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Article: Concomitant induction of heme oxygenase-1 attenuates the cytotoxicity of arsenic species from Lumbricus extract in human liver HepG2 cells
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TitleConcomitant induction of heme oxygenase-1 attenuates the cytotoxicity of arsenic species from Lumbricus extract in human liver HepG2 cells
 
AuthorsQi, H1
Chen, B2
Le, XC2
Rong, J1
 
Issue Date2012
 
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/106056929
 
CitationChemistry And Biodiversity, 2012, v. 9 n. 4, p. 739-754 [How to Cite?]
DOI: http://dx.doi.org/10.1002/cbdv.201100133
 
AbstractHeme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion. The present study was originally designed to characterize the HO-1 induction by Lumbricus extract as a potential cytoprotective mechanism. Through bioactivity-guided fractionation, with human HepG2 cells as the cellular detector, surprisingly, we found that arsenic was enriched in the active fractions isolated from Lumbricus extract. Arsenic speciation was further carried out by liquid chromatography with inductively coupled plasma mass spectrometry (LC/ ICP-MS). Our results showed that Lumbricus extract contained two major arsenic species, arsenite (As III; 53.7%) and arsenate (As V; 34.2%), and six minor arsenic species. Commercial sodium arsenite (NaAsO 2) was used to verify the effects of Lumbricus extract on HO-1 expression and related intracellular signaling pathways. Both p38MAP kinase and NF-E2-related factor 2 (Nrf2) pathways were found to modulate HO-1 induction by Lumbricus extract and NaAsO 2. The cytotoxicity of arsenite was augmented by p38 MAP kinase inhibitor SB202190 and HO-1 inhibitor tin protoporphyrin IX (SnPP), whereas p38 MAP kinase inhibitor SB202190 also inhibited HO-1 induction by NaAsO 2. These results suggest that arsenic-containing compounds are responsible for HO-1 induction by Lumbricus extract. Although the exact role of toxic arsenic compounds in the treatment of oxidative injury remains unclear, concomitant HO-1 induction may be a key mechanism to antagonize the cytotoxicity of arsenic compounds in human cells. © 2012 Verlag Helvetica Chimica Acta AG.
 
ISSN1612-1872
2013 Impact Factor: 1.795
 
DOIhttp://dx.doi.org/10.1002/cbdv.201100133
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorQi, H
 
dc.contributor.authorChen, B
 
dc.contributor.authorLe, XC
 
dc.contributor.authorRong, J
 
dc.date.accessioned2012-08-16T06:17:18Z
 
dc.date.available2012-08-16T06:17:18Z
 
dc.date.issued2012
 
dc.description.abstractHeme oxygenase-1 (HO-1) is an inducible antioxidant enzyme that degrades heme to three products, biliverdin, carbon monoxide (CO), and iron ion. The present study was originally designed to characterize the HO-1 induction by Lumbricus extract as a potential cytoprotective mechanism. Through bioactivity-guided fractionation, with human HepG2 cells as the cellular detector, surprisingly, we found that arsenic was enriched in the active fractions isolated from Lumbricus extract. Arsenic speciation was further carried out by liquid chromatography with inductively coupled plasma mass spectrometry (LC/ ICP-MS). Our results showed that Lumbricus extract contained two major arsenic species, arsenite (As III; 53.7%) and arsenate (As V; 34.2%), and six minor arsenic species. Commercial sodium arsenite (NaAsO 2) was used to verify the effects of Lumbricus extract on HO-1 expression and related intracellular signaling pathways. Both p38MAP kinase and NF-E2-related factor 2 (Nrf2) pathways were found to modulate HO-1 induction by Lumbricus extract and NaAsO 2. The cytotoxicity of arsenite was augmented by p38 MAP kinase inhibitor SB202190 and HO-1 inhibitor tin protoporphyrin IX (SnPP), whereas p38 MAP kinase inhibitor SB202190 also inhibited HO-1 induction by NaAsO 2. These results suggest that arsenic-containing compounds are responsible for HO-1 induction by Lumbricus extract. Although the exact role of toxic arsenic compounds in the treatment of oxidative injury remains unclear, concomitant HO-1 induction may be a key mechanism to antagonize the cytotoxicity of arsenic compounds in human cells. © 2012 Verlag Helvetica Chimica Acta AG.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationChemistry And Biodiversity, 2012, v. 9 n. 4, p. 739-754 [How to Cite?]
DOI: http://dx.doi.org/10.1002/cbdv.201100133
 
dc.identifier.doihttp://dx.doi.org/10.1002/cbdv.201100133
 
dc.identifier.epage754
 
dc.identifier.hkuros203762
 
dc.identifier.issn1612-1872
2013 Impact Factor: 1.795
 
dc.identifier.issue4
 
dc.identifier.pmid22492492
 
dc.identifier.scopuseid_2-s2.0-84859794329
 
dc.identifier.spage739
 
dc.identifier.urihttp://hdl.handle.net/10722/160718
 
dc.identifier.volume9
 
dc.languageeng
 
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/106056929
 
dc.publisher.placeGermany
 
dc.relation.ispartofChemistry and Biodiversity
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshAnimals
 
dc.subject.meshAntineoplastic Agents - chemistry - isolation & purification - pharmacology
 
dc.subject.meshApoptosis - drug effects
 
dc.subject.meshArsenicals - chemistry - isolation & purification - pharmacology
 
dc.subject.meshHeme Oxygenase-1 - metabolism
 
dc.subject.meshHep G2 Cells
 
dc.subject.meshHumans
 
dc.subject.meshNeoplasms - drug therapy - enzymology
 
dc.subject.meshOligochaeta - chemistry
 
dc.subject.meshSignal Transduction - drug effects
 
dc.titleConcomitant induction of heme oxygenase-1 attenuates the cytotoxicity of arsenic species from Lumbricus extract in human liver HepG2 cells
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong Li Ka Shing Faculty of Medicine
  2. University of Alberta