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Segregation of two endocannabinoid-hydrolyzing enzymes into pre- and postsynaptic compartments in the rat hippocampus, cerebellum and amygdala.

Abstract

Fatty acid amide hydrolase (FAAH) and monoglyceride lipase (MGL) catalyse the hydrolysis of the endocannabinoids anandamide and 2-arachidonoyl glycerol. We investigated their ultrastructural distribution in brain areas where the localization and effects of cannabinoid receptor activation are known. In the hippocampus, FAAH was present in somata and dendrites of principal cells, but not in interneurons. It was located mostly on the membrane surface of intracellular organelles known to store Ca(2+) (e.g. mitochondria, smooth endoplasmic reticulum), less frequently on the somatic or dendritic plasma membrane. MGL immunoreactivity was found in axon terminals of granule cells, CA3 pyramidal cells and some interneurons. In the cerebellum, Purkinje cells and their dendrites are intensively immunoreactive for FAAH, together with a sparse axon plexus at the border of the Purkinje cell/granule cell layers. Immunostaining for MGL was complementary, the axons in the molecular layer were intensively labelled leaving the Purkinje cell dendrites blank. FAAH distribution in the amygdala was similar to that of the CB(1) cannabinoid receptor: evident signal in neuronal somata and proximal dendrites in the basolateral nucleus, and hardly any labelling in the central nucleus. MGL staining was restricted to axons in the neuropil, with similar relative signal intensities seen for FAAH in different nuclei. Thus, FAAH is primarily a postsynaptic enzyme, whereas MGL is presynaptic. FAAH is associated with membranes of cytoplasmic organelles. The differential compartmentalization of the two enzymes suggests that anandamide and 2-AG signalling may subserve functional roles that are spatially segregated at least at the stage of metabolism.

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  • Authors+Show Affiliations

    ,

    Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, PO Box 67, H-1450, Hungary. gulyas@koki.hu

    , , , , ,

    Source

    The European journal of neuroscience 20:2 2004 Jul pg 441-58

    MeSH

    Amidohydrolases
    Amygdala
    Animals
    Calbindin 2
    Calbindins
    Cerebellum
    Cholecystokinin
    Fluorescent Antibody Technique
    Glutamate Decarboxylase
    Hippocampus
    Isoenzymes
    Male
    Mice
    Mice, Knockout
    Microscopy, Immunoelectron
    Monoacylglycerol Lipases
    Parvalbumins
    Presynaptic Terminals
    Rats
    Rats, Wistar
    S100 Calcium Binding Protein G
    Synapses

    Pub Type(s)

    Comparative Study
    Journal Article
    Research Support, Non-U.S. Gov't
    Research Support, U.S. Gov't, P.H.S.

    Language

    eng

    PubMed ID

    15233753

    Citation

    Gulyas, A I., et al. "Segregation of Two Endocannabinoid-hydrolyzing Enzymes Into Pre- and Postsynaptic Compartments in the Rat Hippocampus, Cerebellum and Amygdala." The European Journal of Neuroscience, vol. 20, no. 2, 2004, pp. 441-58.
    Gulyas AI, Cravatt BF, Bracey MH, et al. Segregation of two endocannabinoid-hydrolyzing enzymes into pre- and postsynaptic compartments in the rat hippocampus, cerebellum and amygdala. Eur J Neurosci. 2004;20(2):441-58.
    Gulyas, A. I., Cravatt, B. F., Bracey, M. H., Dinh, T. P., Piomelli, D., Boscia, F., & Freund, T. F. (2004). Segregation of two endocannabinoid-hydrolyzing enzymes into pre- and postsynaptic compartments in the rat hippocampus, cerebellum and amygdala. The European Journal of Neuroscience, 20(2), pp. 441-58.
    Gulyas AI, et al. Segregation of Two Endocannabinoid-hydrolyzing Enzymes Into Pre- and Postsynaptic Compartments in the Rat Hippocampus, Cerebellum and Amygdala. Eur J Neurosci. 2004;20(2):441-58. PubMed PMID: 15233753.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - Segregation of two endocannabinoid-hydrolyzing enzymes into pre- and postsynaptic compartments in the rat hippocampus, cerebellum and amygdala. AU - Gulyas,A I, AU - Cravatt,B F, AU - Bracey,M H, AU - Dinh,T P, AU - Piomelli,D, AU - Boscia,F, AU - Freund,T F, PY - 2004/7/6/pubmed PY - 2004/10/1/medline PY - 2004/7/6/entrez SP - 441 EP - 58 JF - The European journal of neuroscience JO - Eur. J. Neurosci. VL - 20 IS - 2 N2 - Fatty acid amide hydrolase (FAAH) and monoglyceride lipase (MGL) catalyse the hydrolysis of the endocannabinoids anandamide and 2-arachidonoyl glycerol. We investigated their ultrastructural distribution in brain areas where the localization and effects of cannabinoid receptor activation are known. In the hippocampus, FAAH was present in somata and dendrites of principal cells, but not in interneurons. It was located mostly on the membrane surface of intracellular organelles known to store Ca(2+) (e.g. mitochondria, smooth endoplasmic reticulum), less frequently on the somatic or dendritic plasma membrane. MGL immunoreactivity was found in axon terminals of granule cells, CA3 pyramidal cells and some interneurons. In the cerebellum, Purkinje cells and their dendrites are intensively immunoreactive for FAAH, together with a sparse axon plexus at the border of the Purkinje cell/granule cell layers. Immunostaining for MGL was complementary, the axons in the molecular layer were intensively labelled leaving the Purkinje cell dendrites blank. FAAH distribution in the amygdala was similar to that of the CB(1) cannabinoid receptor: evident signal in neuronal somata and proximal dendrites in the basolateral nucleus, and hardly any labelling in the central nucleus. MGL staining was restricted to axons in the neuropil, with similar relative signal intensities seen for FAAH in different nuclei. Thus, FAAH is primarily a postsynaptic enzyme, whereas MGL is presynaptic. FAAH is associated with membranes of cytoplasmic organelles. The differential compartmentalization of the two enzymes suggests that anandamide and 2-AG signalling may subserve functional roles that are spatially segregated at least at the stage of metabolism. SN - 0953-816X UR - https://www.unboundmedicine.com/medline/citation/15233753/Segregation_of_two_endocannabinoid_hydrolyzing_enzymes_into_pre__and_postsynaptic_compartments_in_the_rat_hippocampus_cerebellum_and_amygdala_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0953-816X&date=2004&volume=20&issue=2&spage=441 DB - PRIME DP - Unbound Medicine ER -