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Gene Review

MGLL  -  monoglyceride lipase

Homo sapiens

Synonyms: HU-K5, HUK5, Lysophospholipase homolog, Lysophospholipase-like, MAGL, ...
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Disease relevance of MGLL

  • Thus, regulation of effector T cells by MGL expressed on APCs may provide a target for regulating chronic inflammatory and autoimmune diseases [1].
  • Immunohistochemical analysis further established that the expression of monoglyceride lipase was restricted to ductal breast cancer and present in 77% of these tumors, while Vav1 was restricted to MCB and present in 60% of tumors [2].

High impact information on MGLL

  • Here we found that immature APCs downregulated effector T cell function by a mechanism involving the C-type lectin MGL expressed by APCs [1].
  • Regulation of effector T cells by antigen-presenting cells via interaction of the C-type lectin MGL with CD45 [1].
  • The endocannabinoid system consists of two cannabinoid (CB) receptors, seven ligands, and ligand-catabolizing enzymes such as fatty acid amid hydrolase (FAAH) and monoglyceride lipase (MGL) [3].
  • Thus a meta-analysis of ligand extraction studies was performed (chemotaxonomy), and compared to a molecular search for homologs of CB receptors, vanilloid receptors (VR1), FAAH, and MGL in the genomes of sequenced organisms (phylogenomics) [3].
  • Two of these, the macrophage mannose receptor and the macrophage lectin specific for galactose/N-acetylgalactosamine (MGL), were found only in immature DCs, as confirmed by reverse transcriptase-PCR and flow cytometric analysis [4].

Biological context of MGLL

  • In addition, MGL presumably complements lipoprotein lipase in completing the hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides [5].
  • The mouse MGL gene was mapped to chromosome 6 in a region with known homology to human chromosome 3q21 [5].
  • The amino acid sequence derived from human MGL cDNA clones showed 84% identity with mouse MGL [5].
  • Cosmid clones containing the mouse MGL gene were isolated from a genomic library using the coding region of the mouse MGL cDNA as probe [5].
  • In addition, the hMGL gene locus on human chromosome 17p13 contains one gene [4].

Anatomical context of MGLL

  • We report here that RNA interference-mediated silencing of MGL expression greatly enhances 2-AG accumulation in HeLa cells [6].
  • Furthermore, immunodepletion experiments show that MGL accounts for at least 50% of the total 2-AG-hydrolyzing activity in soluble fractions of rat brain, suggesting that this enzyme also contributes to 2-AG deactivation in the central nervous system [6].
  • Furthermore, hMGL, like DC-SIGN and L-SIGN, is present on cells known to be major targets of filoviruses (i.e., macrophages and dendritic cells), suggesting a role for these C-type lectins in viral replication in vivo [7].
  • All hit molecules were tested for their potential MGL inhibitory activity, but no compounds were found capable of inhibiting MGL-like enzymatic activity in rat cerebellar membranes [8].
  • Immunohistochemical studies in the hippocampus showed that MGL distribution has striking laminar specificity, suggesting a presynaptic localization of the enzyme [9].

Associations of MGLL with chemical compounds

  • Immature DCs could incorporate alpha-GalNAc-modified soluble acrylamide polymers, and this was significantly inhibited by pretreatment of the cells with an anti-hMGL monoclonal antibody that blocks the lectin-carbohydrate interaction [4].
  • The results further suggest that PPARgamma agonism stimulates lipolysis by increasing the lipolytic potential, including the expression levels of the genes encoding adipose triglyceride lipase and monoglyceride lipase [10].
  • We have shown previously that overexpression of monoacylglycerol lipase (MGL), a cytosolic serine hydrolase that cleaves 1- and 2-monoacylglycerols to fatty acid and glycerol, reduces stimulus-dependent 2-AG accumulation in primary cultures of rat brain neurons [6].
  • After stimulation with the calcium ionophore ionomycin, 2-AG levels in MGL-silenced cells were comparable with those found in cells in which 2-AG degradation had been blocked using methyl arachidonyl fluorophosphonate, a nonselective inhibitor of 2-AG hydrolysis [6].
  • The CSF action was sensitive to monoglyceride lipase and diminished by homologous desensitization with lysophosphatidic acid (LPA) and by pretreatment with an LPA receptor antagonist Ki16425 [11].

Analytical, diagnostic and therapeutic context of MGLL


  1. Regulation of effector T cells by antigen-presenting cells via interaction of the C-type lectin MGL with CD45. van Vliet, S.J., Gringhuis, S.I., Geijtenbeek, T.B., van Kooyk, Y. Nat. Immunol. (2006) [Pubmed]
  2. Identification of genes with altered expression in medullary breast cancer vs. ductal breast cancer and normal breast epithelia. Gjerstorff, M.F., Benoit, V.M., Laenkholm, A.V., Nielsen, O., Johansen, L.E., Ditzel, H.J. Int. J. Oncol. (2006) [Pubmed]
  3. Phylogenomic and chemotaxonomic analysis of the endocannabinoid system. McPartland, J.M. Brain Res. Brain Res. Rev. (2004) [Pubmed]
  4. The macrophage C-type lectin specific for galactose/N-acetylgalactosamine is an endocytic receptor expressed on monocyte-derived immature dendritic cells. Higashi, N., Fujioka, K., Denda-Nagai, K., Hashimoto, S., Nagai, S., Sato, T., Fujita, Y., Morikawa, A., Tsuiji, M., Miyata-Takeuchi, M., Sano, Y., Suzuki, N., Yamamoto, K., Matsushima, K., Irimura, T. J. Biol. Chem. (2002) [Pubmed]
  5. Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene. Karlsson, M., Reue, K., Xia, Y.R., Lusis, A.J., Langin, D., Tornqvist, H., Holm, C. Gene (2001) [Pubmed]
  6. RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2-arachidonoylglycerol. Dinh, T.P., Kathuria, S., Piomelli, D. Mol. Pharmacol. (2004) [Pubmed]
  7. Human macrophage C-type lectin specific for galactose and N-acetylgalactosamine promotes filovirus entry. Takada, A., Fujioka, K., Tsuiji, M., Morikawa, A., Higashi, N., Ebihara, H., Kobasa, D., Feldmann, H., Irimura, T., Kawaoka, Y. J. Virol. (2004) [Pubmed]
  8. 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]
  9. A role for monoglyceride lipase in 2-arachidonoylglycerol inactivation. Dinh, T.P., Freund, T.F., Piomelli, D. Chem. Phys. Lipids (2002) [Pubmed]
  10. PPARgamma agonism increases rat adipose tissue lipolysis, expression of glyceride lipases, and the response of lipolysis to hormonal control. Festuccia, W.T., Laplante, M., Berthiaume, M., Gélinas, Y., Deshaies, Y. Diabetologia (2006) [Pubmed]
  11. Identification of autotaxin as a neurite retraction-inducing factor of PC12 cells in cerebrospinal fluid and its possible sources. Sato, K., Malchinkhuu, E., Muraki, T., Ishikawa, K., Hayashi, K., Tosaka, M., Mochiduki, A., Inoue, K., Tomura, H., Mogi, C., Nochi, H., Tamoto, K., Okajima, F. J. Neurochem. (2005) [Pubmed]
  12. Monoacylglycerol metabolism in human intestinal Caco-2 cells: evidence for metabolic compartmentation and hydrolysis. Ho, S.Y., Delgado, L., Storch, J. J. Biol. Chem. (2002) [Pubmed]
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