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
2011 Impact Factor: 2.733
2011 SCImago Journal Rankings: 0.207
DOIhttp://dx.doi.org/10.1002/jssc.200800241
ISI Accession Number IDWOS:000258936700013
ReferencesReferences in Scopus
DC Field
Value
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
2011 Impact Factor: 2.733
2011 SCImago Journal Rankings: 0.207
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
Author Affiliations
  1. The University of Hong Kong
  2. Hunan Normal University