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Article: Dual effects of phloretin and phloridzin on the glycation induced by methylglyoxal in model systems

TitleDual effects of phloretin and phloridzin on the glycation induced by methylglyoxal in model systems
Authors
Issue Date2011
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/crt
Citation
Chemical Research In Toxicology, 2011, v. 24 n. 8, p. 1304-1311 How to Cite?
Abstract
In the present study, the dual effects of phloretin and phloridzin on methylglyoxal (MGO)-induced glycation were investigated in three N α-acetyl amino acid (arginine, cysteine, and lysine) models and three N-terminal polypeptide (PP01, PP02, and PP03 containing arginine, cysteine, and lysine, respectively) models. In both N α-acetyl amino acids and N-terminal polypeptides models, the arginine residue was confirmed as the major target for modification induced by MGO. Meanwhile, MGO modification was significantly inhibited by the addition of phloretin or phloridzin via their MGO-trapping abilities, with phloretin being more effective. Interestingly, the cysteine residue was intact when solely incubated with MGO, whereas the consumption of N α-acetylcysteine and PP02 was promoted by the addition of phloretin. Additional adducts, [N α-acetylcysteine + 2MGO + phloretin-H 2O] and [2N α-acetylcysteine + 2MGO + phloretin-2H 2O] were formed in the model composed of N α-acetylcysteine, MGO, and phloretin. Another adduct, [PP02 + 2MGO + phloretin-H 2O] was observed in the model composed of PP02, MGO, and phloretin. The generation of adducts indicates that phloretin could directly participate in the modification of the cysteine residue in the presence of MGO. When creatine kinase (model protein) was exposed to MGO, the addition of phloridzin did not show a significant effect on retaining the activity of creatine kinase impaired by MGO, whereas the addition of phloretin completely inactivated creatine kinase. Results of the mass spectrometric analysis of intact creatine kinase in different models demonstrated that phloretin could directly participate in the reaction between creatine kinase and MGO, which would lead to the inactivation of creatine kinase. Furthermore, the addition of N α-acetylcysteine was found to maintain the activity of creatine kinase incubated with phloretin and MGO. These results showed that phloretin and phloridzin could inhibit the modification of the arginine residue by MGO and that phloretin could directly participate in the reaction between the thiol group and MGO. © 2011 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/140883
ISSN
2013 Impact Factor: 4.190
ISI Accession Number ID
References

 

Author Affiliations
  1. The University of Hong Kong
  2. Peking University
DC FieldValueLanguage
dc.contributor.authorMa, Jen_HK
dc.contributor.authorPeng, Xen_HK
dc.contributor.authorZhang, Xen_HK
dc.contributor.authorChen, Fen_HK
dc.contributor.authorWang, Men_HK
dc.date.accessioned2011-09-23T06:20:55Z-
dc.date.available2011-09-23T06:20:55Z-
dc.date.issued2011en_HK
dc.identifier.citationChemical Research In Toxicology, 2011, v. 24 n. 8, p. 1304-1311en_HK
dc.identifier.issn0893-228Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/140883-
dc.description.abstractIn the present study, the dual effects of phloretin and phloridzin on methylglyoxal (MGO)-induced glycation were investigated in three N α-acetyl amino acid (arginine, cysteine, and lysine) models and three N-terminal polypeptide (PP01, PP02, and PP03 containing arginine, cysteine, and lysine, respectively) models. In both N α-acetyl amino acids and N-terminal polypeptides models, the arginine residue was confirmed as the major target for modification induced by MGO. Meanwhile, MGO modification was significantly inhibited by the addition of phloretin or phloridzin via their MGO-trapping abilities, with phloretin being more effective. Interestingly, the cysteine residue was intact when solely incubated with MGO, whereas the consumption of N α-acetylcysteine and PP02 was promoted by the addition of phloretin. Additional adducts, [N α-acetylcysteine + 2MGO + phloretin-H 2O] and [2N α-acetylcysteine + 2MGO + phloretin-2H 2O] were formed in the model composed of N α-acetylcysteine, MGO, and phloretin. Another adduct, [PP02 + 2MGO + phloretin-H 2O] was observed in the model composed of PP02, MGO, and phloretin. The generation of adducts indicates that phloretin could directly participate in the modification of the cysteine residue in the presence of MGO. When creatine kinase (model protein) was exposed to MGO, the addition of phloridzin did not show a significant effect on retaining the activity of creatine kinase impaired by MGO, whereas the addition of phloretin completely inactivated creatine kinase. Results of the mass spectrometric analysis of intact creatine kinase in different models demonstrated that phloretin could directly participate in the reaction between creatine kinase and MGO, which would lead to the inactivation of creatine kinase. Furthermore, the addition of N α-acetylcysteine was found to maintain the activity of creatine kinase incubated with phloretin and MGO. These results showed that phloretin and phloridzin could inhibit the modification of the arginine residue by MGO and that phloretin could directly participate in the reaction between the thiol group and MGO. © 2011 American Chemical Society.en_HK
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/crten_HK
dc.relation.ispartofChemical Research in Toxicologyen_HK
dc.subject.meshAcetylcysteine - chemistry-
dc.subject.meshPhloretin - chemistry - metabolism-
dc.subject.meshPyruvaldehyde - chemistry - metabolism-
dc.subject.meshPhlorhizin - chemistry - metabolism-
dc.subject.meshSpectrometry, Mass, Electrospray Ionization-
dc.titleDual effects of phloretin and phloridzin on the glycation induced by methylglyoxal in model systemsen_HK
dc.typeArticleen_HK
dc.identifier.emailWang, M: mfwang@hku.hken_HK
dc.identifier.authorityWang, M=rp00800en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/tx2001916en_HK
dc.identifier.pmid21696151en_HK
dc.identifier.scopuseid_2-s2.0-80051720064en_HK
dc.identifier.hkuros192264en_US
dc.identifier.hkuros198290-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-80051720064&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume24en_HK
dc.identifier.issue8en_HK
dc.identifier.spage1304en_HK
dc.identifier.epage1311en_HK
dc.identifier.isiWOS:000294076200012-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridMa, J=9248720900en_HK
dc.identifier.scopusauthoridPeng, X=23995738500en_HK
dc.identifier.scopusauthoridZhang, X=49664372700en_HK
dc.identifier.scopusauthoridChen, F=35195539500en_HK
dc.identifier.scopusauthoridWang, M=7406691844en_HK

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