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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
2013 Impact Factor: 4.190
 
DOIhttp://dx.doi.org/10.1021/tx2001916
 
ISI Accession Number IDWOS:000294076200012
 
ReferencesReferences in Scopus
 
DC FieldValue
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
2013 Impact Factor: 4.190
 
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
 
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<contributor.author>Zhang, X</contributor.author>
<contributor.author>Chen, F</contributor.author>
<contributor.author>Wang, M</contributor.author>
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<description.abstract>In the present study, the dual effects of phloretin and phloridzin on methylglyoxal (MGO)-induced glycation were investigated in three N &#945;-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 &#945;-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 &#945;-acetylcysteine and PP02 was promoted by the addition of phloretin. Additional adducts, [N &#945;-acetylcysteine + 2MGO + phloretin-H 2O] and [2N &#945;-acetylcysteine + 2MGO + phloretin-2H 2O] were formed in the model composed of N &#945;-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 &#945;-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. &#169; 2011 American Chemical Society.</description.abstract>
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Author Affiliations
  1. The University of Hong Kong
  2. Peking University