Disease relevance of Mgst1

• However, the mechanism underlying the association between reduction in Gst pi expression and hepatoprotective effect against APAP toxicity remains to be further explored [1].

High impact information on Mgst1

• This review describes the three mammalian glutathione transferase (GST) families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated MAPEG [2].
• Our data clearly show that As(3+)-, Cd(2+)-, and Cr(6+)-induced oxidative stress modulates Cyp1a1 at transcriptional and posttranscriptional levels but induces Nqo1 and Gst ya at the transcriptional level [3].
• This report reveals a potential novel strategy to enhance the detoxification of APAP or other xenobiotics by manipulating Gst activity through RXRalpha-mediated pathways [4].
• On the other hand, all three metals, alone or in the presence of TCDD, enhanced Nqo1 and Gst ya mRNA levels and Nqo1 activity [3].
• Furthermore, hepatocyte RXRalpha deficiency altered the gene expression profile of the glutathione S-transferase (Gst) family [4].

Biological context of Mgst1

• Microsomal glutathione S-transferase 1 in the retinal pigment epithelium: protection against oxidative stress and a potential role in aging [5].
• Structural organization of the murine microsomal glutathione S-transferase gene (MGST1) from the 129/SvJ strain: identification of the promoter region and a comprehensive examination of tissue expression [6].

Anatomical context of Mgst1

• Finally, Mgst1 and Gpx3 expression appeared to be lower in canine heart and testis than seen in rodents [7].
• Here microsomal glutathione S-transferase (MGST1) is shown to be a dominant, highly expressed enzyme in bovine and mouse RPE microsomes that displays significant reduction activity toward synthetic peroxides, oxidized RPE lipids, and oxidized retinoids [5].
• The specific activity of microsomal glutathione S-transferase also was increased by long-term DHEA treatment; however, its activity was approximately one-tenth of that in corresponding cytosols [8].

Associations of Mgst1 with chemical compounds

• Microsomal GST was not consistently effected by tridiphane [9].
• The RNA synthesis inhibitor actinomycin D significantly inhibited the Nqo1 and Gst ya mRNA induction in response to metals, indicating a requirement of de novo RNA synthesis [10].
• By comparison, oltipraz only significantly elevated the mRNA of Gst mu, adding to the conclusion that across the entire study, no selenium compound appears to be acting purely through the antioxidant response typified by oltipraz [11].
• A comparison of induction of microsomal glutathione S-transferase activity in the liver of the mouse and rat by dietary 2(3)-tert-butyl-4-hydroxyanisole (BHA) [12].

Other interactions of Mgst1

• The cDNA was isolated by RT-PCR using primers designed from published cDNA sequence of rat MGST with the addition of 5' Nde-1 and 3' HindIII sites, and cloned into bacterial expression vector pSP19T7LT [13].
• The liver microsomal glutathione S-transferase activity, which is known to be activated by oxidative stress or active metabolites, was increased by CCl(4) treatment and the increase was also depressed by pretreatment with the mold antioxidant [14].

Analytical, diagnostic and therapeutic context of Mgst1

• Immunoblotting revealed that the in vivo expression of MGST1 in mouse RPE decreases 3-4-fold with age, to trace levels in 18-month-old mice [5].
• By double immunodiffusion, microsomal glutathione S-transferase were shown to have a complete immunological identity with cytosolic F2 and F3 transferase from mouse liver [15].

References