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

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TitleDual effects of phloretin and phloridzin on the glycation induced by methylglyoxal in model systems
AuthorsMa, J1
Peng, X1
Zhang, X1
Chen, F1 2
Wang, M1
Issue Date2011
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/crt
CitationChemical Research In Toxicology, 2011, v. 24 n. 8, p. 1304-1311 [How to Cite?]
DOI: http://dx.doi.org/10.1021/tx2001916
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.
ISSN0893-228X
2011 Impact Factor: 3.779
2011 SCImago Journal Rankings: 0.337
DOIhttp://dx.doi.org/10.1021/tx2001916
ISI Accession Number IDWOS:000294076200012
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorMa, J
dc.contributor.authorPeng, X
dc.contributor.authorZhang, X
dc.contributor.authorChen, F
dc.contributor.authorWang, M
dc.date.accessioned2011-09-23T06:20:55Z
dc.date.available2011-09-23T06:20:55Z
dc.date.issued2011
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.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationChemical Research In Toxicology, 2011, v. 24 n. 8, p. 1304-1311 [How to Cite?]
DOI: http://dx.doi.org/10.1021/tx2001916
dc.identifier.doihttp://dx.doi.org/10.1021/tx2001916
dc.identifier.epage1311
dc.identifier.hkuros192264
dc.identifier.hkuros198290
dc.identifier.isiWOS:000294076200012
dc.identifier.issn0893-228X
2011 Impact Factor: 3.779
2011 SCImago Journal Rankings: 0.337
dc.identifier.issue8
dc.identifier.pmid21696151
dc.identifier.scopuseid_2-s2.0-80051720064
dc.identifier.spage1304
dc.identifier.urihttp://hdl.handle.net/10722/140883
dc.identifier.volume24
dc.languageeng
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/crt
dc.publisher.placeUnited States
dc.relation.ispartofChemical Research in Toxicology
dc.relation.referencesReferences in Scopus
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 systems
dc.typeArticle
Author Affiliations
  1. The University of Hong Kong
  2. Peking University