of action is not well elucidated in plants. The present studies were conducted to evaluate the effect of l-DOPA on root growth of cucumber (Cucumis sativus L.) and the possible involvement of quinoproteins (quinone-incorporated proteins) in phytotoxicity of l-DOPA. The results revealed that l-DOPA significantly inhibited root growth, induced cell death, increased polyphenol oxidase (PPO) activity, reduced free cysteine content, and enhanced quinoprotein formation in cucumber roots. The decrease in free cysteine content and increase in PPO activity suggested that quinones covalently bind with cysteine to form quinoproteins. The quinoproteins may be involved in phytotoxic action of l-DOPA in cucumber roots.

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Section: Discussionmentioning

confidence: 99%

Bioactive l-DOPA induced quinoprotein formation to inhibit root growth of cucumber seedlings

2013

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“…Hence, EP300 is unlikely to be a direct target of EGCG and cysteamine. However, this result reveals that the protein cross-linking activity of EGCG 17,18 can be antagonized by cysteamine. …”

Section: Effects Of Cysteamine and Egcg On Protein Acetylation And Crmentioning

confidence: 52%

Metabolic interactions between cysteamine and epigallocatechin gallate

et al. 2017

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Phase II clinical trials indicate that the combination of cysteamine plus epigallocatechin gallate (EGCG) is effective against cystic fibrosis in patients bearing the most frequent etiological mutation (CFTRDF508). Here, we investigated the interaction between both agents on cultured respiratory epithelia cells from normal and CFTRDF508-mutated donors. We observed that the combination of both agents affected metabolic circuits (and in particular the tricarboxylic acid cycle) in a unique way and that cysteamine plus EGCG reduced cytoplasmic protein acetylation more than each of the 2 components alone. In a cell-free system, protein cross-linking activity of EGCG was suppressed by cysteamine. Finally, EGCG was able to enhance the conversion of cysteamine into taurine in metabolic flux experiments. Altogether, these results indicate that multiple pharmacological interactions occur between cysteamine and EGCG, suggesting that they contribute to the unique synergy of both agents in restoring the function of mutated CFTRDF508.

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“…EGCG is reported to form covalent bonds with sulfur atoms of cysteine [72] in presence of oxidizing agents or through auto-oxidation thereby linking proteins through sulfhydrylmediated intermolecular cross-linkages. [73] FIG URE respectively. [74] Certain quinones are subjected to 1,4-Michael addition by the amine groups of proteins resulting in protein cross linkages and the process is somewhat similar for a free thiol group.…”

Section: Docking Studiesmentioning

confidence: 95%

β‐cyclodextrin encapsulated polyphenols as effective antioxidants

et al. 2017

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Formation of dityrosine (DT) cross-linkages in proteins is one of the most widely used markers of oxidative stress. Ribonuclease A (RNase A) has 6 Tyr residues and shows a characteristic DT fluorescence peak upon oxidation in addition to major changes in its secondary structure. DT formation can be prevented by using polyphenols (GA, ECG, and EGCG) which are known to have strong antioxidant activity. However, it has been observed that ECG and EGCG initiate protein oligomerization due to protein-polyphenol cross-linkages. To prevent the formation of such crosslinkages we have used b-cyclodextrin (b-CD) to encapsulate the polyphenols and studied its antioxidant properties along with that of free polyphenols. The polyphenol/b-cyclodextrin (b-CD) inclusion complexes not only prevent DT formation but also reduce protein oligomerization. This may be attributed to the fact that the quinone forming rings of ECG and EGCG become encapsulated in the cavity of b-CD and are no longer available for protein cross-linking.b-cyclodextrin encapsulation, dityrosine, oxidative stress, polyphenols, protein oligomerization | I N TR ODU C TI ONBiological aging in mammalian cells is a direct indication of oxidative stress in proteins. [1] These oxidatively modified forms of proteins are generated due to the presence of reactive oxygen species (ROS) such as hydroxyl and superoxide free radicals. [2,3] Persulfates, a key ingredient in flour, are a source of sulfate (SO 2 4 ) free radicals under neutral pH. [4,5] Due to the higher oxidizing power of the sulfate radical (E 0 5 12.60 V) and longer half-life period over the OH radical, it has drawn attention in recent times as a powerful oxidizing agent. [6][7][8] Many chemical and cosmetic industries require persulfates as their key components [9] and workers often suffer from skin and respiratory diseases due to hypersensitive reactions. [10] Generally, the lower thermal energy at room temperature (25-508C) is not sufficient enough to activate persulfate, but generation of SO 2 4 radical is facilitated in presence of metal cations. Since proteins tend to lose their structure and function at high temperatures, [11] we have carried out the oxidation of ribonuclease A (RNase A) in presence of persulfate using cobalt (II) ion at 378C. [12] Cobalt is an integral component of vitamin B12 and thus physiologically found in most tissues mainly in liver and kidney. [13,14] Gill et al., reported the formation of oligomeric species (dimer, trimer, tetramer) when RNase A was exposed to KHSO 5 in presence of metal ions such as Ni 21 and Cu 21 and the high molecular weight species were identified using SDS-PAGE. [12] An important biomarker of oxidative stress is the dityrosine moiety generated due to the covalent linkage of two Tyr residues. [15] Dityrosine bond formation is an indication of aging, and disease related problems since it generally occurs during amyloid fibril formation, [16] Parkinson disease, [17] cerebrospinal fluid damage, [18] and also in the cataract of the eye lens. [19,20] D...

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Green tea polyphenol epigallocatechin-3-gallate (EGCG) induced intermolecular cross-linking of membrane proteins

Cited by 85 publications

References 35 publications

Bioactive l-DOPA induced quinoprotein formation to inhibit root growth of cucumber seedlings

Bioactive l-DOPA induced quinoprotein formation to inhibit root growth of cucumber seedlings

Metabolic interactions between cysteamine and epigallocatechin gallate

β‐cyclodextrin encapsulated polyphenols as effective antioxidants

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