Erratum
for
RODRÍGUEZ de FONSECA et al., Alcohol Alcohol. 40 (1) 2-14.
Alcohol and Alcoholism 2005 40(2):159-160; doi:10.1093/alcalc/agh140
Alcohol & Alcoholism Vol. 40, No. 2 © Medical Council on Alcohol 2005; all rights reserved
ERRATUM
de Fonseca, F. R., del Arco, I., Bermudez-Silva, F. J., Bilbao,
A., Cippitelli, A. and Navarro, M. (2005) The Endocannabinoid
System: Physiology and Pharmacology.
Alcohol and Alcoholism 40, 2–14.
The publisher wishes to apologise to the authors for printing Fig. 2 and Fig. 3 in black and white. The colour figures are reproduced below.
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Fig. 2. Overview of the biochemical pathways for synthesis, degradation and cellular actions of the endogenous cannabinoid anandamide. Anandamide is released from a membrane lipid precursor (N-arachidonoyl-phosphatidylethanolamine, NAPE) by the action of a specific phospholipase D (PLD) activated by depolarization or G-protein-coupled receptor (GPCR) stimulation. NAPE biosynthesis is catalysed by a membrane enzyme, N-acyltransferase (NAT) activated by calcium (Ca2+) and cAMP. Anandamide acts as a retrograde messenger at presynaptic cannabinoid receptors (CB1), where it regulates neurotransmitter release (NT) through its second transduction systems [mainly Ca2+ incorporated through voltage-gated calcium channels (VGCC) or glutamate NMDA (N-methyl-D-aspartate) receptors]. Anandamide also acts as a neuromodulator of major transmitter systems, including dopamine, at postsynaptic cells, where it regulates excitability and synaptic plasticity through its modulation of potassium (K+) channels, and the regulation of a broad spectrum of protein kinases (PK) including protein kinase A and mitogen-activated protein kinases (MAPK). Anandamide action is terminated through a two-step process, which includes, first, its cellular uptake through a specific anandamide transporter (AT) and second, degradation by enzymatic cleavage to arachidonic acid (AA) and ethanolamide by the membrane-bound enzyme fatty acid amidohydrolase (FAAH).
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Fig. 3. Imaging cannabinoid CB1 receptor in circuits of the rat brain reward system. Cannabinoid receptors are mainly located at presynaptic axon terminals. In the basal ganglia, CB1 receptor mRNA expression (panels A and B) is located mainly in GABAergic projecting neurons of the caudate-putamen (CPu), but not in the target nuclei, the globus pallidus or the substantia nigra (GP and SN). However, the protein is mainly detected by immunohistochemistry (panels C and D) in the axon terminals innervating both outflow nuclei of the basal ganglia. Panel E shows the dense presence of CB1 receptors in the substantia nigra and ventral tegmental area (VTA) as mapped by CB1 receptor agonist-stimulated GTP- -S incorporation. In these areas, CB1 receptors are not located in dopaminergic neurons (Panel F): confocal imaging using specific antibodies against CB1 receptors (green) and tyrosine hydroxilase (red) shows the compartmentalization of CB1 receptors in GABAergic afferents to the substantia nigra pars reticulata (SNr), whereas dopaminergic cells are restricted to the pars compacta (SNc). The segregation of CB1 receptors and catecholaminergic transmission is also observed in the hippocampus-dentate gyrus (Hpc-DG, panel G).
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