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Gene Review

Mgll  -  monoglyceride lipase

Rattus norvegicus

Synonyms: MAGL, MGL, Mgl2, Monoacylglycerol lipase, Monoglyceride lipase
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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


Associations of Mgll with chemical compounds


Analytical, diagnostic and therapeutic context of Mgll


  1. Activities of enzymes metabolizing phospholipids in rat cerebral ischemia. Hirashima, Y., Moto, A., Endo, S., Takaku, A. Mol. Chem. Neuropathol. (1989) [Pubmed]
  2. Brain monoglyceride lipase participating in endocannabinoid inactivation. Dinh, T.P., Carpenter, D., Leslie, F.M., Freund, T.F., Katona, I., Sensi, S.L., Kathuria, S., Piomelli, D. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. Characterization of the sulfhydryl-sensitive site in the enzyme responsible for hydrolysis of 2-arachidonoyl-glycerol in rat cerebellar membranes. Saario, S.M., Salo, O.M., Nevalainen, T., Poso, A., Laitinen, J.T., Järvinen, T., Niemi, R. Chem. Biol. (2005) [Pubmed]
  4. Fatty acid amide hydrolase inhibitors from virtual screening of the endocannabinoid system. Saario, S.M., Poso, A., Juvonen, R.O., Järvinen, T., Salo-Ahen, O.M. J. Med. Chem. (2006) [Pubmed]
  5. Chronic Schwann cell denervation and the presence of a sensory nerve reduce motor axonal regeneration. Sulaiman, O.A., Midha, R., Munro, C.A., Matsuyama, T., Al-Majed, A., Gordon, T. Exp. Neurol. (2002) [Pubmed]
  6. Are monoglyceride-lipase, triglyceride-lipase and phospholipase A of rat liver microsomes distinct protein entities? Colbeau, A., Ngo-Tri, H., Chabert, J., Vignais, P.M. Biochimie (1977) [Pubmed]
  7. Changes in lipase and phosphatase activities of rat spermatozoa in transit from the caput to the cauda epididymidis. Terner, C., MacLaughlin, J., Smith, B.R. J. Reprod. Fertil. (1975) [Pubmed]
  8. Monoglyceride lipase-like enzymatic activity is responsible for hydrolysis of 2-arachidonoylglycerol in rat cerebellar membranes. Saario, S.M., Savinainen, J.R., Laitinen, J.T., Järvinen, T., Niemi, R. Biochem. Pharmacol. (2004) [Pubmed]
  9. Role of the basolateral nucleus of the amygdala in endocannabinoid-mediated stress-induced analgesia. Connell, K., Bolton, N., Olsen, D., Piomelli, D., Hohmann, A.G. Neurosci. Lett. (2006) [Pubmed]
  10. Ethanediol monoester hydrolysis by monoacylglycerol lipase of rat liver microsomes. Parthasarathy, S., Lin, J.T., Baumann, W.J. Biochim. Biophys. Acta (1979) [Pubmed]
  11. Distribution of digestive enzyme activities along intestine in blue fox, mink, ferret and rat. Oleinik, V.M. Comp. Biochem. Physiol. A Physiol. (1995) [Pubmed]
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