GSTP1 and cancer: Expression, methylation, polymorphisms and signaling (Review)
- Authors:
- Published online on: February 10, 2020 https://doi.org/10.3892/ijo.2020.4979
- Pages: 867-878
Abstract
1. GST family: Multifunctional enzymes involved in oxidative stress, poisoning, and cancer
The glutathione-S transferase (GST) family consists of a group of isoenzymes involved in phase II detoxification of xenobiotics by glutathione conjugation (1,2). It is widely found in nematodes, fruit flies, yeast, and the cytoplasm of higher vertebrates. Studies have shown that soluble GST accounts for 4% of total soluble protein in human and rodent livers (3). Three major protein subfamilies have been reported to exhibit glutathione transferase activity: Cytoplasmic, mitochondrial and microsomal GSTs (4,5). Microsomal GSTs are membrane-associated proteins in eicosanoid and glutathione metabolism (6,7). Cytoplasmic GSTs are the largest subfamily of these transferases and have unique activities. They catalyze the thiolysis of 4-nitrophenyl acetate, exhibit thiol transferase activity, reduce trinitroglycerin, dehydroascorbic acid and monomethyl decanoic acid, and catalyze ethyl maleate and 5-3 isomerization of ketosteroids (8).
According to the similarity in amino acid sequences, different structures of genes, and immunological cross-reactivity, GSTs are divided into seven subtypes (9) as follows: Alpha (α), pi (π), mu (μ), theta (θ), omega (ω), sigma (σ), and zeta (Table I). Among those, μ, θ and π are the most widely studied GST subtypes in mammals (10). It is well known that μ-class glutathione S-transferase 1 (GSTM1) plays an important role in the toxicity and effectiveness of medical drugs. GSTM10 is the most common polymorphism, resulting in loss of enzymatic activity (11,12). Glutathione S-transferase θ 1 (GSTT1) plays a role in human carcinogenesis (13). GSTM1-null and GSTT1-null may contribute to the clinical course of patients with type 2 diabetes mellitus (T2DM) (14). GSTs interact with several factors, such as regulatory kinases, and modulate numerous pathways involved in cell proliferation, differentiation and death. Previous studies have demonstrated that GST plays a major role in cancer cell proliferation and death via its cytoprotective and regulatory functions (15,16). GST enzymes also play an important role in detoxifying chemotherapy drugs (17). They may be used to detoxify oxidized or alkylated drugs directly by combining active compounds or drugs (18). In addition to their well-characterized catalytic activity, there is evidence that GST isoenzymes also participate in regulating the expression of mitogen-activated protein kinases, and promote S-glutathionylation of cysteine residues in target proteins (19). In addition, genetic variants of GST have been reported to be involved in various fluorouracil- and platinum-based chemotherapies for the treatment of metastatic advanced cancers, such as acute myeloid leukemia (AML), gastrointestinal tumors, non-small cell lung cancer (NSCLC) and prostate cancer (PCa) (20,21). Therefore, it is clear that members of the GST family have a wide range of applications in detoxification and drug treatment.
2. GSTP1: A major regulator in the occurrence and development of cancer
GSTP1 is the most widely studied member of the GST family (22). The GSTP1 gene (π) is located on chromosome 11q13. It consists of nine exons and is 3.2 kb in length, protects cells from carcinogens and cytotoxins, and was originally isolated from a cosmid library. The gene spans ~3 kb and is interrupted by six introns with regions around the 5′-end having high G + C and CpG content typical of HpaII micro-fragment islands (23). In humans, GSTP1 usually consists of two identical dimeric subunits, each consisting of 210 amino acids and two binding sites, G and H. Different G and H sites with different amino acid residues in GST may play different roles. GSTP1 specifically binds to GSH or GSH analogs via the G site and catalyzes the interaction between GST amino acid residues and GSH thiols and conventional electrophiles at the H site (24). Therefore, G-site modification generally contributes to the development of specific GSTP1 inhibitors.
GSTP1 has a wide range of physiological functions: It is involved in metabolism, detoxification and elimination of potentially genotoxic foreign complexes, metabolizes a variety of carcinogenic compounds, and protects cells against DNA damage and canceration. In the GST family, early studies demonstrated that the GSTP1 gene plays an important role in several cellular processes, including catalysis and deoxylation of electrophilic compounds, oxidative stress regulation, cell signaling and carcinogenesis (25,26). GSTP1 actively protects cells from carcinogens and electrophilic compounds (27,28). It has been suggested that GSTP1 also protects cells from oxidants and electrophilic-mediated genomic damage (29). GSTP1 is involved in apoptosis resistance and metabolism of several chemotherapeutic agents. Platinum-based drugs have been found to be metabolized by GSTP1, allowing GSTP1 to be expressed in ovarian tumors. Therefore, GSTP1 may be used as a target gene and candidate response biomarker for platinum-based chemotherapy. In addition, GSTP1 plays a major role in the metabolism of cisplatin and carboplatin in ovarian cancer cells (30,31). Differences in expression of GSTP1 may affect the response of patients with ovarian cancer to platinum-based chemotherapy (32). Taken together, the studies on changes in GSTP1 expression of tumor cells may contribute to the development of antitumor drugs. GSTP1 appears hold promise in drug development, and the GSTP1 gene is involved in the regulation of activator proteins. It plays an important role in the regulation of tumor necrosis factor. Both activator protein 1 and nuclear factor (NF)-κB mediate regulation of GSTP through a redox process (33). A chimeric inhibitor that binds the affinity recognition moiety to a chelated transition metal has been explored to develop metal-mediated affinity reagents or drugs for hGSTP1-1 (34). GSTP1 is also a key regulator of hepatocyte proliferation during the initial stages of liver regeneration (35). The -323/-314 sequence located in the GSTP1 promoter binds to NF-κBp50/65 and p65/p65 dimers, and is involved in the regulation of this gene by tumor necrosis factor α (36-38). The GSTP1 gene (OMIM 134660) encoding the π-GST partial GSTP1-1 protein is widely expressed in most tissues, particularly in the lungs, esophagus and placenta (39). Ubiquitous epigenetic silencing of GSTP1 in PCa leads to increased survival and accumulation of potential priming DNA conjugates after exposure to long-term oxidative damage, suggesting that GSTP1 has protective and antitumor functions (40). As mentioned above, GSTP1 has important physiological functions in the detoxification and antioxidation of metabolites.
GSTP1 not only has important physiological functions, but also major pathological functions. GSTP1 is closely associated with exposure to low doses of ionizing radiation, heavy metals, and other chemicals (Table II). Manganese (Mn) has been shown to be a naturally occurring trace element that is essential for human health and development, but is neurotoxic at high concentrations (41,42). Studies have shown a possible synergistic effect between the blood Mn concentration and GSTP1 in autism spectrum disorder (43). GSTP1 is induced by lead and may be used as a biomarker for lead exposure. It is only involved in the changes during the later stages of lead poisoning (44,45). Previous studies have found that arsenic compounds are useful as drugs, but have toxic effects, and GSTP1 is a major factor in resistance to these drugs (46,47). GSTP1 detoxifies arsenic-based drugs by isolating the active site and dimer interface, reacting with cysteine in the presence of sufficient GSH under low GSH conditions (48,49). GSTP1 also reduces the retention time of As2O3 in the cells. Catabolism of H2O2 reduces the amount of H2O2 in the cells, thereby blocking apoptosis of lymphoma cells induced by As2O3 (50). In addition, GSTP1 may participate in the elimination of carcinogens in tobacco and participates in the occurrence of smoking-related lung adenocarcinoma. GSTP1 plays a role in the elimination of toxic substances from cigarette smoke in both normal lung and cancer cells (51). GSTP1 is also involved in the detoxification process of benzo(a)pyrene (BaP), which excretes the conjugates of BaP metabolism and detoxification (52). It is also involved in the protection of cells against 222Rn-induced DNA damage (53). GSTP1 also blocks lipopolysaccharide (LPS) -induced overproduction of proinflammatory factors and has anti-inflammatory effects on the LPS response (54). Therefore, as a detoxifying enzyme, GSTP1 plays an important role in the detoxification of heavy metals and may facilitate exploring metal-mediated affinity drugs. GSTP1 is also closely associated with radiation damage. Our previous studies indicated that GSTP1 is involved in the radiation-induced stress response of liver tissue in C57BL/6J mice and it may be used as a biomarker of low-dose radiation for early identification of radiation contamination. Therefore, the mechanism of GSTP1 in the radiation-induced stress response is worthy of further investigation (55,56). Of note, the involvement of GSTP1 in the development of diseases is a complex process involving multiple steps and factors. GSTP1 is a key regulator in the occurrence and development of multiple cancer types.
3. Expression of GSTP1: A factor involved in the development of multiple cancer types
There is a close association between GSTP1 expression and tumor development. In several tumor tissues, >90% of active GSTs is GSTP1 (57). Therefore, the difference in expression of GSTP1 in diseases such as tumors has attracted significant attention. Compared with normal tissues, the difference in GSTP1 expression is associated with multiple diseases (Table III). GSTP1 is highly expressed in various types of cancer and preneoplastic legions, such as colorectal, esophageal, lung, bladder, thyroid and breast cancer (58,59). GSTP1 is overexpressed at various stages of colorectal cancer, from abnormal crypt foci to advanced cancer (8,60). GSTP1 may be used as a clinically useful target for anti-colon cancer drugs (61). High expression of GSTP1 in esophageal cancer tissues may reduce the chemosensitivity of cancer cells (62,63). Increased expression of GSTP1 in bladder transitional cell carcinoma is associated with altered apoptotic pathways (64). Upregulation of GSTP1 expression contributes to an increase in the antioxidant capacity of bladder transitional cell carcinoma cells (65,66). High expression of GSTP1 plays a role in tumor growth and carcinogenesis of papillary thyroid cancer (67). Moreover, high expression of GSTP1 confers resistance of breast cancer cells to adriamycin by promoting autophagy (68). In addition, overexpression of GSTP1 inhibits the proliferation of HepG2 and Huh7 liver cancer (69). GSTP1 and multidrug resistance protein 1 (MRP1) are overexpressed in malignant melanoma. GSTP1 acts together with MRP1 to protect melanoma cells against the toxic effects of etoposide (70).
 | Table IIIDifferences in the expression of GSTP1 are involved in the development of various types of cancer. |
It is interesting that miRNAs regulate GSTP1, particularly in relation to human diseases. miR-133b overexpression contributes to the suppression of malignant growth and aggressiveness of cisplatin-resistant NSCLC cells by targeting GSTP1 (71). miRNA-130b may be involved in the development of drug resistance of ovarian cancer by regulating the expression level of the GSTP1 protein (72). Similarly, miR-133a directly regulates the GSTP1 gene in bladder cancer (BC) and mediates GSTP1-mediated anti-apoptotic effects by downregulation of miR-133a in human BC (73). There are also data suggesting that miR-133α in head and neck squamous cell carcinoma (HNSCC) regulates the carcinogenic effects of GSTP1, thereby providing new insights into the mechanisms underlying HNSCC carcinogenesis (74). Downregulation of GSTP1 may facilitate the function of miR-124 in doxorubicin resistance and enable the development of new treatments to overcome chemoresistance in colorectal cancer (CRC) patients (75). miR-513a-3p sensitizes human lung adenocarcinoma cells to cisplatin by regulating GSTP1 (76). Therefore, the regulation of GSTP1 by miRNA is crucial in several human diseases.
The expression of GSTP1 in tumors is low; for example, its expression in PCa is low, and downregulation of GSTP1 expression may play an important role in the progression of PCa (77). Downregulation of GSTP1 expression in PCa may be a useful biomarker for early detection and prognosis (78). Loss of GSTP1 expression in human PCa cells increases their susceptibility to oxidative stress-induced DNA damage and may be an important target for primary prevention of PCa (79). In certain diseases, the expression of GSTP1 may also play a regulatory and predictive role. GSTP1 expression may predict the pathological response to 5-fluorouracil/epirubicin/cyclophosphamide in estrogen receptor (ER)-negative tumors (80). The difference in the expression of GSTP1 is associated with multiple diseases and plays an important role in prediction and treatment.
4. GSTP1 methylation: A tissue biomarker that performs well in several types of malignancies
The promoter region of the GSTP1 gene is usually affected by methylation, and changes in methylation status suppress normal gene expression, which may lead to weakening or loss of its detoxification and antioxidant functions. In several cancer types, the GSTP1 gene is affected by hypermethylation. GSTP1 is a major tissue biomarker that performs well in several types of malignancies, such as PCa, breast and lung cancer, and hepatocellular carcinoma (HCC) (81). GSTP1 methylation has been found to be associated with the development of several diseases (Fig. 1). Recent research has confirmed that hypermethylation of GSTP1 inactivates the GSTP1 gene and plays a major role in liver cancer. It may increase the risk of HCC, and is also significantly associated with a poor prognosis of patients with HCC (82,83). It has been reported that hypermethylation of the GSTP1 gene promoter region may be a potential biomarker for distinguishing HCC from other liver diseases (84). Of note, methylation of the GSTP1 gene promoter may be associated with the invasiveness of HCC. Chronic hepatitis B virus infection may be responsible for inactivation of p16 induced by GSTP1 methylation (85). GSTP1 methylation is associated with oxidative stress-induced liver injury in acute-chronic hepatitis B liver failure. Abnormal methylation of the GSTP1 promoter is also present in acute-chronic hepatitis B liver failure and may have a high predictive value for short-term mortality. Therefore, GSTP1 may be a potential prognostic indicator of acute hepatitis B-related acute liver failure (86). GSTP1 methylation has a strong influence on liver-related diseases and may play a role in the treatment of liver-related diseases. GSTP1 methylation is associated with the recurrence and prognosis of PCa, and may be a potential epigenetic marker (87-92). Similar to PCa, GSTP1 hypermethylation also occurs in early events of breast cancer (93). The heterogenous DNA methylation pattern in the GSTP1 promoter is a major obstacle for DNA methylation analysis of the GSTP1 gene, which explains some of the contradictory differences in the role of GSTP1 promoter methylation in breast cancer (94). Although previous studies have shown no clear correlation between the GSTP1 status and the clinicopathological characteristics of PCa, GSTP1 methylation is associated with a more aggressive ER-positive breast cancer phenotype (95). Furthermore, GSTP1 methylation is associated with ER positivity (96-98). GSTP1 methylation was found to be correlated with the clinicopathological characteristics of breast cancer (99). Therefore, GSTP1 methylation is important for breast cancer research. The frequency of GSTP1 methylation in cancer tissues of patients with NSCLC ranges from 0 to 25%, while lower or no methylation is observed in adjacent benign tissues (100-105). Abnormal methylation of GSTP1 may contribute to the carcinogenesis of neuroblastoma and may be used as a new marker (106). In addition, in acromegaly, methylation of the GSTP1 gene is associated with resistance to treatment with somatostatin analogues (107). Therefore, GSTP1 methylation appears to play a key role in numerous diseases.
5. GSTP1 polymorphism: A potential biomarker for cancer risk
It has been demonstrated that GSTP1 enzymatic activity is strongly dependent on a single-nucleotide polymorphism, the A313 G polymorphism, which replaces isoleucine (Ile) with valine (Val) at the 105 amino acid position (Ile105Val) (IE), producing three GSTP1 genotypes: Ile/Ile homozygous wildtype, Ile/Val heterozygotes, and Val/Val homozygous variants (108,109). Genetic polymorphism of GSTP1 is associated with several cancer types. The genetic polymorphism of GSTP1 may be associated with the detoxification of polycyclic aromatic hydrocarbons in cigarette smoke and exhibits the highest expression in lung tissue (110,111). In the Chinese population, the GSTP1 Ile105Val polymorphism may increase the risk of lung cancer (112-114). Furthermore, GSTP1 exon 5 polymorphism is associated with lung cancer susceptibility. Stratified analysis has revealed a correlation between the GSTP1 exon 5 gene polymorphism and the risk of lung squamous cell carcinoma (115). GSTP1 genotyping may help identify patients at higher risk of developing anti-tuberculosis treatment-related hepatotoxicity (114,116). GSTP1 gene polymorphism may also be used as an independent prognostic marker for patients with HCC (117). GSTP1 Ile105Val may be associated with an increased risk of CRC (118,116). The Ile105Val polymorphism of the GSTP1 gene may also have a genetic effect on the occurrence of skin cancer (119,120). The GSTP1 polymorphism has been shown to be a potential biomarker for PCa risk (121,122). The GSTP1 Ile105Val polymorphism may also be associated with the risk of gastric cancer (123,124), and the GSTP1 Val allele appears to reduce the risk of premalignant lesions (125,126). An interesting finding is that the GSTP1 *C variant may exert protective effects against pancreatic cancer in the elderly (127). It has been demonstrated that GSTP1 is associated with response to chemotherapy, PFS and OS in patients with osteosarcoma, and GSTP1 polymorphism may help design individualized treatments (128,129). GSTP1 gene polymorphism may also play an important role in the prognosis of osteosarcoma patients treated with chemotherapy (130,131). In addition, GSTP1 gene polymorphism is associated with risk of oral SCC (132). The GSTP1 codon 105 polymorphism may play a major role in leukemia by altering the protein function and reducing its ability to detoxify certain mutagens and carcinogens, which may result in increased DNA damage and mutations that increase cancer risk (133). An individual with at least one Val allele at codon 105 of the GSTP1 enzyme may be susceptible to cancer. Following cytotoxic chemotherapy, the Val allele at GSTP1 codon 105 may result in treatment-related AML (134). It has been reported that GSTP1 polymorphism is important for the development of AML and the formation of AML-specific chromosomal abnormalities (135,136). Variant genotypes of the GSTP1 Ile105Val gene polymorphism may contribute to the risk of chronic myelogenous leukemia (137-139). Therefore, GSTP1 gene polymorphism may contribute to the treatment of leukemia.
GSTP1 gene polymorphism is not only involved in the development of cancer, but is also associated with a number of other diseases (Table IV). Diabetic neuropathy is a common complication of T2DM, and GSTP1 gene polymorphism may contribute to the development of T2DM (140,141). There is no clinical proof that GSTP1 IIe105Val polymorphisms affect the risk of gestational diabetes mellitus in a Chinese population (142). A significant correlation has been found between the GSTP1 (105) Ile/(105)Ile genotype and the development of grade ≥2 docetaxel (taxotere)-induced peripheral neuropathy (143). It has been demonstrated that the presence of the GSTP1 A114V rather than the I105V variant increases the risk of motor neuron disease (MND). Moreover, the combination of GSTP1 polymorphisms in codons 105 and 114 may result in protective reduction in the toxicity of electrophilic compounds to organic and inorganic hydrogen peroxides in MND patients (144). GSTP1 polymorphism plays a role in the incidence of chronic kidney disease and is associated with higher numbers of micronuclei (145,146). The GSTP1 Ile105Val genotype may affect the excretion and metabolism of inorganic arsenic (147). Furthermore, changes in GSTP1 may affect the risk of non-photo-induced drug eruptions (148). It has been found that the GSTP1 Ile105Val polymorphism is also associated with inter-individual variations in urinary and blood arsenic levels (132). Thus, GSTP1 gene polymorphism is closely associated with various diseases and may prove to be helpful for the development of therapeutic drugs.
6. GSTP1: A key factor involved in complex processes mediated by multiple signals
GSTP1 may mediate the storage and transport mechanisms of gases and react with some compounds. Nitric oxide (NO) plays an important role in cell signaling, blood pressure, coagulation, and tumor cell killing. A novel GSTP1 and multidrug resistance protein 1-mediated NO storage and transport mechanism (MRP1/ABCC1) protects an M1-macrophage model from the effect of NO (149-153). GSTP1 also reduces the inducible NO synthase (iNOS) protein level. GSTP1 regulates iNOS by affecting S-nitrosylation, dimerization and stability (154). It is also associated with some chemicals in the human body, and 1-octyl-3-methylimidazolium bromide upregulates GSTP1 (155). The compound 4b ('p-cyano-PABA/NO') is more favorable for product distribution in the presence of GSTP1 (156). GSTP1 is also involved in endogenous regulation of cellular signaling pathways (Fig. 2). The c-Jun N-terminal kinase (JNK)-mediated cell signaling pathway is endogenously regulated by protein-protein interactions with GSTP1 (157). It is believed that there is a direct interaction between the C-terminus of JNK and GSTP1, and GSTP1 is considered to act as a key ligand-binding protein that regulates the kinase pathway (158). GSTP1 binds to mitogen-activated protein kinase JNK and inhibits JNK downstream signaling (159). Epidermal growth factor receptor phosphorylation of GSTP1 enhances JNK signaling and provides a survival advantage for tumors (160). GSTP1 acts as a direct inhibitor of JNK in vivo to regulate constitutive expression of specific downstream molecular targets of the JNK signaling pathway (161). The mechanism of GSTP1 protection against serum depletion-induced cell death is mediated through an apoptosis signal-regulating kinase 1 (ASK1) pathway, ASK1-MKK7-JNK (162). There may also be a novel non-enzymatic effect of GSTP, which plays an important role in the regulation of the classical ERα signaling pathway by modification of transcriptional cofactors, such as receptor interacting protein 140 (163). Increased levels of GSTP1 may be another mechanism regulating cyclin-dependent kinase-5 signaling, eliminating oxidative stress, and preventing neurodegeneration (164). Transcriptional activation of the GSTP1 gene is also regulated by the Nrf2 pathway (165). GSTP1 plays an important role in the regulation of signal transduction. Therefore, GSTP1 may be involved in complex processes mediated by multiple factors and multiple signals.
7. Conclusion
As an important phase II detoxification enzyme, GSTP1 is involved in the development and progression of various types of cancer. The expression, methylation and genetic polymorphisms of GSTP1 are closely associated with cancer. GSTP1 plays an important regulatory role in the metabolism, detoxification and elimination of potentially genotoxic foreign complexes. Therefore, GSTP1 may act as a critical regulator in the occurrence and development of multiple cancer types.
Funding
The present study was supported by grants from the Hunan Natural Science Foundation (no. 2019JJ40238), the Defense Industrial Technology Development Program (no. JCKY2016403C001), the National Natural Science Foundation of China (no. 81400117), the China Postdoctoral Science Foundation (no. 2014 M562115) and the Research Initiation Funding of University of South China for the Returned Scholars From Abroad (no. 2014XQD46) and Hunan Province University Students Study and Innovation Pilot Project (no. S201910555122).
Availability of materials and data
Not applicable.
Authors' contributions
JC made substantial contributions to conception and design of the study, acquisition, analysis and interpretation of data, revised the manuscript critically for important intellectual content, and was a major contributor to writing the manuscript. GL, JY, LL, YT, HW, BL, LD, JT and YC were involved in drafting the manuscript. LY made substantial contributions to the conception and design of the study, acquisition, analysis and interpretation of data, and gave final approval of the version to be published.
Ethics approval and consent to participate
Not applicable.
Patient consent for publication
Not applicable.
Competing interests
The authors declare that they have no competing interests.
Abbreviations:
|
AML |
acute myeloid leukemia |
|
BaP |
benzo(a) pyrene |
|
BC |
bladder cancer |
|
CRC |
colorectal cancer |
|
ER |
estrogen receptor |
|
GST |
glutathione-S transferase |
|
GSTP1 |
glutathione S-transferase Pi |
|
GSTM1 |
Mu-class glutathione S-transferase 1 |
|
GSTT1 |
glutathione S-transferase theta 1 |
|
HCC |
hepatocellular carcinoma |
|
HNSCC |
head and neck squamous cell carcinoma |
|
iNOS |
inducible NO synthase |
|
JNK |
c-Jun N-terminal kinase |
|
Mn |
manganese |
|
MRP1 |
multidrug resistance protein 1 |
|
NF-κB |
nuclear factor-κB |
|
NSCLC |
non-small cell lung cancer |
|
NO |
nitric oxide |
|
PCa |
prostate cancer |
|
T2DM |
type-2 diabetes mellitus |
Acknowledgments
Not applicable.
References
|
Townsend DM and Tew KD: The role of glutathione-S-transferase in anti-cancer drug resistance. Oncogene. 22:7369–7375. 2003. View Article : Google Scholar : PubMed/NCBI | |
|
Chatterjee A and Gupta S: The multifaceted role of glutathione S-transferases in cancer. Cancer Lett. 433:33–42. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Eaton DL and Bammler TK: Concise review of the glutathione S-transferases and their significance to toxicology. Toxicol Sci. 49:156–164. 1999. View Article : Google Scholar : PubMed/NCBI | |
|
Ladner JE, Parsons JF, Rife CL, Gilliland GL and Armstrong RN: Parallel evolutionary pathways for glutathione transferases: Structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1. Biochemistry. 43:352–361. 2004. View Article : Google Scholar : PubMed/NCBI | |
|
Hayes JD, Flanagan JU and Jowsey IR: Glutathione transferases. Annu Rev Pharmacol Toxicol. 45:51–88. 2005. View Article : Google Scholar : PubMed/NCBI | |
|
Jakobsson PJ, Morgenstern R, Mancini J, Ford-Hutchinson A and Persson B: Common structural features of MAPEG - a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Sci. 8:689–692. 1999. View Article : Google Scholar : PubMed/NCBI | |
|
Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, et al: Identification, characterization, and crystal structure of the Omega class glutathione transferases. J Biol Chem. 275:24798–24806. 2000. View Article : Google Scholar : PubMed/NCBI | |
|
Miyanishi K, Takayama T, Ohi M, Hayashi T, Nobuoka A, Nakajima T, Takimoto R, Kogawa K, Kato J, Sakamaki S, et al: Glutathione S-transferase-pi overexpression is closely associated with K-ras mutation during human colon carcinogenesis. Gastroenterology. 121:865–874. 2001. View Article : Google Scholar : PubMed/NCBI | |
|
Morel F, Rauch C, Petit E, Piton A, Theret N, Coles B and Guillouzo A: Gene and protein characterization of the human glutathione S-transferase kappa and evidence for a peroxisomal localization. J Biol Chem. 279:16246–16253. 2004. View Article : Google Scholar : PubMed/NCBI | |
|
Nordgard SH, Ritchie MD, Jensrud SD, Motsinger AA, Alnaes GI, Lemmon G, Berg M, Geisler S, Moore JH, Lønning PE, et al: ABCB1 and GST polymorphisms associated with TP53 status in breast cancer. Pharmacogenet Genomics. 17:127–136. 2007. View Article : Google Scholar : PubMed/NCBI | |
|
Vasieva O: The many faces of glutathione transferase pi. Curr Mol Med. 11:129–139. 2011. View Article : Google Scholar : PubMed/NCBI | |
|
Hollman AL, Tchounwou PB and Huang HC: The Association between Gene-Environment Interactions and Diseases Involving the Human GST Superfamily with SNP Variants. Int J Environ Res Public Health. 13:3792016. View Article : Google Scholar : PubMed/NCBI | |
|
Bolt HM and Thier R: Relevance of the deletion polymorphisms of the glutathione S-transferases GSTT1 and GSTM1 in pharmacology and toxicology. Curr Drug Metab. 7:613–628. 2006. View Article : Google Scholar : PubMed/NCBI | |
|
Pinheiro DS, Rocha Filho CR, Mundim CA, Júnior PM, Ulhoa CJ, Reis AA and Ghedini PC: Evaluation of glutathione S-transferase GSTM1 and GSTT1 deletion polymorphisms on type-2 diabetes mellitus risk. PLoS One. 8:e762622013. View Article : Google Scholar : PubMed/NCBI | |
|
Yin Z, Ivanov VN, Habelhah H, Tew K and Ronai Z: Glutathione S-transferase p elicits protection against H2O2-induced cell death via coordinated regulation of stress kinases. Cancer Res. 60:4053–4057. 2000.PubMed/NCBI | |
|
Singh S: Cytoprotective and regulatory functions of glutathione S-transferases in cancer cell proliferation and cell death. Cancer Chemother Pharmacol. 75:1–15. 2015. View Article : Google Scholar | |
|
Salinas AE and Wong MG: Glutathione S-transferases - a review. Curr Med Chem. 6:279–309. 1999.PubMed/NCBI | |
|
Hayes JD and Pulford DJ: The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit Rev Biochem Mol Biol. 30:445–600. 1995. View Article : Google Scholar : PubMed/NCBI | |
|
McIlwain CC, Townsend DM and Tew KD: Glutathione S-transferase polymorphisms: Cancer incidence and therapy. Oncogene. 25:1639–1648. 2006. View Article : Google Scholar : PubMed/NCBI | |
|
Hung RJ, van der Hel O, Tavtigian SV, Brennan P, Boffetta P and Hashibe M: Perspectives on the molecular epidemiology of aerodigestive tract cancers. Mutat Res. 592:102–118. 2005. View Article : Google Scholar : PubMed/NCBI | |
|
Schnekenburger M, Karius T and Diederich M: Regulation of epigenetic traits of the glutathione S-transferase P1 gene: From detoxification toward cancer prevention and diagnosis. Front Pharmacol. 5:1702014. View Article : Google Scholar : PubMed/NCBI | |
|
Brockmöller J, Cascorbi I, Kerb R and Roots I: Combined analysis of inherited polymorphisms in arylamine N-acetyltransferase 2, glutathione S-transferases M1 and T1, microsomal epoxide hydrolase, and cytochrome P450 enzymes as modulators of bladder cancer risk. Cancer Res. 56:3915–3925. 1996.PubMed/NCBI | |
|
Cowell IG, Dixon KH, Pemble SE, Ketterer B and Taylor JB: The structure of the human glutathione S-transferase pi gene. Biochem J. 255:79–83. 1988. View Article : Google Scholar : PubMed/NCBI | |
|
Laborde E: Glutathione transferases as mediators of signaling pathways involved in cell proliferation and cell death. Cell Death Differ. 17:1373–1380. 2010. View Article : Google Scholar : PubMed/NCBI | |
|
Moyer AM, Salavaggione OE, Wu TY, Moon I, Eckloff BW, Hildebrandt MA, Schaid DJ, Wieben ED and Weinshilboum RM: Glutathione s-transferase p1: Gene sequence variation and functional genomic studies. Cancer Res. 68:4791–4801. 2008. View Article : Google Scholar : PubMed/NCBI | |
|
Sau A, Pellizzari Tregno F, Valentino F, Federici G and Caccuri AM: Glutathione transferases and development of new principles to overcome drug resistance. Arch Biochem Biophys. 500:116–122. 2010. View Article : Google Scholar : PubMed/NCBI | |
|
Henderson CJ, McLaren AW, Moffat GJ, Bacon EJ and Wolf CR: Pi-class glutathione S-transferase: Regulation and function. Chem Biol Interact. 111-112:69–82. 1998. View Article : Google Scholar : PubMed/NCBI | |
|
Nelson WG, De Marzo AM, Deweese TL, Lin X, Brooks JD, Putzi MJ, Nelson CP, Groopman JD and Kensler TW: Preneoplastic prostate lesions: An opportunity for prostate cancer prevention. Ann N Y Acad Sci. 952:135–144. 2001. View Article : Google Scholar | |
|
Nelson WG, DeWeese TL and DeMarzo AM: The diet, prostate inflammation, and the development of prostate cancer. Cancer Metastasis Rev. 21:3–16. 2002. View Article : Google Scholar : PubMed/NCBI | |
|
Sawers L, Ferguson MJ, Ihrig BR, Young HC, Chakravarty P, Wolf CR and Smith G: Glutathione S-transferase P1 (GSTP1) directly influences platinum drug chemosensitivity in ovarian tumour cell lines. Br J Cancer. 111:1150–1158. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Hagrman D, Goodisman J and Souid AK: Kinetic study on the reactions of platinum drugs with glutathione. J Pharmacol Exp Ther. 308:658–666. 2004. View Article : Google Scholar | |
|
Zhang J, Wu Y, Hu X, Wang B, Wang L, Zhang S, Cao J and Wang Z: GSTT1, GSTP1, and GSTM1 genetic variants are associated with survival in previously untreated metastatic breast cancer. Oncotarget. 8:105905–105914. 2017.PubMed/NCBI | |
|
Duvoix A, Schnekenburger M, Delhalle S, Blasius R, Borde-Chiché P, Morceau F, Dicato M and Diederich M: Expression of glutathione S-transferase P1-1 in leukemic cells is regulated by inducible AP-1 binding. Cancer Lett. 216:207–219. 2004. View Article : Google Scholar : PubMed/NCBI | |
|
Alqarni MH, Muharram MM and Labrou NE: Ligand-induced glutathione transferase degradation as a therapeutic modality: Investigation of a new metal-mediated affinity cleavage strategy for human GSTP1-1. Int J Biol Macromol. 116:84–90. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Pajaud J, Ribault C, Ben Mosbah I, Rauch C, Henderson C, Bellaud P, Aninat C, Loyer P, Morel F and Corlu A: Glutathione transferases P1/P2 regulate the timing of signaling pathway activations and cell cycle progression during mouse liver regeneration. Cell Death Dis. 6:e15982015. View Article : Google Scholar : PubMed/NCBI | |
|
Morceau F, Duvoix A, Delhalle S, Schnekenburger M, Dicato M and Diederich M: Regulation of glutathione S-transferase P1-1 gene expression by NF-kappaB in tumor necrosis factor alpha-treated K562 leukemia cells. Biochem Pharmacol. 67:1227–1238. 2004. View Article : Google Scholar : PubMed/NCBI | |
|
Duvoix A, Morceau F, Delhalle S, Schmitz M, Schnekenburger M, Galteau MM, Dicato M and Diederich M: Induction of apoptosis by curcumin: Mediation by glutathione S-transferase P1-1 inhibition. Biochem Pharmacol. 66:1475–1483. 2003. View Article : Google Scholar : PubMed/NCBI | |
|
Duvoix A, Delhalle S, Blasius R, Schnekenburger M, Morceau F, Fougère M, Henry E, Galteau MM, Dicato M and Diederich M: Effect of chemopreventive agents on glutathione S-transferase P1-1 gene expression mechanisms via activating protein 1 and nuclear factor kappaB inhibition. Biochem Pharmacol. 68:1101–1111. 2004. View Article : Google Scholar : PubMed/NCBI | |
|
Moscow JA, Fairchild CR, Madden MJ, Ransom DT, Wieand HS, O'Brien EE, Poplack DG, Cossman J, Myers CE and Cowan KH: Expression of anionic glutathione-S-transferase and P-glycoprotein genes in human tissues and tumors. Cancer Res. 49:1422–1428. 1989.PubMed/NCBI | |
|
Mian OY, Khattab MH, Hedayati M, Coulter J, Abubaker-Sharif B, Schwaninger JM, Veeraswamy RK, Brooks JD, Hopkins L, Shinohara DB, et al: GSTP1 Loss results in accumulation of oxidative DNA base damage and promotes prostate cancer cell survival following exposure to protracted oxidative stress. Prostate. 76:199–206. 2016. View Article : Google Scholar : | |
|
Rahbar MH, Samms-Vaughan M, Ma J, Bressler J, Dickerson AS, Hessabi M, Loveland KA, Grove ML, Shakespeare-Pellington S, Beecher C, et al: Synergic effect of GSTP1 and blood manganese concentrations in Autism Spectrum Disorder. Res Autism Spectr Disord. 18:73–82. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Bhang SY, Cho SC, Kim JW, Hong YC, Shin MS, Yoo HJ, Cho IH, Kim Y and Kim BN: Relationship between blood manganese levels and children's attention, cognition, behavior, and academic performance--a nationwide cross-sectional study. Environ Res. 126:9–16. 2013. View Article : Google Scholar : PubMed/NCBI | |
|
Rahbar MH, Samms-Vaughan M, Lee M, Christian MA, Bressler J, Hessabi M, Grove ML, Shakespeare-Pellington S, Desai CC, Reece JA, et al: Interaction between manganese and GSTP1 in relation to autism spectrum disorder while controlling for exposure to mixture of lead, mercury, arsenic, and cadmium. Res Autism Spectr Disord. 55:50–63. 2018. View Article : Google Scholar | |
|
Wright LS, Kornguth SE, Oberley TD and Siegel FL: Effects of lead on glutathione S-transferase expression in rat kidney: A dose-response study. Toxicol Sci. 46:254–259. 1998. | |
|
Li C, Yang X, Xu M, Zhang J and Sun N: Association between GSTP1 CpG methylation and the early phase of lead exposure. Toxicol Mech Methods. 24:111–115. 2014. View Article : Google Scholar | |
|
Kwong YL and Todd D: Delicious poison: Arsenic trioxide for the treatment of leukemia. Blood. 89:3487–3488. 1997. View Article : Google Scholar : PubMed/NCBI | |
|
Liu J, Chen H, Miller DS, Saavedra JE, Keefer LK, Johnson DR, Klaassen CD and Waalkes MP: Overexpression of glutathione S-transferase II and multidrug resistance transport proteins is associated with acquired tolerance to inorganic arsenic. Mol Pharmacol. 60:302–309. 2001. View Article : Google Scholar : PubMed/NCBI | |
|
Parker LJ, Bocedi A, Ascher DB, Aitken JB, Harris HH, Lo Bello M, Ricci G, Morton CJ and Parker MW: Glutathione transferase P1-1 as an arsenic drug-sequestering enzyme. Protein Sci. 26:317–326. 2017. View Article : Google Scholar | |
|
González-Martínez F, Sánchez-Rodas D, Cáceres DD, Martínez MF, Quiñones LA and Johnson-Restrepo B: Arsenic exposure, profiles of urinary arsenic species, and polymorphism effects of glutathione-s-transferase and metallothioneins. Chemosphere. 212:927–936. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Zhou L, Jing Y, Styblo M, Chen Z and Waxman S: Glutathione-S-transferase pi inhibits As2O3-induced apoptosis in lymphoma cells: Involvement of hydrogen peroxide catabolism. Blood. 105:1198–1203. 2005. View Article : Google Scholar | |
|
Van Dyck E, Nazarov PV, Muller A, Nicot N, Bosseler M, Pierson S, Van Moer K, Palissot V, Mascaux C, Knolle U, et al: Bronchial airway gene expression in smokers with lung or head and neck cancer. Cancer Med. 3:322–336. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Krais AM, Mühlbauer KR, Kucab JE, Chinbuah H, Cornelius MG, Wei QX, Hollstein M, Phillips DH, Arlt VM and Schmeiser HH: Comparison of the metabolic activation of environmental carcinogens in mouse embryonic stem cells and mouse embryonic fibroblasts. Toxicol In Vitro. 29:34–43. 2015. View Article : Google Scholar | |
|
Gilliland FD, Harms HJ, Crowell RE, Li YF, Willink R and Belinsky SA: Glutathione S-transferase P1 and NADPH quinone oxidoreductase polymorphisms are associated with aberrant promoter methylation of P16(INK4a) and O(6)-methylguanine-DNA methyltransferase in sputum. Cancer Res. 62:2248–2252. 2002.PubMed/NCBI | |
|
Xue B, Wu Y, Yin Z, Zhang H, Sun S, Yi T and Luo L: Regulation of lipopolysaccharide-induced inflammatory response by glutathione S-transferase P1 in RAW264.7 cells. FEBS Lett. 579:4081–4087. 2005. View Article : Google Scholar : PubMed/NCBI | |
|
Yi L, Li L, Yin J, Hu N, Li G and Ding D: Proteomics analysis of liver tissues from C57BL/6J mice receiving low-dose 137Cs radiation. Environ Sci Pollut Res Int. 23:2549–2556. 2016. View Article : Google Scholar | |
|
Yi L, Hu N, Yin J, Sun J, Mu H, Dai K and Ding D: Up-regulation of calreticulin in mouse liver tissues after long-term irradiation with low-dose-rate gamma rays. PLoS One. 12:e01826712017. View Article : Google Scholar : PubMed/NCBI | |
|
Lu M, Xia L, Luo D, Waxman S and Jing Y: Dual effects of glutathione-S-transferase pi on As2O3 action in prostate cancer cells: Enhancement of growth inhibition and inhibition of apoptosis. Oncogene. 23:3945–3952. 2004. View Article : Google Scholar : PubMed/NCBI | |
|
Fujikawa Y, Nampo T, Mori M, Kikkawa M and Inoue H: Fluorescein diacetate (FDA) and its analogue as substrates for Pi-class glutathione S-transferase (GSTP1) and their biological application. Talanta. 179:845–852. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Wang J, Ren JH, Lin B, Jing YK and Cheng MS: Advances of studies on glutathione-S-transferase π. Zhongguo Yaowu Huaxue Zazhi. 15:251–256. 2005. | |
|
Ranganathan S and Tew KD: Immunohistochemical localization of glutathione S-transferases alpha, mu, and pi in normal tissue and carcinomas from human colon. Carcinogenesis. 12:2383–2387. 1991. View Article : Google Scholar : PubMed/NCBI | |
|
Zhang R, Kang KA, Piao MJ, Kim KC, Zheng J, Yao CW, Cha JW, Maeng YH, Chang WY, Moon PG, et al: Epigenetic alterations are involved in the overexpression of glutathione S-transferase π-1 in human colorectal cancers. Int J Oncol. 45:1275–1283. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Ding XQ, Bi JH, Ma ZG, Jiang ZX, Xi JF, Liu PZ and Zhang B: Correlation of ERCC1 and GSTP1 expression in esophageal cancer tissue with platinum-based chemotherapy sensitivity as well as apoptosis and proliferation gene expression. Hainan Yixueyuan Xuebao. 23:103–107. 2017. | |
|
Song Y, Du Y, Zhou Q, Ma J, Yu J, Tao X and Zhang F: Association of GSTP1 Ile105Val polymorphism with risk of esophageal cancer: A meta-analysis of 21 case-control studies. Int J Clin Exp Med. 7:3215–3224. 2014.PubMed/NCBI | |
|
Pljesa-Ercegovac M, Savic-Radojevic A, Dragicevic D, Mimic-Oka J, Matic M, Sasic T, Pekmezovic T, Vuksanovic A and Simic T: Enhanced GSTP1 expression in transitional cell carcinoma of urinary bladder is associated with altered apoptotic pathways. Urol Oncol. 29:70–77. 2011. View Article : Google Scholar | |
|
Savic-Radojevic A, Mimic-Oka J, Pljesa-Ercegovac M, Opacic M, Dragicevic D, Kravic T, Djokic M, Micic S and Simic T: Glutathione S-transferase-P1 expression correlates with increased antioxidant capacity in transitional cell carcinoma of the urinary bladder. Eur Urol. 52:470–477. 2007. View Article : Google Scholar : PubMed/NCBI | |
|
Gao L, Fang YQ, Zhang TY, Ge B, Xu B, Huang JF, Zhang ZF and Tan N: GSTP1 arrests bladder cancer T24 cells in G0/G1 phase and up-regulates p21 expression. Int J Clin Exp Med. 7:2984–2991. 2014.PubMed/NCBI | |
|
Oguztuzun Serpil, Ergün Duygu, Kilic Murat, Bozer Busra, Simsek Gulcin Güler and Bulus Hakan: The expression of GST and CYP isoenzymes in thyroid nodular hyperplasia and papillary thyroid cancer tissue: Correlation with clinical parameters. Entomol Appl Sci Lett. 5:97–103. 2016. | |
|
Dong X, Yang Y, Zhou Y, Bi X, Zhao N, Zhang Z, Li L, Hang Q, Zhang R, Chen D, et al: Glutathione S-transferases P1 protects breast cancer cell from adriamycin-induced cell death through promoting autophagy. Cell Death Differ. 26:2086–2099. 2019. View Article : Google Scholar : PubMed/NCBI | |
|
Liu X, Tan N, Liao H, Pan G, Xu Q, Zhu R, Zou L, He S and Zhu H: High GSTP1 inhibits cell proliferation by reducing Akt phosphorylation and is associated with a better prognosis in hepatocellular carcinoma. Oncotarget. 9:8957–8971. 2017. | |
|
Depeille P, Cuq P, Passagne I, Evrard A and Vian L: Combined effects of GSTP1 and MRP1 in melanoma drug resistance. Br J Cancer. 93:216–223. 2005. View Article : Google Scholar : PubMed/NCBI | |
|
Lin C, Xie L, Lu Y, Hu Z and Chang J: miR-133b reverses cisplatin resistance by targeting GSTP1 in cisplatin-resistant lung cancer cells. Int J Mol Med. 41:2050–2058. 2018.PubMed/NCBI | |
|
Zong C, Wang J and Shi TM: MicroRNA 130b enhances drug resistance in human ovarian cancer cells. Tumour Biol. 35:12151–12156. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Uchida Y, Chiyomaru T, Enokida H, Kawakami K, Tatarano S, Kawahara K, Nishiyama K, Seki N and Nakagawa M: MiR-133a induces apoptosis through direct regulation of GSTP1 in bladder cancer cell lines. Urol Oncol. 31:115–123. 2013. View Article : Google Scholar | |
|
Mutallip M, Nohata N, Hanazawa T, Kikkawa N, Horiguchi S, Fujimura L, Kawakami K, Chiyomaru T, Enokida H, Nakagawa M, et al: Glutathione S-transferase P1 (GSTP1) suppresses cell apoptosis and its regulation by miR-133α in head and neck squamous cell carcinoma (HNSCC). Int J Mol Med. 27:345–352. 2011. | |
|
Zhu J, Zhang R, Yang D, Li J, Yan X, Jin K, Li W, Liu X, Zhao J, Shang W, et al: Knockdown of Long Non-Coding RNA XIST Inhibited Doxorubicin Resistance in Colorectal Cancer by Upregulation of miR-124 and Downregulation of SGK1. Cell Physiol Biochem. 51:113–128. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Zhang X, Zhu J, Xing R, Tie Y, Fu H, Zheng X and Yu B: miR-513a-3p sensitizes human lung adenocarcinoma cells to chemotherapy by targeting GSTP1. Lung Cancer. 77:488–494. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Song X, Wang R, Xiao F, Zhang SX, Gong M, Wang XL, Zhang Y and Huang JY: Expressions of glutathione S-transferase P1 and 4-hydroxynonenal and the progression of prostate cancer. Zhonghua Nan Ke Xue. 23:412–416. 2017.In Chinese. | |
|
Singh S, Shukla GC and Gupta S: MicroRNA Regulating Glutathione S-Transferase P1 in Prostate Cancer. Curr Pharmacol Rep. 1:79–88. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Kanwal R, Pandey M, Bhaskaran N, Maclennan GT, Fu P, Ponsky LE and Gupta S: Protection against oxidative DNA damage and stress in human prostate by glutathione S-transferase P1. Mol Carcinog. 53:8–18. 2014. View Article : Google Scholar : | |
|
Miyake T, Nakayama T, Naoi Y, Yamamoto N, Otani Y, Kim SJ, Shimazu K, Shimomura A, Maruyama N, Tamaki Y, et al: GSTP1 expression predicts poor pathological complete response to neoadjuvant chemotherapy in ER-negative breast cancer. Cancer Sci. 103:913–920. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Gurioli G, Martignano F, Salvi S, Costantini M, Gunelli R and Casadio V: GSTP1 methylation in cancer: A liquid biopsy biomarker? Clin Chem Lab Med. 56:702–717. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Li Y, Cai Y, Chen H and Mao L: Clinical significance and association of GSTP1 hypermethylation with hepatocellular carcinoma: A meta-analysis. J Cancer Res Ther. 14(Suppl): S486–S489. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Li QF, Li QY, Gao AR and Shi QF: Correlation between promoter methylation in the GSTP1 gene and hepatocellular carcinoma development: A meta-analysis. Genet Mol Res. 14:6762–6772. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Jain S, Chen S, Chang KC, Lin YJ, Hu CT, Boldbaatar B, Hamilton JP, Lin SY, Chang TT, Chen SH, et al: Impact of the location of CpG methylation within the GSTP1 gene on its specificity as a DNA marker for hepatocellular carcinoma. PLoS One. 7:e357892012. View Article : Google Scholar : PubMed/NCBI | |
|
Qu Z, Jiang Y, Li H, Yu DC and Ding YT: Detecting abnormal methylation of tumor suppressor genes GSTP1, P16, RIZ1, and RASSF1A in hepatocellular carcinoma and its clinical significance. Oncol Lett. 10:2553–2558. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Gao S, Sun FK, Fan YC, Shi CH, Zhang ZH, Wang LY and Wang K: Aberrant GSTP1 promoter methylation predicts short-term prognosis in acute-on-chronic hepatitis B liver failure. Aliment Pharmacol Ther. 42:319–329. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Costa VL, Henrique R and Jerónimo C: Epigenetic markers for molecular detection of prostate cancer. Dis Markers. 23:31–41. 2007. View Article : Google Scholar : PubMed/NCBI | |
|
Goering W, Kloth M and Schulz WA: DNA methylation changes in prostate cancer. Methods Mol Biol. 863:47–66. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Maldonado L, Brait M, Loyo M, Sullenberger L, Wang K, Peskoe SB, Rosenbaum E, Howard R, Toubaji A, Albadine R, et al: GSTP1 promoter methylation is associated with recurrence in early stage prostate cancer. J Urol. 192:1542–1548. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Zelic R, Fiano V, Zugna D, Grasso C, Delsedime L, Daniele L, Galliano D, Pettersson A, Gillio-Tos A, Merletti F, et al: Global Hypomethylation (LINE-1) and Gene-Specific Hypermethylation (GSTP1) on Initial Negative Prostate Biopsy as Markers of Prostate Cancer on a Rebiopsy. Clin Cancer Res. 22:984–992. 2016. View Article : Google Scholar | |
|
Lee WH, Morton RA, Epstein JI, Brooks JD, Campbell PA, Bova GS, Hsieh WS, Isaacs WB and Nelson WG: Cytidine methylation of regulatory sequences near the pi-class glutathione S-transferase gene accompanies human prostatic carcinogenesis. Proc Natl Acad Sci USA. 91:11733–11737. 1994. View Article : Google Scholar : PubMed/NCBI | |
|
Haluskova J, Lachvac L and Nagy V: The investigation of GSTP1, APC and RASSF1 gene promoter hypermethylation in urine DNA of prostate-diseased patients. Bratisl Lek Listy. 116:79–82. 2015.PubMed/NCBI | |
|
Lee JS: GSTP1 promoter hypermethylation is an early event in breast carcinogenesis. Virchows Arch. 450:637–642. 2007. View Article : Google Scholar : PubMed/NCBI | |
|
Alnaes GI, Ronneberg JA, Kristensen VN and Tost J: Heterogeneous DNA Methylation Patterns in the GSTP1 Promoter Lead to Discordant Results between Assay Technologies and Impede Its Implementation as Epigenetic Biomarkers in Breast Cancer. Genes (Basel). 6:878–900. 2015. View Article : Google Scholar | |
|
Miyake T, Nakayama T, Kagara N, Yamamoto N, Nakamura Y, Otani Y, Uji K, Naoi Y, Shimoda M, Maruyama N, et al: Association of GSTP1 methylation with aggressive phenotype in ER-positive breast cancer. Anticancer Res. 33:5617–5623. 2013.PubMed/NCBI | |
|
Muggerud AA, Rønneberg JA, Wärnberg F, Botling J, Busato F, Jovanovic J, Solvang H, Bukholm I, Børresen-Dale AL, Kristensen VN, et al: Frequent aberrant DNA methylation of ABCB1, FOXC1, PPP2R2B and PTEN in ductal carcinoma in situ and early invasive breast cancer. Breast Cancer Res. 12:R32010. View Article : Google Scholar : PubMed/NCBI | |
|
Feng W, Shen L, Wen S, Rosen DG, Jelinek J, Hu X, Huan S, Huang M, Liu J, Sahin AA, et al: Correlation between CpG methylation profiles and hormone receptor status in breast cancers. Breast Cancer Res. 9:R572007. View Article : Google Scholar : PubMed/NCBI | |
|
Sunami E, Shinozaki M, Sim MS, Nguyen SL, Vu AT, Giuliano AE and Hoon DS: Estrogen receptor and HER2/neu status affect epigenetic differences of tumor-related genes in primary breast tumors. Breast Cancer Res. 10:R462008. View Article : Google Scholar : PubMed/NCBI | |
|
Song B, Wang L, Zhang Y, Li N, Dai H, Xu H, Cai H and Yan J: Combined Detection of HER2, Ki67, and GSTP1 Genes on the Diagnosis and Prognosis of Breast Cancer. Cancer Biother Radiopharm. 34:85–90. 2019. View Article : Google Scholar | |
|
Yanagawa N, Tamura G, Oizumi H, Takahashi N, Shimazaki Y and Motoyama T: Promoter hypermethylation of tumor suppressor and tumor-related genes in non-small cell lung cancers. Cancer Sci. 94:589–592. 2003. View Article : Google Scholar : PubMed/NCBI | |
|
Russo AL, Thiagalingam A, Pan H, Califano J, Cheng KH, Ponte JF, Chinnappan D, Nemani P, Sidransky D and Thiagalingam S: Differential DNA hypermethylation of critical genes mediates the stage-specific tobacco smoke-induced neoplastic progression of lung cancer. Clin Cancer Res. 11:2466–2470. 2005. View Article : Google Scholar : PubMed/NCBI | |
|
Vaissière T, Hung RJ, Zaridze D, Moukeria A, Cuenin C, Fasolo V, Ferro G, Paliwal A, Hainaut P, Brennan P, et al: Quantitative analysis of DNA methylation profiles in lung cancer identifies aberrant DNA methylation of specific genes and its association with gender and cancer risk factors. Cancer Res. 69:243–252. 2009. View Article : Google Scholar : PubMed/NCBI | |
|
Haroun RA, Zakhary NI, Mohamed MR, Abdelrahman AM, Kandil EI and Shalaby KA: Assessment of the prognostic value of methylation status and expression levels of FHIT, GSTP1 and p16 in non-small cell lung cancer in Egyptian patients. Asian Pac J Cancer Prev. 15:4281–4287. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Drilon A, Sugita H, Sima CS, Zauderer M, Rudin CM, Kris MG, Rusch VW and Azzoli CG: A prospective study of tumor suppressor gene methylation as a prognostic biomarker in surgically resected stage I to IIIA non-small-cell lung cancers. J Thorac Oncol. 9:1272–1277. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Kim DS, Cha SI, Lee JH, Lee YM, Choi JE, Kim MJ, Lim JS, Lee EB, Kim CH, Park TI, et al: Aberrant DNA methylation profiles of non-small cell lung cancers in a Korean population. Lung Cancer. 58:1–6. 2007. View Article : Google Scholar : PubMed/NCBI | |
|
Gumy-Pause F, Pardo B, Khoshbeen-Boudal M, Ansari M, Gayet-Ageron A, Sappino AP, Attiyeh EF and Ozsahin H: GSTP1 hypermethylation is associated with reduced protein expression, aggressive disease and prognosis in neuroblastoma. Genes Chromosomes Cancer. 51:174–185. 2012. View Article : Google Scholar | |
|
Ferraù F, Romeo PD, Puglisi S, Ragonese M, Spagnolo F, Salpietro C, Ientile R, Currò M, Visalli G, Alibrandi A, et al: GSTP1 gene methylation and AHR rs2066853 variant predict resistance to first generation somatostatin analogs in patients with acromegaly. J Endocrinol Invest. 2018. | |
|
Ali-Osman F, Akande O, Antoun G, Mao JX and Buolamwini J: Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins. J Biol Chem. 272:10004–10012. 1997. View Article : Google Scholar : PubMed/NCBI | |
|
Cote ML, Chen W, Smith DW, Benhamou S, Bouchardy C, Butkiewicz D, Fong KM, Gené M, Hirvonen A, Kiyohara C, et al: Meta- and pooled analysis of GSTP1 polymorphism and lung cancer: A HuGE-GSEC review. Am J Epidemiol. 169:802–814. 2009. View Article : Google Scholar : PubMed/NCBI | |
|
Pérez-Ramírez C, Cañadas-Garre M, Alnatsha A, Villar E, Delgado JR, Calleja-Hernández MÁ and Faus-Dáder MJ: Impact of DNA repair, folate and glutathione gene polymorphisms on risk of non small cell lung cancer. Pathol Res Pract. 214:44–52. 2018. View Article : Google Scholar | |
|
Saarikoski ST, Voho A, Reinikainen M, Anttila S, Karjalainen A, Malaveille C, Vainio H, Husgafvel-Pursiainen K and Hirvonen A: Combined effect of polymorphic GST genes on individual susceptibility to lung cancer. Int J Cancer. 77:516–521. 1998. View Article : Google Scholar : PubMed/NCBI | |
|
Li XM, Yu XW, Yuan Y, Pu MZ, Zhang HX, Wang KJ and Han XD: Glutathione S-transferase P1, gene-gene interaction, and lung cancer susceptibility in the Chinese population: An updated meta-analysis and review. J Cancer Res Ther. 11:565–570. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Tarek F: Role of glutathione S-transferase P-1 (GSTP-1) gene polymorphism in COPD patients. Egypt J Chest Dis Tuberc. 65:739–744. 2016. View Article : Google Scholar | |
|
Lakhdar R, Denden S, Knani J, Leban N, Daimi H, Hassine M, Lefranc G, Ben Chibani J and Haj Khelil A: Relationship between glutathione S-transferase P1 polymorphisms and chronic obstructive pulmonary disease in a Tunisian population. Genet Mol Res. 9:897–907. 2010. View Article : Google Scholar : PubMed/NCBI | |
|
Wang Y, Ren BU, Zhang L and Guo Z: Correlation between metabolic enzyme GSTP1 polymorphisms and susceptibility to lung cancer. Exp Ther Med. 10:1521–1527. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
He L, Gao L, Shi Z, Li Y, Zhu L, Li S, Zhang P, Zheng G, Ren Q, Li Y, et al: Involvement of cytochrome P450 1A1 and glutathione S-transferase P1 polymorphisms and promoter hypermethylation in the progression of anti-tuberculosis drug-induced liver injury: A case-control study. PLoS One. 10:e01194812015. View Article : Google Scholar : PubMed/NCBI | |
|
Qu K, Liu SS, Wang ZX, Huang ZC, Liu SN, Chang HL, Xu XS, Lin T, Dong YF and Liu C: Polymorphisms of glutathione S-transferase genes and survival of resected hepatocellular carcinoma patients. World J Gastroenterol. 21:4310–4322. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Song QB, Wang Q and Hu WG: A systemic review of glutathione S-transferase P1 Ile105Val polymorphism and colorectal cancer risk. Chin J Cancer Res. 26:255–267. 2014.PubMed/NCBI | |
|
Lei Z, Liu T, Li X, Xu X and Fan D: Contribution of glutathione S-transferase gene polymorphisms to development of skin cancer. Int J Clin Exp Med. 8:377–386. 2015.PubMed/NCBI | |
|
Lira MG, Provezza L, Malerba G, Naldi L, Remuzzi G, Boschiero L, Forni A, Rugiu C, Piaserico S, Alaibac M, et al: Glutathione S-transferase and CYP1A1 gene polymorphisms and non-melanoma skin cancer risk in Italian transplanted patients. Exp Dermatol. 15:958–965. 2006. View Article : Google Scholar : PubMed/NCBI | |
|
Gsur A, Haidinger G, Hinteregger S, Bernhofer G, Schatzl G, Madersbacher S, Marberger M, Vutuc C and Micksche M: Polymorphisms of glutathione-S-transferase genes (GSTP1, GSTM1 and GSTT1) and prostate-cancer risk. Int J Cancer. 95:152–155. 2001. View Article : Google Scholar : PubMed/NCBI | |
|
Harries LW, Stubbins MJ, Forman D, Howard GC and Wolf CR: Identification of genetic polymorphisms at the glutathione S-transferase Pi locus and association with susceptibility to bladder, testicular and prostate cancer. Carcinogenesis. 18:641–644. 1997. View Article : Google Scholar : PubMed/NCBI | |
|
Chen ZH, Xian JF and Luo LP: Association between GSTM1, GSTT1, and GSTP1 polymorphisms and gastric cancer risk, and their interactions with environmental factors. Genet Mol Res. 16:gmr160188772017. View Article : Google Scholar | |
|
Nguyen TV, Janssen MJ, van Oijen MG, Bergevoet SM, te Morsche RH, van Asten H, Laheij RJ, Peters WH and Jansent JB: Genetic polymorphisms in GSTA1, GSTP1, GSTT1, and GSTM1 and gastric cancer risk in a Vietnamese population. Oncol Res. 18:349–355. 2010. View Article : Google Scholar : PubMed/NCBI | |
|
Negovan A, Iancu M, Moldovan V, Mocan S and Banescu C: The Interaction between GSTT1, GSTM1, and GSTP1 Ile105Val Gene Polymorphisms and Environmental Risk Factors in Premalignant Gastric Lesions Risk. BioMed Res Int. 2017:73650802017. View Article : Google Scholar : | |
|
Tripathi S, Ghoshal U, Ghoshal UC, Mittal B, Krishnani N, Chourasia D, Agarwal AK and Singh K: Gastric carcinogenesis: Possible role of polymorphisms of GSTM1, GSTT1, and GSTP1 genes. Scand J Gastroenterol. 43:431–439. 2008. View Article : Google Scholar : PubMed/NCBI | |
|
Jiao L, Bondy ML, Hassan MM, Chang DZ, Abbruzzese JL, Evans DB, Smolensky MH and Li D: Glutathione S-transferase gene polymorphisms and risk and survival of pancreatic cancer. Cancer. 109:840–848. 2007. View Article : Google Scholar : PubMed/NCBI | |
|
Liu S, Yi Z, Ling M, Shi J, Qiu Y and Yang S: Predictive potential of ABCB1, ABCC3, and GSTP1 gene polymorphisms on osteosarcoma survival after chemotherapy. Tumour Biol. 35:9897–9904. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Wei L, Song XR, Wang XW, Li M and Zuo WS: Expression of MDR1 and GST-pi in osteosarcoma and soft tissue sarcoma and their correlation with chemotherapy resistance. Zhonghua Zhong Liu Za Zhi. 28:445–448. 2006.In Chinese. PubMed/NCBI | |
|
Zhang SL, Mao NF, Sun JY, Shi ZC, Wang B and Sun YJ: Predictive potential of glutathione S-transferase polymorphisms for prognosis of osteosarcoma patients on chemotherapy. Asian Pac J Cancer Prev. 13:2705–2709. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Yang LM, Li XH and Bao CF: Glutathione S-transferase P1 and DNA polymorphisms influence response to chemotherapy and prognosis of bone tumors. Asian Pac J Cancer Prev. 13:5883–5886. 2012. View Article : Google Scholar | |
|
Ben Ami T, Sarig O, Sprecher E and Goldberg I: Glutathione S-transferase polymorphisms in patients with photosensitive and non-photosensitive drug eruptions. Photodermatol Photoimmunol Photomed. 35:214–220. 2019. View Article : Google Scholar : PubMed/NCBI | |
|
Rajesh D, Balakrishna S, Azeem Mohiyuddin SM, Suryanarayana R and Kutty AVM: Novel association of oral squamous cell carcinoma with GSTP1 Arg187Trp gene polymorphism. J Cell Biochem. 120:5906–5912. 2019. View Article : Google Scholar | |
|
Dunna NR, Vuree S, Kagita S, Surekha D, Digumarti R, Rajappa S and Satti V: Association of GSTP1 gene (I105V) polymorphism with acute leukaemia. J Genet. 91:e60–e63. 2012.PubMed/NCBI | |
|
Allan JM, Wild CP, Rollinson S, Willett EV, Moorman AV, Dovey GJ, Roddam PL, Roman E, Cartwright RA and Morgan GJ: Polymorphism in glutathione S-transferase P1 is associated with susceptibility to chemotherapy-induced leukemia. Proc Natl Acad Sci USA. 98:11592–11597. 2001. View Article : Google Scholar : PubMed/NCBI | |
|
Daraki A, Zachaki S, Rosmaraki F, Kalomoiraki M, Aleporou-Marinou V, Sambani C, Kollia P and Manola KN: Association of GSTP1 inactivating polymorphism with acute myeloid leukemia and its specific chromosomal abnormalities. Leuk Lymphoma. 58:2505–2507. 2017. View Article : Google Scholar : PubMed/NCBI | |
|
Bănescu C, Iancu M, Trifa AP, Cândea M, Benedek Lazar E, Moldovan VG, Duicu C, Tripon F, Crauciuc A and Dobreanu M: From Six Gene Polymorphisms of the Antioxidant System, Only GPX Pro198Leu and GSTP1 Ile105Val Modulate the Risk of Acute Myeloid Leukemia. Oxid Med Cell Longev. 2016:25367052016. View Article : Google Scholar | |
|
Bănescu C, Trifa AP, Voidăzan S, Moldovan VG, Macarie I, Benedek Lazar E, Dima D, Duicu C and Dobreanu M: CAT, GPX1, MnSOD, GSTM1, GSTT1, and GSTP1 genetic polymorphisms in chronic myeloid leukemia: A case-control study. Oxid Med Cell Longev. 2014:8758612014. View Article : Google Scholar | |
|
He HR, Zhang XX, Sun JY, Hu SS, Ma Y, Dong YL and Lu J: Glutathione S-transferase gene polymorphisms and susceptibility to chronic myeloid leukemia. Tumour Biol. 35:6119–6125. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Sailaja K, Surekha D, Rao DN, Rao DR and Vishnupriya S: Association of the GSTP1 gene (Ile105Val) polymorphism with chronic myeloid leukemia. Asian Pac J Cancer Prev. 11:461–464. 2010.PubMed/NCBI | |
|
Kasznicki J, Kosmalski M, Sliwinska A, Mrowicka M, Stanczyk M, Majsterek I and Drzewoski J: Evaluation of oxidative stress markers in pathogenesis of diabetic neuropathy. Mol Biol Rep. 39:8669–8678. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Stoian A, Bănescu C, Bălaşa RI, Moţăţăianu A, Stoian M, Moldovan VG, Voidăzan S and Dobreanu M: Influence of GSTM1, GSTT1, and GSTP1 Polymorphisms on Type 2 Diabetes Mellitus and Diabetic Sensorimotor Peripheral Neuropathy Risk. Dis Markers. 2015:6386932015. View Article : Google Scholar : PubMed/NCBI | |
|
Qiu YH, Xu YL and Zhang WH: Effect of GSTM1, GSTT1, and GSTP1 IIe105Val polymorphisms on susceptiblity to gestational diabetes mellitus. Genet Mol Res. 15:gmr.150277112016. View Article : Google Scholar | |
|
Mir O, Alexandre J, Tran A, Durand JP, Pons G, Treluyer JM and Goldwasser F: Relationship between GSTP1 Ile(105)Val polymorphism and docetaxel-induced peripheral neuropathy: Clinical evidence of a role of oxidative stress in taxane toxicity. Ann Oncol. 20:736–740. 2009. View Article : Google Scholar : PubMed/NCBI | |
|
Gajewska B, Kaźmierczak B, Kuźma-Kozakiewicz M, Jamrozik Z and Barańczyk-Kuźma A: GSTP1 Polymorphisms and their Association with Glutathione Transferase and Peroxidase Activities in Patients with Motor Neuron Disease. CNS Neurol Disord Drug Targets. 14:1328–1333. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Pastor S, Rodríguez-Ribera L, Corredor Z, da Silva Filho MI, Hemminki K, Coll E, Försti A and Marcos R: Levels of DNA damage (Micronuclei) in patients suffering from chronic kidney diseaseRole of GST polymorphisms. Mutat Res Genet Toxicol Environ Mutagen. 836(Pt A): 41–46. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Agusa T, Kunito T, Tue NM, Lan VT, Fujihara J, Takeshita H, Minh TB, Trang PT, Takahashi S, Viet PH, et al: Individual variations in arsenic metabolism in Vietnamese: The association with arsenic exposure and GSTP1 genetic polymorphism. Metallomics. 4:91–100. 2012. View Article : Google Scholar | |
|
Stoyanova E, Pastor S, Coll E, Azqueta A, Collins AR and Marcos R: Base excision repair capacity in chronic renal failure patients undergoing hemodialysis treatment. Cell Biochem Funct. 32:177–182. 2014. View Article : Google Scholar | |
|
Lok HC, Suryo Rahmanto Y, Hawkins CL, Kalinowski DS, Morrow CS, Townsend AJ, Ponka P and Richardson DR: Nitric oxide storage and transport in cells are mediated by glutathione S-transferase P1-1 and multidrug resistance protein 1 via dinitrosyl iron complexes. J Biol Chem. 287:607–618. 2012. View Article : Google Scholar : | |
|
Suryo Rahmanto Y, Kalinowski DS, Lane DJ, Lok HC, Richardson V and Richardson DR: Nitrogen monoxide (NO) storage and transport by dinitrosyl-dithiol-iron complexes: Long-lived NO that is trafficked by interacting proteins. J Biol Chem. 287:6960–6968. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Lok HC, Sahni S, Richardson V, Kalinowski DS, Kovacevic Z, Lane DJ and Richardson DR: Glutathione S-transferase and MRP1 form an integrated system involved in the storage and transport of dinitrosyldithiolato iron complexes in cells. Free Radic Biol Med. 75:14–29. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Lok HC, Sahni S, Jansson PJ, Kovacevic Z, Hawkins CL and Richardson DR: A Nitric Oxide Storage and Transport System That Protects Activated Macrophages from Endogenous Nitric Oxide Cytotoxicity. J Biol Chem. 291:27042–27061. 2016. View Article : Google Scholar : PubMed/NCBI | |
|
Kovacevic Z, Sahni S, Lok H, Davies MJ, Wink DA and Richardson DR: Regulation and control of nitric oxide (NO) in macrophages: Protecting the "professional killer cell" from its own cytotoxic arsenal via MRP1 and GSTP1. Biochim Biophys Acta, Gen Subj. 1861(5 Pt A): 995–999. 2017. View Article : Google Scholar | |
|
Cao X, Kong X, Zhou Y, Lan L, Luo L and Yin Z: Glutathione S-transferase P1 suppresses iNOS protein stability in RAW264.7 macrophage-like cells after LPS stimulation. Free Radic Res. 49:1438–1448. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Zhang B, Jing C, Li X and Wang J: Effect of 1-octyl-3-methyl-imidazolium bromide on the expressions of CYP1A1, CYP1A2, CYP3A4, and GSTP1, and the receptors AhR, ARNT, and PXR in HepG2 cells. J Toxicol Toxin Rev. 34:72015. View Article : Google Scholar | |
|
Kim Y, Maciag AE, Cao Z, Deschamps JR, Saavedra JE, Keefer LK and Holland RJ: PABA/NO lead optimization: Improved targeting of cytotoxicity to glutathione S-transferase P1-overexpressing cancer cells. Bioorg Med Chem. 23:4980–4988. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Adler V, Yin Z, Fuchs SY, Benezra M, Rosario L, Tew KD, Pincus MR, Sardana M, Henderson CJ, Wolf CR, et al: Regulation of JNK signaling by GSTp. EMBO J. 18:1321–1334. 1999. View Article : Google Scholar : PubMed/NCBI | |
|
Wang T, Arifoglu P, Ronai Z and Tew KD: Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus. J Biol Chem. 276:20999–21003. 2001. View Article : Google Scholar : PubMed/NCBI | |
|
Tew KD and Townsend DM: Regulatory functions of glutathione S-transferase P1-1 unrelated to detoxification. Drug Metab Rev. 43:179–193. 2011. View Article : Google Scholar : PubMed/NCBI | |
|
Okamura T, Antoun G, Keir ST, Friedman H, Bigner DD and Ali-Osman F: Phosphorylation of Glutathione S-Transferase P1 (GSTP1) by Epidermal Growth Factor Receptor (EGFR) Promotes Formation of the GSTP1-c-Jun N-terminal kinase (JNK) Complex and Suppresses JNK Downstream Signaling and Apoptosis in Brain Tumor Cells. J Biol Chem. 290:30866–30878. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Elsby R, Kitteringham NR, Goldring CE, Lovatt CA, Chamberlain M, Henderson CJ, Wolf CR and Park BK: Increased constitutive c-Jun N-terminal kinase signaling in mice lacking glutathione S-transferase Pi. J Biol Chem. 278:22243–22249. 2003. View Article : Google Scholar : PubMed/NCBI | |
|
Yin ZM, Liu AH and Jiang Y: Glutathione S-transferase pi Protects Serum Depletion-induced Cell Death by Inhibiting ASK1-MKK7-JNK Pathway in the 293 Cells. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 33:185–190. 2001. | |
|
Liu X, An BH, Kim MJ, Park JH, Kang YS and Chang M: Human glutathione S-transferase P1-1 functions as an estrogen receptor α signaling modulator. Biochem Biophys Res Commun. 452:840–844. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Sun KH, Chang KH, Clawson S, Ghosh S, Mirzaei H, Regnier F and Shah K: Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase activity. J Neurochem. 118:902–914. 2011. View Article : Google Scholar : PubMed/NCBI | |
|
Wan Hasan WN, Kwak MK, Makpol S, Wan Ngah WZ and Mohd Yusof YA: Piper betle induces phase I & II genes through Nrf2/ARE signaling pathway in mouse embryonic fibroblasts derived from wild type and Nrf2 knockout cells. BMC Complement Altern Med. 14:722014. View Article : Google Scholar : |
