High impact information on Hagh

• Several esterases, including phospholipase A2, glyoxalase II, and acetylcholinesterase, did not remove fatty acid from PLP [1].
• Glyoxalase II and glutathione levels in rat liver mitochondria during cold storage in Euro-Collins and University of Wisconsin solutions [2].
• Diffusion-dependent rates for the hydrolysis reaction catalyzed by glyoxalase II from rat erythrocytes [3].
• Glyoxalase II from rat erythrocytes is a near optimal catalyst for the hydrolysis of S-D-lactoylglutathione in the sense that the magnitude of kcat/Km is limited, in large part, by the rate constant for diffusion-controlled encounter between substrate and active site [3].
• This is in marked contrast to other glyoxalase II competitive inhibitors, which in general are even more effective against glyoxalase I. The S-(o-, m-, and p-nitrocarbobenzoxy)glutathiones have found utility as affinity ligands for the purification of rat liver glyoxalase II and may well have use in the study of the glyoxalase enzymes in vivo [4].

Biological context of Hagh

• The high expression of RSP29 in testis and its stimulatory effects on Sertoli cells suggest that RSP29 could be especially important in the regulation of spermatogenesis [5].
• The entire amino acid sequence of RSP29 showed significant homology with that of hDP1, which was later identified as glyoxalase II [5].
• S-2-hydroxyacylglutathione hydrolase (glyoxalase II): active-site mapping of a nonserine thiolesterase [6].

Anatomical context of Hagh

• The RSP29 mRNA is expressed in many tissues but has an extremely high abundance in testis [5].
• RSP29, a protein secreted by rat round spermatids, stimulates the secretory function of Sertoli cells in the testis [5].
• S-2-Hydroxyacylglutathione hydrolase (glyoxalase II) from rat erythrocytes is a specific thiolesterase [6].
• Glyoxalase I and glyoxalase II activities were decreased in the liver and increased in skeletal muscle of diabetic rats and of Statil-treated diabetic rats, relative to normal controls [7].
• Pure glyoxalase II from rat liver cytosol was chemically polymerized and used as antigen [8].

Associations of Hagh with chemical compounds

• Mitochondrial glutathione and glyoxalase II were severely depleted soon after 7 hr of cold storage in Euro-Collins, whereas the same parameters did not change in liver stored in UW after 24 hr [2].
• While showing marked competitive inhibition of glyoxalase II, the glutathione derivatives were almost inactive as inhibitors of glyoxalase I. For example, with the para isomer, [I]0.5 values for rat liver glyoxalase I and II were 925 and 12 microM, respectively [4].
• Chemical modification studies with phenylmethanesulfonic acid, N-ethylmaleimide, and 5,5'-dithiobis(2-nitrobenzoate) suggest that glyoxalase II does not have a serine or a cysteine residue at the active site [6].
• 13-Hydroperoxylinoleic acid inhibits rat liver glyoxalase II [9].
• Glyoxalase II catalyzes the destruction of S-lactoylglutathione [9].

Other interactions of Hagh

• A study of the activities of glutathione-dependent antioxidant enzymes in the renal cortical homogenates showed that the activities of glutathione peroxidase and glyoxalase II were altered significantly [10].

Analytical, diagnostic and therapeutic context of Hagh

• Mitochondrial glyoxalase II did not show any change by reperfusion [11].
• The aim of our study was to evaluate the cytosolic and mitochondrial glutathione levels, the glyoxalase II activity, and the mitochondrial hydroperoxide contents of livers stored in different preservation solutions for 7 or 24 h and after transplantation [11].
• Antibodies were raised in rabbits and the antiserum was used for comparison of the two purified mitochondrial enzymes with cytosolic glyoxalase II by immunoblotting [8].
• Rat liver glyoxalase II has been purified to homogeneity by a rapid, two-step procedure involving affinity chromatography on S-carbobenzoxyglutathione coupled to Sepharose 4B [12].
• Glyoxalase II (S-(2-hydroxyacyl)glutathione hydrolase, EC 3.1.2.6) was purified to homogeneity and separated into two forms (alpha, pI = 8.0; beta, pI = 7.4) from both liver and brain of wistar rats by column isoelectric focusing [13].

References