GST isoenzymes in matched normal and neoplastic breast tissue

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dc.contributor.authorOguztuzun, S.
dc.contributor.authorAbu-Hijleh, A.
dc.contributor.authorCoban, T.
dc.contributor.authorBulbul, D.
dc.contributor.authorKilic, M.
dc.contributor.authorIscan, M.
dc.contributor.authorIscan, M.
dc.date.accessioned2020-06-25T17:52:19Z
dc.date.available2020-06-25T17:52:19Z
dc.date.issued2011
dc.departmentKırıkkale Üniversitesi
dc.descriptionKilic, Murat/0000-0002-1377-2021
dc.description.abstractThe potential to metabolize endogenous and exogenous substances may influence breast cancer development and tumor growth. Therefore we investigated GST activity and the protein expression of glutathione S-transferases (GSTs) isoenzymes known to be involved in the metabolism of endogenous and exogenous carcinogens in breast cancer tissue to obtain new information on their possible role in tumor progression. The interindividual variation in the conjugation of 1-chloro-2,4-dinitrobenzene (CDNB) and of 1,2-epoxy-3-(p-nitrophenoxy) propane (EPNP) with glutathione (GSH) by cytosolic glutathione S-transferases (GSTs) were investigated in human breast matched normal and tumor samples. The GSTA, GSTM, GSTP and GSTT isoenzymes from the crude extracts of matched breast normal and tumor tissues in terms of their immunological properties using western blotting were compared. In most of the samples, the GST activities were higher in the tumor than in the normal cytosolic fractions against both CDNB and EPNP. In the western blotting analysis, it was proved statistically that in normal and tumor epithelial cells, there was difference between GST pi and theta isoenzymes expressions (p<0.05), but no difference between the staining scores of GST mu and alpha isoenzymes (p>0.05). In normal epithelium there was a stronger GST theta expression than in invasive tumor tissues (p=0.013). However, the stronger GST pi expression was observed in tumor epithelium than in normal epithelium in human breast cancers (p=0.000). We found the GSTP protein level and GST activities were higher in the breast tumor than in the normal cytosolic fractions against both CDNB and EPNP, thus implicating a certain biological importance.en_US
dc.identifier.citationOguztuzun, S., Abu-Hijleh, A., Coban, T., Bulbul, D., Kilic, M., Iscan, M., & Iscan, M. (2011). GST isoenzymes in matched normal and neoplastic breast tissue. Neoplasma, 58(4), 304–310.en_US
dc.identifier.doi10.4149/neo_2011_04_304
dc.identifier.endpage310en_US
dc.identifier.issn0028-2685
dc.identifier.issn1338-4317
dc.identifier.issue4en_US
dc.identifier.pmid21520986
dc.identifier.scopus2-s2.0-80052551805
dc.identifier.scopusqualityQ2
dc.identifier.startpage304en_US
dc.identifier.urihttps://doi.org/10.4149/neo_2011_04_304
dc.identifier.urihttps://hdl.handle.net/20.500.12587/5130
dc.identifier.volume58en_US
dc.identifier.wosWOS:000290695900005
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherAepress Sroen_US
dc.relation.ispartofNeoplasma
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectBreast canceren_US
dc.subjectglutathione S-transferasesen_US
dc.subjectthetaen_US
dc.subjectalphaen_US
dc.subjectmu and pi classes of GSTsen_US
dc.subjectwestern blottingen_US
dc.titleGST isoenzymes in matched normal and neoplastic breast tissueen_US
dc.typeArticle

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