Determination of glutathione, glutathione reductase, glutathione peroxidase and glutathione S-transferase levels in human lung cancer tissues

Saydam, Nurten; Kirb, A.; Demir, Orhan; Hazan, E; Oto, Öxtekin; Saydam, Okay; Güner, Gül

doi:10.1016/s0304-3835(97)00245-0

Cited by 117 publications

(71 citation statements)

References 36 publications

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“…This value was slightly same or higher those reported earlier for carcinomas of the uterine cervix (96%) [31] and colorectum (88%) [32]. In a more extended study, Saydam and coworkers [33] and Hida and coworkers [34] reported significantly higher GST enzyme activity levels and plasma GSTP values in human lung cancers as compared with control tissues.…”

Section: Discussionsupporting

confidence: 84%

The expression of GST isoenzymes and p53 in non-small cell lung cancer.

Oğuztüzün¹,

Aydın²,

Demırağ³

et al. 2010

Folia Histochem Cytobiol.

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This study investigated the immunohistochemical staining characteristics of glutathione-S-transferase alpha, pi, mu, theta and p53 in non-small cell lung carcinoma and normal lung tissue from 50 patients. The relationships between expressions of the Glutathione-S-transferase isoenzymes and some clinicopathological features were also examined. Expression of glutathione-S-transferase pi, mu, alpha, theta and p53 was assessed by immunohistochemistry for primary lung carcinomas of 50 patients from the Sanitarium Education and Research Hospital, Ankara lung cancer collection. The relationships between expression of the glutathione-S-transferase isoenzymes, p53 in normal and tumor tissue by Student T test and the clinicopathological data were also examined by Spearman Rank tests. When the normal and tumor tissue of these cases were compared according to their staining intensity and percentage of positive staining, glutathione-S-transferase alpha, pi, mu, theta expressions in tumor cells was significantly higher than normal cells (p<0.05). There was no significant difference in the expression of p53 between normal and tumor cells (p>0.05). When the immunohistochemical results of glutathione-S-transferase isoenzymes and p53 were correlated with the clinical parameters, there were no significant associations between glutathione-S-transferases and p53 expressions and tumor stage, tumor grade and smoking status (p>0.05).

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Section: Discussionsupporting

confidence: 84%

The expression of GST isoenzymes and p53 in non-small cell lung cancer.

Oğuztüzün¹,

Aydın²,

Demırağ³

et al. 2010

Folia Histochem Cytobiol.

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“…The higher mean cytosolic GST and GR activity in patients with buccal mucosa, as found in the present study, were possibly due to transcriptional activation of these enzymes by xenobiotic responsive elements as an adaptive response to chemical and oxidative stress during tumor development (Hayes and Pulford, 1995;Ilio et al, 1988;Saydam et al, 1997;Wang et al, 1997). Large inter-individual variations in enzyme activities have been demonstrated for GST (Ilio et al, 1988).…”

Section: Discussionsupporting

confidence: 65%

“…Phase-II detoxifying enzymes involved in the detoxification of xenobiotics and drugs have been found to be of prime importance in carcinogenesis (Tsuchida et al, 1989;Ilio et al, 1988;Saydam et al, 1997). In the present investigation, GST and GR were estimated in sera and in tumor cytosol fractions prepared from adjacent non-cancerous and cancerous buccal mucosa tissues of the same patient.…”

Section: Discussionmentioning

confidence: 67%

Assessment of glutathione-S-transferase and glutathione reductase in patients with squamous-cell carcinoma of buccal mucosa

Rawal

Patel

et al. 1999

Int. J. Cancer

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“…At the same time, tumor cells show enhanced levels of antioxidant molecules like GSH and certain reductases that may play a role in demodifying oxidative and nitrosative stress-responsive proteins and thwarting cell death (51). Indeed, higher levels and activity of glutathione S-transferases, glutathione peroxidase, and others have been identified in tumors compared with normal tissue (52,53). Our findings establish nuclear translocation of CLIC4 as a redox-regulated event.…”

Section: Discussionmentioning

confidence: 56%

S-Nitrosylation Regulates Nuclear Translocation of Chloride Intracellular Channel Protein CLIC4

Malik

Shukla

Amin

et al. 2010

Journal of Biological Chemistry

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Nuclear translocation of chloride intracellular channel protein CLIC4 is essential for its role in Ca2؉ -induced differentiation, stress-induced apoptosis, and modulating TGF-␤ signaling in mouse epidermal keratinocytes. However, post-translational modifications on CLIC4 that govern nuclear translocation and thus these activities remain to be elucidated. The structure of CLIC4 is dependent on the redox environment, in vitro, and translocation may depend on reactive oxygen and nitrogen species in the cell. Here we show that NO directly induces nuclear translocation of CLIC4 that is independent of the NO-cGMP pathway. Indeed, CLIC4 is directly modified by NO through S-nitrosylation of a cysteine residue, as measured by the biotin switch assay. NO enhances association of CLIC4 with the nuclear import proteins importin ␣ and Ran. This is likely a result of the conformational change induced by S-nitrosylated CLIC4 that leads to unfolding of the protein, as exhibited by CD spectra analysis and trypsinolysis of the modified protein. Cysteine mutants of CLIC4 exhibit altered nitrosylation, nuclear residence, and stability, compared with the wild type protein likely as a consequence of altered tertiary structure. Moreover, tumor necrosis factor ␣-induced nuclear translocation of CLIC4 is dependent on nitric-oxide synthase activity. Inhibition of nitric-oxide synthase activity inhibits tumor necrosis factor ␣-induced nitrosylation and association with importin ␣ and Ran and ablates CLIC4 nuclear translocation. These results suggest that S-nitrosylation governs CLIC4 structure, its association with protein partners, and thus its intracellular distribution.CLIC4 (chloride intracellular channel protein 4) belongs to a family of differentially expressed chloride channel proteins that are largely conserved from Caenorhabditis elegans to humans.Various members have been implicated in cell signaling cascades, ranging from stimulation of chloride channel activity by CLIC3 following association with extracellular signal-regulated kinase (ERK) 7 (1) to CLIC5A that is implicated in bone resorption and HCl transport in osteoclasts, in response to phosphorylation by c-Src (2). However, a number of functions of CLIC proteins are independent of channel activity (3, 4).The best characterized of the CLIC family members is CLIC4, identified in our laboratory as a p53 and TNF␣ 2 response gene that is up-regulated during keratinocyte differentiation. CLIC4 has emerged as a crucial player in many physiological processes, including tubular morphogenesis during angiogenesis (5-7), transdifferentiation of mammary fibroblasts to myofibroblasts in response to TGF-␤ (8), and adipocyte differentiation (9). CLIC4 has been established as a significant effector of mouse and human keratinocyte differentiation, associated with G 1 cell cycle arrest and expression of differentiation markers (10).An intriguing aspect of CLIC4 biology is its role as an effector of apoptosis, including p53-and c-Myc-induced apoptosis, as well as in response to cytotoxic and ...

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Determination of glutathione, glutathione reductase, glutathione peroxidase and glutathione S-transferase levels in human lung cancer tissues

Cited by 117 publications

References 36 publications

The expression of GST isoenzymes and p53 in non-small cell lung cancer.

The expression of GST isoenzymes and p53 in non-small cell lung cancer.

Assessment of glutathione-S-transferase and glutathione reductase in patients with squamous-cell carcinoma of buccal mucosa

S-Nitrosylation Regulates Nuclear Translocation of Chloride Intracellular Channel Protein CLIC4

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