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Article: Use of capillary electrophoresis to evaluate protective effects of methylglyoxal scavengers on the activity of creatine kinase
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TitleUse of capillary electrophoresis to evaluate protective effects of methylglyoxal scavengers on the activity of creatine kinase
 
AuthorsMa, J1 2
Peng, X1
Cheng, KW1
Chen, F1
Yang, D2
Chen, B2
Wang, MF1
 
KeywordsCapillary electrophoresis
Creatine kinase
Methylglyoxal
Thiols
Tiopronin
 
Issue Date2008
 
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/jss
 
CitationJournal Of Separation Science, 2008, v. 31 n. 15, p. 2846-2851 [How to Cite?]
DOI: http://dx.doi.org/10.1002/jssc.200800241
 
AbstractMethylglyoxal (MGO) is a highly reactive α-oxoaldehyde formed endogenously in numerous enzymatic and nonenzymatic reactions. The reactions between MGO and various amino residues in proteins not only result in inactivation of enzymes, but also lead to the formation of different detrimental advanced glycation endproducts (AGEs). Recently, it was reported that creatine kinase (CK, EC 2.7.3.2) activity could be reduced or even lost under incubation with MGO in vitro. In this study, an efficient CE analytical method was developed for the evaluation of CK activity. Based on this CE method, the inhibitory effect of MGO on CK activity was confirmed. Several MGO scavengers such as aminoguanidine (AG) and some thiols showed obvious protective effects on CK activity against MGO. Furthermore, tiopronin (TP), a hepatoprotective drug, was found for the first time to counteract MGO-induced inhibition of CK activity in CK reaction. Meanwhile, TP also retained adenosine diphosphate (ADP) generation level in plasma treated with MGO, which implies that this drug may have potential protective effect on other enzymes which are associated with adenine nucleotide metabolism. Besides, the established CE approach can be utilized as a model for screening effective MGO scavengers by monitoring CK-catalyzed conversion between adenosine triphosphate and ADP. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA, Weinhem.
 
ISSN1615-9306
2013 Impact Factor: 2.594
 
DOIhttp://dx.doi.org/10.1002/jssc.200800241
 
ISI Accession Number IDWOS:000258936700013
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorMa, J
 
dc.contributor.authorPeng, X
 
dc.contributor.authorCheng, KW
 
dc.contributor.authorChen, F
 
dc.contributor.authorYang, D
 
dc.contributor.authorChen, B
 
dc.contributor.authorWang, MF
 
dc.date.accessioned2010-05-31T04:16:18Z
 
dc.date.available2010-05-31T04:16:18Z
 
dc.date.issued2008
 
dc.description.abstractMethylglyoxal (MGO) is a highly reactive α-oxoaldehyde formed endogenously in numerous enzymatic and nonenzymatic reactions. The reactions between MGO and various amino residues in proteins not only result in inactivation of enzymes, but also lead to the formation of different detrimental advanced glycation endproducts (AGEs). Recently, it was reported that creatine kinase (CK, EC 2.7.3.2) activity could be reduced or even lost under incubation with MGO in vitro. In this study, an efficient CE analytical method was developed for the evaluation of CK activity. Based on this CE method, the inhibitory effect of MGO on CK activity was confirmed. Several MGO scavengers such as aminoguanidine (AG) and some thiols showed obvious protective effects on CK activity against MGO. Furthermore, tiopronin (TP), a hepatoprotective drug, was found for the first time to counteract MGO-induced inhibition of CK activity in CK reaction. Meanwhile, TP also retained adenosine diphosphate (ADP) generation level in plasma treated with MGO, which implies that this drug may have potential protective effect on other enzymes which are associated with adenine nucleotide metabolism. Besides, the established CE approach can be utilized as a model for screening effective MGO scavengers by monitoring CK-catalyzed conversion between adenosine triphosphate and ADP. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA, Weinhem.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationJournal Of Separation Science, 2008, v. 31 n. 15, p. 2846-2851 [How to Cite?]
DOI: http://dx.doi.org/10.1002/jssc.200800241
 
dc.identifier.doihttp://dx.doi.org/10.1002/jssc.200800241
 
dc.identifier.epage2851
 
dc.identifier.hkuros151445
 
dc.identifier.isiWOS:000258936700013
 
dc.identifier.issn1615-9306
2013 Impact Factor: 2.594
 
dc.identifier.issue15
 
dc.identifier.openurl
 
dc.identifier.pmid18655020
 
dc.identifier.scopuseid_2-s2.0-51549112193
 
dc.identifier.spage2846
 
dc.identifier.urihttp://hdl.handle.net/10722/60675
 
dc.identifier.volume31
 
dc.languageeng
 
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/jss
 
dc.publisher.placeGermany
 
dc.relation.ispartofJournal of Separation Science
 
dc.relation.referencesReferences in Scopus
 
dc.subjectCapillary electrophoresis
 
dc.subjectCreatine kinase
 
dc.subjectMethylglyoxal
 
dc.subjectThiols
 
dc.subjectTiopronin
 
dc.titleUse of capillary electrophoresis to evaluate protective effects of methylglyoxal scavengers on the activity of creatine kinase
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. Hunan Normal University