Disease relevance of Mgll

• Activities of phospholipase A, phospholipase C, and di- and monoglyceride lipase, assayed with optimal concentrations of Ca2+ and lysophospholipase, did not significantly change by 60 min of ischemia, whereas acylation enzymes of lysophospholipid decreased in activity to an extent of 70% of control at 15 min after the ischemic treatment [1].

High impact information on Mgll

• The results suggest that hydrolysis by means of MGL is a primary mechanism for 2-AG inactivation in intact neurons [2].
• Immunohistochemical studies in the hippocampus showed that MGL distribution has striking laminar specificity, suggesting a presynaptic localization of the enzyme [2].
• Here we tested the hypothesis that monoglyceride lipase (MGL), a serine hydrolase that converts monoglycerides to fatty acid and glycerol, participates in 2-AG inactivation [2].
• We cloned MGL by homology from a rat brain cDNA library [2].
• Adenovirus-mediated transfer of MGL cDNA into rat cortical neurons increased MGL expression and attenuated N-methyl-D-aspartate/carbachol-induced 2-AG accumulation in these cells [2].

Biological context of Mgll

• A comparison model of MGL was constructed to get a view on the cysteine residues located near the binding site [3].
• Additionally, compound 7 inhibited MGL-like enzymatic activity with an IC50 value of 31 microM [4].

Anatomical context of Mgll

• Northern blot and in situ hybridization analyses revealed that MGL mRNA is heterogeneously expressed in the rat brain, with highest levels in regions where CB(1) cannabinoid receptors are also present (hippocampus, cortex, anterior thalamus, and cerebellum) [2].
• We have previously reported that the endocannabinoid, 2-arachidonoyl-glycerol (2-AG), is hydrolyzed in rat cerebellar membranes by monoglyceride lipase (MGL)-like enzymatic activity [3].
• The number of regenerated nerve fibers was 1522 +/- 81 in the MGL group, 888 +/- 18 in the MGM group, and 516 +/- 44 in the MGS group, although the high number of nerve fibers in the MGL group was due partly to the elaboration of multiple sprouts [5].
• Are monoglyceride-lipase, triglyceride-lipase and phospholipase A of rat liver microsomes distinct protein entities [6]?
• Against the background of the activities of some glycolytic enzymes which remained constant the activity of alkaline phosphatase decreased in spermatozoa migrating through the epididymis, whereas the activity of monoglyceride lipase increased [7].

Associations of Mgll with chemical compounds

• Monoglyceride lipase-like enzymatic activity is responsible for hydrolysis of 2-arachidonoylglycerol in rat cerebellar membranes [8].
• To examine the contribution of endocannabinoids in the BLA to SIA, we used selective pharmacological inhibitors of the anandamide-degrading enzyme fatty-acid amide hydrolase (FAAH) and the 2-arachidonoylglycerol-degrading enzyme monoacylglycerol lipase (MGL) [9].
• Because diol monoester is also utilized by the cholinephosphotransferase system of liver to form highly lytic acyl diol phosphocholines, efficient diol monoester hydrolysis by monoglyceride lipase may be a significant step in regulating acyl diol phosphocholine levels in biological systems [10].
• The activities of amylase, total proteases, monoglyceride lipase, glycyl-leucine dipeptidase and sucrase were investigated in mucosa from five consecutive parts of small intestine in blue fox, mink, ferret and rat [11].

Analytical, diagnostic and therapeutic context of Mgll

• The FAAH inhibitor URB597 and MGL inhibitor URB602, at doses that enhanced SIA following microinjection in the midbrain periaqueductal gray, did not alter SIA relative to control conditions [9].

References