Relevant bibliographies by topics / Glutathione-S-transferase P1

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Academic literature on the topic 'Glutathione-S-transferase P1'

Author: Grafiati
Published: 4 June 2025
Last updated: 23 June 2025

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Journal articles on the topic "Glutathione-S-transferase P1"

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Balchin, David, Stoyan H. Stoychev, and Heini W. Dirr. "S-Nitrosation Destabilizes Glutathione Transferase P1-1." Biochemistry 52, no. 51 (2013): 9394–402. http://dx.doi.org/10.1021/bi401414c.

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Haaften, Rachel I. M. van, Guido R. M. M. Haenen, Chris T. A. Evelo, and Aalt Bast. "Tocotrienols Inhibit Human Glutathione S-Transferase P1-1." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 54, no. 2 (2002): 81–84. http://dx.doi.org/10.1080/15216540214315.

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Woo, Hee-Yeon, Kye-Hyun Kim, and Se-Won Lim. "Estrogen receptor 1, Glutathione S-transferase P1, Glutathione S-transferase M1, and Glutathione S-transferase T1 Genes with Dysmenorrhea in Korean Female Adolescents." Annals of Laboratory Medicine 30, no. 1 (2010): 76–83. http://dx.doi.org/10.3343/kjlm.2010.30.1.76.

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Singh, Savita, Girish C. Shukla, and Sanjay Gupta. "MicroRNA Regulating Glutathione S-Transferase P1 in Prostate Cancer." Current Pharmacology Reports 1, no. 2 (2015): 79–88. http://dx.doi.org/10.1007/s40495-014-0009-3.

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Mulder, Theo P. �J, Wilbert H. �M Peters, Theo Wobbes, Ben J. �M Witteman, and Jan B. �M �J Jansen. "Measurement of glutathione S-transferase P1-1 in plasma." Cancer 80, no. 5 (1997): 873–80. http://dx.doi.org/10.1002/(sici)1097-0142(19970901)80:5<873::aid-cncr7>3.0.co;2-m.

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Manar, Martha H., Milton R. Brown, Theresa W. Gauthier, and Lou Ann S. Brown. "Association of Glutathione-S-Transferase-P1 (GST-P1) Polymorphisms with Bronchopulmonary Dysplasia." Journal of Perinatology 24, no. 1 (2003): 30–35. http://dx.doi.org/10.1038/sj.jp.7211020.

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Russell, Tiffany M., Mahan Gholam Azad, and Des R. Richardson. "The Relationship of Glutathione-S-Transferase and Multi-Drug Resistance-Related Protein 1 in Nitric Oxide (NO) Transport and Storage." Molecules 26, no. 19 (2021): 5784. http://dx.doi.org/10.3390/molecules26195784.

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Nitric oxide is a diatomic gas that has traditionally been viewed, particularly in the context of chemical fields, as a toxic, pungent gas that is the product of ammonia oxidation. However, nitric oxide has been associated with many biological roles including cell signaling, macrophage cytotoxicity, and vasodilation. More recently, a model for nitric oxide trafficking has been proposed where nitric oxide is regulated in the form of dinitrosyl-dithiol-iron-complexes, which are much less toxic and have a significantly greater half-life than free nitric oxide. Our laboratory has previously examined this hypothesis in tumor cells and has demonstrated that dinitrosyl-dithiol-iron-complexes are transported and stored by multi-drug resistance-related protein 1 and glutathione-S-transferase P1. A crystal structure of a dinitrosyl-dithiol-iron complex with glutathione-S-transferase P1 has been solved that demonstrates that a tyrosine residue in glutathione-S-transferase P1 is responsible for binding dinitrosyl-dithiol-iron-complexes. Considering the roles of nitric oxide in vasodilation and many other processes, a physiological model of nitric oxide transport and storage would be valuable in understanding nitric oxide physiology and pathophysiology.
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Velden, Jos van der, C. Matthew Kinsey, James D. Nolin, et al. "Glutathione S-Transferase P1-Catalyzed Protein S-Glutathionylation in Lung Cancer." Free Radical Biology and Medicine 87 (October 2015): S74. http://dx.doi.org/10.1016/j.freeradbiomed.2015.10.194.

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Salehi, Zivar, Arvand Akbari, and Shahin Koohmanai. "Significant difference between the frequency of glutathione-S-transferase M1, glutathione-S-transferase T1 and glutathione-S-transferase P1 polymorphisms in type 1 diabetes patients and controls." Annals of Tropical Medicine and Public Health 10, no. 6 (2017): 1479. http://dx.doi.org/10.4103/atmph.atmph_359_17.

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Kim, Sook Un, Kyoung Mu Lee, Sue Kyung Park, et al. "Glutathione S-transferase P1 Genetic Polymorphisms and Breast Cancer Risk." Cancer Research and Treatment 34, no. 3 (2002): 205–11. http://dx.doi.org/10.4143/crt.2002.34.3.205.

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Dissertations / Theses on the topic "Glutathione-S-transferase P1"

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Ralat, Luis A. "Insights into the multiple functions of glutathione S-transferase P1-1 characterization of its several ligand sites and examination of its interaction with 1-cysteine peroxiredoxin /." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 263 p, 2008. http://proquest.umi.com/pqdweb?did=1679675771&sid=8&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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Duvoix, Annelyse. "Régulation transcriptionnelle de la glutathion S-transférase P1-1 via AP-1 et NF-kB dans les cellules leucémiques humaines@ : effet inhibiteur des agents chimiopréventifs d'origine naturelle." Nancy 1, 2003. http://docnum.univ-lorraine.fr/public/SCD_T_2003_0248_DUVOIX.pdf.

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La glutathion S-Transférase Pl-1 (GSTP1-1), impliquée dans la conjugaison de composés électrophiles au glutathion, la cancérogénèse et le développement de résistances aux anticancéreux, reste peu étudiée dans 16' cas des leucémies humaines en ce qui concerne l'expression du gène ainsi que des voies de transduction du signal impliquées. Dans une étude précédente, notre équipe a montré l'importance du site AP-l en tant que régulateur du promoteur minimal de la GSTP1-l. Pour ce travail, nous montrons dans un premier temps que des inducteurs typiques d'AP-l comme l'ester de phorbol TPA ou les mét1!. Ux lourds n'induisent pas l'expression de l'ARNm de la GSTPl-l dans la lignée leucémique K562. Par contre, nous confirmons l'importance de c-Jun, c-Fos et de la voie de signalisation menant à l'induction de AP-l dans la régulation de l'expression de la GSTPl-l. La plupart des gènes régulés par AP-l étant aussi régulés par NF-KB, nous avons décidé de vérifier le rôle de ce facteur dans la régulation de la GSTPl-l dont l'ARNm est inductible au TNFa. Grâce à un outil informatique, nous avons pu découvrir la présence d'un site NF-KB qui fixe les sous-unités p50 et p65 de NF-KB en réponse à un traitement au TNFa. Des expériences de co-transfections nous ont permis de compléter nos études en prouvant que la voie de signalisation NF-KB est bien impliquée dans la régulation de la GSTP1-1. Finalement, nous avons démontré l'efficacité d'agents chimiopréventifs, grâce à l'utilisation de la curcumine dont nous démontrons ici la capacité d'inhiber l'expression de la GSTPl-l en bloquant la fixation d' AP-l et de NF-KB tout en induisant l'apoptose dans les cellules leucémiques K562. Nous avons élargi nos résultats vers à l'utilisation d'autres agents chimiopréventifs dont la capsaicine et l'émodine. En résumé, nos résultats montrent que la GSTPl-l est régulée par les facteurs de transcription AP-l et NF-KB et inhibée par des agents chimiopréventifs qui présentent un intérêt potentiel pour de nouvelles thérapies anti-cancéreuses.
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Schnekenburger, Michael Trentesaux Chantal. "Régulation de l'expression de la glutathion S-transférase P1-1 au cours de la différenciation de la lignée leucémique humaine K562." [S.l.] : [s.n.], 2004. http://scdurca.univ-reims.fr/exl-doc/GED00000075.pdf.

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Schnekenburger, Michael. "Régulation de l'expression de la glutathion S-transférase P1-1 au cours de la différencification de la lignée leucémique humaine K562." Reims, 2004. http://theses.univ-reims.fr/exl-doc/GED00000075.pdf.

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La @glutathion S-transférase (GST) P1-1 est une enzyme associée à la carcinogenèse et au développement de résistance aux médicaments anticancéreux. Notre hypothèse de travail repose sur le fait que la différenciation cellulaire peut-être une approche thérapeutique dans le traitement des leucémies. Notre objectif est de savoir si l'expression du gène codant pour la GSTP1-1 est modulée au cours de la différenciation. Nos résultats montrent que l'expression de la GSTP1-1 est augmentée par des inducteurs de la différenciation érythroi͏̈de (anthracyclines, hémine) de la leucémie humaine K562, alors qu'elle est diminuée par le TPA qui induit la voie mégacaryocytaire dans ces cellules. L'induction de différenciation par le butyrate vers ces voies myéloi͏̈des s'accompagne d'une diminution de l'expression de l'ARNm de GSTP1-1. L'étude de la séquence promotrice du gène de la GSTP1-1 nous a permis de découvrir deux séquences GATA. La caractérisation des sites met en évidence un complexe résultant de l'interaction entre le site situé à -1208 et le facteur de transcription GATA-1, impliqué dans les processus de différenciation hématopoi͏̈étique. Avec les anthracyclines (aclarubicine et doxorubicine), le TPA et le butyrate, l'intensité de ce complexe est corrélée à l'expression de l'ARNm de GSTP1-1 et à la voie de différenciation induite. Dans le cas de l'hémine, c'est une stabilisation de l'ARNm de GSTP1-1 qui est à l'origine de l'accumulation d'ARNm observée. En conclusion, nous montrons que la GSTP1-1 est régulée au cours de la différenciation érythroi͏̈de et mégacaryocytaire de cellules leucémiques avec la participation probable de GATA-1<br>@Glutathione S-transferase (GST) P1-1 is an enzyme implicated in carcinogenesis and closely associated with the development of resistance to anti-cancer drugs. Our working hypothesis is based on the fact that the cellular differentiation can be used as a therapeutic approach in the treatment of leukaemias. We wanted to know if the GSTP1-1 expression is modulated during erythroid and megakaryocytic differentiation. Results show that its expression is increased during aclarubicine (acla), doxorubicin (dox) and hemin-induced erythroid differentiation of the human K562 cells (a pluripotent chronic myelogenous leukaemia). In contrast, GSTP1-1 expression is down-regulated during phorbol ester TPA-induced megakaryocytic differentiation of these cells. Moreover, time- and concentration-dependent activation of both erythroid and megakaryocytic differentiation pathways by butyric acid progressively inhibited GSTP1-1 expression. An analysis of the GSTP1-1 promoter sequence enabled us to discover two GATA sequences. By electrophoretic mobility shift assay, we determine the specificity of a GATA-1 binding on the site located at -1208. GATA-1 is known to be implicated in the process of hematopoietic differentiation and we show that GATA-1 promoter binding activity is correlated with the GSTP1-1 mRNA expression depending on the differentiation pathway induced by acla, dox, TPA and butyrate. A post-transcriptional stabilization of mRNA is involved in GSTP1-1 increase during hemin-induced erythroid differentiation. In conclusion, these results demonstrate the implication of GATA-1 transcription factor in differentiation-specific variations of GSTP1-1 expression
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Balchin, David. "Regulation of glutathione transferase P1-1 by S-nitrosation." Thesis, 2014.

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S-Nitrosation is a post-translational modification of protein cysteine residues, which occurs in response to cellular oxidative stress. Although it is increasingly being linked to physiologically important processes, the molecular basis for protein regulation by this modification remains poorly understood. Biophysical methods were used to elucidate the mechanism and molecular consequences of S-nitrosation of glutathione transferase (GST) P1-1, a ubiquitous homodimeric detoxification enzyme and important target for cancer therapeutics. Transient kinetic techniques, isothermal titration calorimetry and protein engineering were used to develop a minimal mechanism for S-nitrosation of GSTP1-1, the first for any protein. Cys47 of GSTP1-1 is S-nitrosated according to a conformational selection mechanism, with the chemical step limited by a pre-equilibrium between the open and closed conformations of a dynamic helix at the active site. Cys101, in contrast, is Snitrosated in a single step but is subject to negative cooperativity due to steric hindrance at the dimer interface. S-Nitrosation at Cys47 and Cys101 was found to reduce the detoxification activity of GSTP1-1 by 94%. Circular dichroism spectroscopy, acrylamide quenching and amide hydrogen-deuterium exchange mass spectrometry experiments revealed that the loss of activity is due to the introduction of local disorder at the active site. Furthermore, the modification destabilises domain 1 of GSTP1-1 against denaturation, smoothing the unfolding energy landscape of the protein and introducing a refolding defect. These data elucidate the physical basis for the regulation of GSTP1-1 by S-nitrosation, and provide general insight into the mechanism of S-nitrosation and its effect protein stability and dynamics.
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Hsiao, Ru-Ling, and 蕭茹鈴. "The associations between Glutathione S-Transferase P1 polymorphisms, cigarette smoking and risk of asthma among adults." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/79390765711534248497.

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碩士<br>高雄醫學大學<br>公共衛生學研究所<br>100<br>Background：Asthma is a global public health issue. There is more than 90% of GST enzyme activity encoded by GSTP1 gene in human lung epithelium. Previous studies have reported that a single nucleotide polymorphism (SNP) of GSTP1 is a new marker for identifying bronchial hyperresponsiveness and asthma. Objective：The aim of the present study was to explore the association between polymorphisms of GSTP1 gene and asthma, and to determine whether the relationship between GSTP1 gene and asthma was modified by smoking habit. We also investigated the association between GSTP1 genotype, lung function and IgE concentrations in adult asthma. Materials and methods：524 hospital based asthmatic adults and 524 age and sex matched community controls were recruited in the present case-control study, and the controls were free from asthma, pneumonia, tuberculosis, emphysema, COPD and cancers by self-report. We selected five tagSNPs which included GSTP1 rs6591256, GSTP1 Ile105Val (rs1695), rs749174, rs1871042 and rs947895 from HapMap website. All subjects completed a questionnaire and were genotyped by using real-time PCR. Results：After controlling for confounding factors, the smokers carried major homozygous allele for five SNPs had a significantly increase risk of asthma (AOR=2.58, 2.56, 2.49, 2.47 and 2.47 for GSTP1 rs6591256, rs1695, rs749174, rs1871042 and rs947895, respectively). The haplotype analyses showed an increasing risk for the major allele (AAC) of rs6591256-rs1695-rs1871042 on asthma (OR=1.93) in ever-smokers, but not in never smokers. Conclusion：Among ever-smokers, major homozygous carriers and the haplotype (AAC) of GSTP1 tagSNPs are associated with an increasing risk of asthma. The results suggested that cigarette smoking and GSTP1 gene may play important roles in adult asthma.
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Book chapters on the topic "Glutathione-S-transferase P1"

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Thakur, Vijay S., and Sanjay Gupta. "Plant Polyphenols as Epigenetic Modulators of Glutathione S-Transferase P1 Activity." In Epigenetics and Cancer. Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6612-9_13.

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Akbas, E., H. Mutluhan-Senli, N. Eras-Erdogan, T. Colak, Ö. Türkmenoglu, and S. Kul. "The Investigation of Relationship between the Poly-Morphism in Exon 5 of Glutathione S-Transferase P1 (Gstp1) Gene and Breast Cancer." In Biodefence. Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-94-007-0217-2_15.

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Slonchak, Andrii, Agata Chwieduk, Joanna Rzeszowska-Wolny, and Maria Obolenskay. "Regulation of the Glutathione S-Transferase P1 Expression in Melanoma Cells." In Breakthroughs in Melanoma Research. InTech, 2011. http://dx.doi.org/10.5772/18747.

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Morales, Guillermo A., and Edgardo Laborde. "Chapter 20 Small-Molecule Inhibitors of Glutathione S-Transferase P1-1 as Anticancer Therapeutic Agents." In Annual Reports in Medicinal Chemistry Volume 42. Elsevier, 2007. http://dx.doi.org/10.1016/s0065-7743(07)42020-6.

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Conference papers on the topic "Glutathione-S-transferase P1"

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Liu, Tao. "Notice of Retraction: Cigarette Smoking, Glutathione S-Transferase P1 Genetic Variant, and Cardiovascular Fitness." In 2011 5th International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2011. http://dx.doi.org/10.1109/icbbe.2011.5781306.

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Ali-Osman, Francis, and Jiewu Liu. "Abstract 1061: Glutathione S-transferase P1 is required for growth and survival of human glioma cells." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1061.

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Liu, Mingli. "Abstract 4368: The clinicopathological significance of glutathione S-transferase P1 hypermethylation in breast cancer, a meta-analysis and literature review." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-4368.

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Thakur, Vijay S., Gauri Deb, Mark W. Jackson, and Sanjay Gupta. "Abstract 5257: Upregulation of glutathione S-transferase P1 by green tea polyphenols: A novel transcriptional target of p53 tumor suppressor gene." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-5257.

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OH, SUNG YONG, Ki Han Kim, Sung Hyun Kim, et al. "Abstract 3739: Clinicopathologic significance of ERCC1, Thymidylate Synthase and Glutathione S-Transferase P1 expression for advanced gastric cancer patients receiving adjuvant 5-FU and cisplatin chemotherapy." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3739.

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Turley, Ryan S., Jiewu Liu, Douglas Tyler, and Francis Ali-Osman. "Abstract 1635: Short hairpin RNA-mediated transcriptional suppression of glutathione S-transferase P1 suppresses growth and induces apoptosis through altered MAP kinase signaling in melanoma cells." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1635.

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Stepanova, Yevgenya, Igor Kolpakov, Vitaliy Vdovenko, Valentina Kondrashova, Victor Zygalo, and Olena Leonovych. "Role of glutathione S-transferase M1 (GSTM1), P1 (GSTP1), and T1 (GSTT1) gene polymorphisms in the development of the bronchial hyperreactivity in children residing at radiologically contaminated territories of Ukraine." In RAD Conference. RAD Centre, 2021. http://dx.doi.org/10.21175/rad.abstr.book.2021.27.7.

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Turley, Ryan S., Michael E. Lidsky, Douglas S. Tyler, and Francis Ali-Osman. "Abstract 2012: MAP kinase activation and suppression of anti-apoptotic Bcl-2 family members are associated with induction of apoptotic death in melanoma cells following down-regulation of glutathione S-transferase P1." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2012.

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