Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.5.1.18 (glutathione S-transferase)
 22,582 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We report that the C-terminal domain of skeletal muscle dystrophin expressed as a fusion protein with glutathione S-transferase (designated GST-CT-1) is a substrate for Ca2+/calmodulin-dependent phosphorylation and dephosphorylation. GST-CT-1 and GST-CT-1F (GST-CT-1 truncated by 20-25 residues) were phosphorylated by Ca2+/calmodulin-dependent protein kinase II (CaM kinase II). The stoichiometries of phosphorylation by CaM kinase II were 1.65 mol of Pi/mol of GST-CT-1 and 0.39 mol of Pi/mol of GST-CT-1F, respectively, suggesting that the principal site(s) of phosphorylation is (are) located in the C-terminal 20-25 residues that are missing from GST-CT-1F. The GST-CT-1 fusion protein was phosphorylated on both serine and threonine residues, whereas GST-CT-1F was phosphorylated only on serine. CaM kinase II-phosphorylated GST-CT-1 and GST-CT-1F were efficiently dephosphorylated by calcineurin, a Ca2+/calmodulin-dependent protein phosphatase (type 2B protein phosphatase). Importantly, calcineurin was found to be associated with a purified sarcolemmal membrane preparation enriched in dystrophin. Type 2A protein phosphatase isolated from smooth muscle (SMP-I) and its catalytic subunit (SMP-ic) also dephosphorylated GST-CT-1, but were less active toward these substrates than was calcineurin. Type 2C phosphatase (SMP-II) and type 1 protein phosphatases [SMP-III, SMP-IV, and myosin-associated phosphatase (PP1M) of smooth muscle and skeletal muscle protein phosphatase 1c] were ineffective in dephosphorylating the C-terminal region of dystrophin.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Characterization of the recombinant C-terminal domain of dystrophin: phosphorylation by calmodulin-dependent protein kinase II and dephosphorylation by type 2B protein phosphatase. 772 17

The influence of ionol (100mg/kg) on the rate of superoxide generation (V) and activities of antioxidant enzymes: CuZn- and Mn-SOD, glutathione peroxidase (GSH-Px), glutathione S-transferase (GST) in different subcellular organelles of mice liver was studied. Ionol is shown to result in realiable a synchronous changes of all studied antioxidant enzyme activities in cytosol and whole blood. On the first day the level of these enzymes increased by 1.5 times and on the third day it returned to normal. The obtained data indicate retention of regulatory relation in antioxidant system in liver cytosol within the sector SOD-GSH-Px. In the mitochondria the Mn-SOD activity changes in antibate manner as compared CuZn-SOD activity, on the first day Mn-SOD activity decreases and remains on lowered level during the whole period investigated. In microsomes the value of V is found to be reduced. In the case of SMP on the first day after the administration of ionol V value didn't increase significantly. However, owing to Mn-SOD activity decrease the ratio V/A, showing the level of superoxide radicals in subcellular organelles grows 3-fold. In nuclei V value increases 4-6-fold during 1-3 hours after ionol injection. The data obtained show that administration of high dose of ionol to intact mice suppresses antioxidant enzyme system of mitochondria, induces abrupt production of superoxide radicals in nuclei and reduces of functioning of electron transport chaine in microsomes. The observed disturbances have short-lived character and are normalized during 3 days after administration of ionol. The toxic effects of ionol may be connected with the action of oxidative modification products formed in organism.
 ...
PMID:[Effect of ionol on superoxide radical metabolism in murine liver]. 1054 81