Where are the receptors, and what do they do? Tap a body system below.
Where in your body are the cannabinoid receptors, what do they do there, and what is actually known about CBD? Built with real anatomy, real data and real molecular structures. Lesson mode and classroom mode for teaching; three reading levels for Everyone, Students and Experts.
28 regions319 sourcesData: Human Protein Atlas, BodyParts3D, Z-Anatomy, RCSB PDBLast updated:
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Where in your body are the cannabinoid receptors?
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Level
Reproductive organs
Regions
Brain
Hormone glands
Nerves and senses
Chest
Digestion and metabolism
Kidneys and urinary tract
Immune system and blood formation
Blood vessels and skin
Muscles and movement
Reproductive organs
How to read it Choose a region, or tap a glowing point on the map.
Solid light is the CB1 receptor, a ring is CB2. Each region has its own color; the color only tells regions apart.
The strength of the light is the receptor gene level measured in human tissue (Human Protein Atlas). That is why the liver’s point is dim: a healthy liver has few receptors.
With the layer selector above you can also see other receptors, the enzymes that make and break down endocannabinoids, and the liver enzymes that break down CBD and THC.
Every piece of information shows its source and the type of evidence (human, animal, cell). You can change the reading level above.
Drag to rotate. Use the + and − buttons to zoom; on a computer, Ctrl or ⌘ with the scroll wheel, on a phone, two fingers.
What is the endocannabinoid system?
It is a widespread regulatory system in the nervous system: it plays a role in how the nervous system develops, in strengthening and weakening the connections between nerve cells, and in the response to injury. It has three parts: receptors, the body's own cannabinoids, and the enzymes that make and break them down. The most abundant receptor is CB1. Cannabinoids taken in from outside, such as THC, act through these receptors. Lu and Mackie 2016Review
In the brain, CB1 is especially dense in the cerebral cortex, hippocampus, amygdala, basal ganglia and cerebellum; it sits mostly at the endings of nerve cells and tunes signal transmission. Mackie 2005ReviewHerkenham 1990Human tissueAnimal CB2, on the other hand, is found mostly in immune tissues. Galiègue 1995Human tissueMunro 1993AnimalCell / lab
The 28 regions on the map
The brightness of the points is the receptor gene RNA level measured by the Human Protein Atlas in human tissues (nTPM; CNR1 = CB1, CNR2 = CB2). RNA level does not fully show where the protein is or how much of it there is; in the brain, CB1 sits mostly on axons and nerve endings, far from the cell body where the RNA is made. Mackie 2005Review
Cerebral cortex: RNA level of the receptor gene in human tissue. The tissue where CB1 is measured highest. Human Protein AtlasHuman tissue
In the human brain, the CB1 receptor is found in every region of the cerebral cortex, but its density varies from place to place. It is densest in the "association" areas of the frontal and limbic lobes, where higher-level thinking takes place, and sparsest in the primary sensory and motor areas. It is also relatively high in regions of the left hemisphere linked to language.
Hippocampal formation: RNA level of the receptor gene in human tissue. Human Protein AtlasHuman tissue
In the hippocampus, the CB1 receptor clusters especially on the terminals of a group of inhibitory (GABA-releasing) nerve cells. At these terminals, endocannabinoids briefly reduce GABA release; the signal travels backward from the receiving cell.
Amygdala: RNA level of the receptor gene in human tissue. Human Protein AtlasHuman tissue
Measurements in the human brain found cannabinoid receptors to be plentiful in the amygdala. One part of the amygdala (the basolateral amygdala) plays an important role in noticing threats and in letting a learned fear fade over time. In rats and mice, the receptor (CB1) here clusters on the terminals of a group of nerve cells that act as a brake (they release GABA), and it eases this brake.
Hypothalamus: RNA level of the receptor gene in human tissue. Human Protein AtlasHuman tissue
The hypothalamus senses the body's nutritional state and regulates appetite and energy balance; it does this mostly through signals from leptin, a hormone that reduces appetite. In human brains examined after death, nerve cells in the hypothalamus carried moderate amounts of the building instructions (mRNA) for CB1. In mice, CB1 was found in hypothalamic cells that make substances regulating appetite.
Basal ganglia: RNA level of the receptor gene in human tissue. Human Protein AtlasHuman tissue
In brain slices, cannabinoid receptor binding was densest in the output nuclei of the basal ganglia (the globus pallidus and substantia nigra), and also in the hippocampus and cerebellum. This distribution was similar across the mammals studied, including humans, and suggests that cannabinoids play a role in movement.
Cerebellum: RNA level of the receptor gene in human tissue. Human Protein AtlasHuman tissue
When Purkinje cells in the cerebellum are stimulated, they release endocannabinoids; this reduces the excitatory signal reaching them for tens of seconds. In this way, the cells can adjust their own inputs.
Pituitary gland: RNA level of the receptor gene in human tissue. CB1 RNA is close to that of the cerebral cortex (18.6) and about twice that of the hypothalamus (9.0); CB2 was not measured. Human Protein AtlasHuman tissue
CB1 receptor RNA is measured at high levels in the pituitary gland, close to the level in the cerebral cortex. In human pituitary tissue, CB1 was found mostly in hormone cells called corticotrophs and in folliculostellate (star-shaped) cells; it was also present in some of the cells that release prolactin and growth hormone. Researchers think this may be related to control of the stress response. Endocannabinoids (anandamide and 2-AG) have also been measured in the human pituitary.
Adrenal gland: RNA level of the receptor gene in human tissue. CB1 at moderate levels; CB2 was not measured. Human Protein AtlasHuman tissue
The adrenal gland makes hormones that are released during stress: its outer layer (the cortex) makes steroid hormones, and its inner part (the medulla) makes adrenaline. CB1 was found in the human adrenal cortex, but CB2 was not. In the lab, anandamide reduced the release of steroid hormones from human adrenal cortex cells; a substance that blocks CB1 reversed this effect. In rabbits, cannabinoids reduced adrenaline release; but no CB1 was found in the gland itself, and researchers think the effect comes from the nerve endings that stimulate the gland.
Thyroid gland: RNA level of the receptor gene in human tissue. Human Protein AtlasHuman tissue
CB1 receptor RNA is measured at moderate levels in the human thyroid. In the rat thyroid, CB1 was seen in both follicular and parafollicular cells. A synthetic cannabinoid given to rats lowered blood levels of thyroid hormones (T3 and T4) by about 30% within 4 hours; a substance that blocks CB1 prevented this.
Spinal cord: RNA level of the receptor gene in human tissue. In the tissue consensus data, this is the average for the whole spinal cord tissue; in animal studies, the receptor is concentrated at the surface of the dorsal horn. Human Protein AtlasHuman tissue
In the rat spinal cord, CB1 was seen mostly in the surface layers of the dorsal horn, where pain signals are first processed; most of it was in the interneurons there. Some of the nerve cells that carry sensory signals to the spinal cord also make CB1; these are mostly medium-sized and large cells.
Retina: RNA level of the receptor gene in human tissue. For the eye, HPA measures only the retina; the ciliary body at the front of the eye is not in this data. Human Protein AtlasHuman tissue
Pressure inside the eye depends on the balance between how much fluid is made to fill the front part of the eye and how much drains out. In human eyes examined after death, the CB1 receptor was prominent in the ciliary body, which makes this fluid, and in the trabecular meshwork, where the fluid drains out; the body's own cannabinoids were also measured in the same tissues.
Lung: RNA level of the receptor gene in human tissue. Across lung tissue as a whole, CB1 RNA is low; CB2 is very low. Human Protein AtlasHuman tissue
Across lung tissue as a whole, CB1 receptor RNA is measured at low levels, but the receptor works at specific points in the airways. In the lab, in bronchial segments taken from 88 people, some cannabinoids reduced nerve-triggered bronchial contraction through CB1; the receptor was not on the muscle itself but on the ending of the nerve that reaches it. In guinea pigs and rats, the body's own cannabinoid anandamide was made in lung tissue and tuned the response of the bronchi in two directions through CB1 on the endings of airway nerves.
Breast: RNA level of the receptor gene in human tissue. CB1 RNA is high; CB2 was not measured. Human Protein AtlasHuman tissue
CB1 receptor RNA is measured at high levels in breast tissue; CB2 RNA is too low to measure. According to a review, CB1 and CB2 are found in the mammary gland. The mammary gland develops largely in adulthood; in one laboratory study, the endocannabinoid-degrading enzyme FAAH turned out to be important in this development: by adjusting anandamide levels and the CB1 activation that depends on them, it guided the differentiation of gland cells.
Colon · Small intestine: RNA level of the receptor gene in human tissue. CB1 is 10.0 in the colon and 8.1 in the small intestine; CB2 is 3.1 in the small intestine and 0.2 in the colon. Human Protein AtlasHuman tissue
The endocannabinoid system is found throughout the digestive tract: in the gut's nerve network, in the cells lining the gut, and in immune cells. It plays a role in regulating gut movement, secretion, appetite, nausea, gut sensitivity and inflammation.
Stomach: RNA level of the receptor gene in human tissue. CB1 is moderate across the whole organ; in the human stomach lining it was shown in the acid-secreting cells. Human Protein AtlasHuman tissue
The acid-secreting cells lining the stomach carry the CB1 receptor: in human stomach biopsies with normal findings, CB1 in the stomach lining was seen only in these cells. In human tissue, RNA for CB1 and CB2 was found in the stomach, and RNA for CB1 in the vagus nerve, which links the stomach to the brain. In rats, CB1 sat on the nerves in the stomach wall; cannabinoids lowered stomach acid through these nerves and protected the stomach from stress-induced sores.
LiverFat metabolism; a receptor that rises in disease
CB1very low
CB2very low
Liver: RNA level of the receptor gene in human tissue. In healthy liver tissue, RNA for both receptors is very low. Human Protein AtlasHuman tissue
The healthy liver has few receptors, but they come to the fore in disease: CB1 rose markedly in samples of cirrhosis and in the liver cells that make scar tissue. In mice, CB1 in the liver increased fat production and contributed to weight gain on a high-fat diet.
Adipose tissue: RNA level of the receptor gene in human tissue. CB1 RNA is very close to the highest value, in the cerebral cortex (18.6); CB2 is very low. Human Protein AtlasHuman tissue
In adipose (fat) tissue, RNA for the CB1 receptor is measured at a level very close to that of the cerebral cortex. Human fat cells carry both CB1 and CB2 and make their own endocannabinoids. Stimulating CB1 increased sugar uptake in human fat cells and fat production in mouse fat cells.
Pancreas: RNA level of the receptor gene in human tissue. CB1 RNA is low across the whole organ; CB2 was not measured. Human Protein AtlasHuman tissue
Across the pancreas as a whole, RNA for the CB1 receptor is measured as low. But in the islets of Langerhans, small clusters of hormone-secreting cells, the parts of the endocannabinoid system are found together: human islets taken from organ donors carried CB1 and CB2 and also contained the enzymes that make and break down 2-AG. The amount of 2-AG in the islets changed with the sugar in their surroundings.
KidneyBlood flow, salt and water balance, and excretion
CB1very low
CB2very low
Kidney: RNA level of the receptor gene in human tissue. RNA for both receptors is very low across the whole organ; CB1 is concentrated in certain tubule cells (human tissue study). Human Protein AtlasHuman tissue
Across the kidney as a whole, RNA for both receptors is measured as very low, but CB1 is concentrated in certain cells. In the human kidney, CB1 was found clearly in the cells of the first coiled tubule (proximal tubule), where 70–80% of the filtered fluid is reabsorbed, and of the second coiled tubule (distal tubule), as well as in the intercalated cells of the collecting ducts; the distribution was similar in adult and fetal kidney. The same study did not find CB2; another study, however, reported that CB2 was reduced in kidney samples from people with advanced diabetic kidney disease. So findings on CB2 in the kidney do not agree. According to a review, CB1 is the leading endocannabinoid receptor in the kidney.
Urinary bladder: RNA level of the receptor gene in human tissue. CB1 is moderate across the whole bladder; CB2 RNA is very low. Human Protein AtlasHuman tissue
In the human bladder, both receptors have been shown both in the inner lining (urothelium) and in the muscle layer (detrusor). In one study, RNA for CB1 was higher than for CB2 in both layers; in another study that examined rat, monkey and human bladders together, however, CB2 was higher in the inner lining (mucosa) than in the muscle layer and was also found in the sensory nerves just beneath the lining. The lining of the human bladder also contains the enzyme that breaks down anandamide (FAAH), in the same place as CB2. In the laboratory, stimulating either receptor reduced electrically induced contraction in muscle strips taken from the human bladder.
Spleen: RNA level of the receptor gene in human tissue. The tissue where CB2 is measured highest; tonsil (7.0) and lymph node (6.9) follow. Human Protein AtlasHuman tissue
The second cannabinoid receptor (CB2) was identified from immune cells of the spleen. In human tissues, CB2 is 10–100 times more abundant than CB1 in immune organs; among blood cells, it is found most in B lymphocytes.
Tonsil · lymph node: RNA level of the receptor gene in human tissue. CB2 is 7.0 in the tonsil and 6.9 in the lymph node: the two highest tissues after the spleen (8.4). CB1 is 3.5 in the tonsil and 2.9 in the lymph node. Human Protein AtlasHuman tissue
The CB2 receptor is abundant in the tonsils: the CB2 RNA measured there matched the amount of CB1 in the brain. In lymphoid organs, CB2 is found most in B lymphocytes, a type of immune cell.
Bone marrow: RNA level of the receptor gene in human tissue. HPA does not measure bone tissue; the value is for bone marrow. Human Protein AtlasHuman tissue
Bone is constantly renewed: bone-building cells lay down new bone, and bone-resorbing cells remove the old. Both of these cell types carry the CB2 receptor and make their own endocannabinoids. In mice lacking CB2, age-related bone loss sped up markedly; in humans, too, certain variations in the CB2 gene were found to be associated with postmenopausal osteoporosis.
Blood vessel: RNA level of the receptor gene in human tissue. CB1 RNA is higher than in the basal ganglia (15.1) and hippocampus (13.2); CB2 is very low. Human Protein AtlasHuman tissue
RNA for the CB1 receptor is measured as high in blood vessel tissue; the value is even higher than in the basal ganglia and hippocampus. The cells lining the inside of blood vessels (endothelium) carry CB1. In pieces of artery taken from patients having bowel surgery, the body's own cannabinoid anandamide moderately relaxed the vessel through CB1 and the endothelium.
Skin: RNA level of the receptor gene in human tissue. The value is the average of the whole skin sample; in human skin sections, both receptors stained in many cell types. Human Protein AtlasHuman tissue
In human skin, CB1 and CB2 receptors have been seen in many cells: in the cells of the outer skin, in hair follicles, in oil and sweat glands, in some immune cells and in the fine sensory nerves that branch through the skin.
Skeletal muscle: RNA level of the receptor gene in human tissue. RNA for both receptors is at a low level. Human Protein AtlasHuman tissue
Across muscle as a whole, RNA for CB1 and CB2 is measured as low. Skeletal muscle carries parts of the endocannabinoid system: in human muscle samples, RNA was found for CB1, CB2, TRPV1 and FAAH, the enzyme that breaks down anandamide. In biopsies taken from the muscle on the front and outer side of the thigh (vastus lateralis), there was more CB1 in older men than in young men; CB1 was concentrated more in type I fibers, which have a high capacity to make energy using oxygen, and CB2 in type II fibers. By contrast, in one cell study CB1 was found to be high in mouse brain but could not be detected in mouse muscle or muscle cells. In samples taken from the tissue fluid of the human shoulder muscle, anandamide and related fat molecules could be measured; in women with chronic neck and shoulder pain, two of them were higher.
Endometrium: RNA level of the receptor gene in human tissue. CB1 is moderate in the uterine lining, and CB2 RNA is very low; in the fallopian tube, CB1 is 5.4 nTPM. The muscle layer is not a separate tissue in HPA. Human Protein AtlasHuman tissue
In the lining of the uterus, RNA for CB1 is measured at a moderate level and for CB2 at a very low level; CB1 is also moderate in the fallopian tube. The uterus has two main layers: the lining (endometrium), which matures again in every menstrual cycle, and the muscle layer that surrounds it (myometrium). In human uterine samples taken at different phases of the cycle, CB1 and CB2 receptors were widely spread through the tissue. In the lining they were found mostly in gland cells, and in the muscle layer in muscle cells; the most marked staining was in the muscle cells of blood vessel walls. The muscle layer has been shown to be able to make endocannabinoids, respond to them and break them down. A more recent study, however, measured CB1 at a very low level in lining cells; findings on the amount of CB1 in the lining do not agree. According to a review, the most studied endocannabinoid in the uterus is anandamide; studies on CB2 and on the other main endocannabinoid, 2-AG, are few.
Prostate: RNA level of the receptor gene in human tissue. CB1 RNA is low across the whole prostate, and CB2 RNA is very low; in the seminal vesicle, CB1 is 1.4 nTPM. Human Protein AtlasHuman tissue
Across the prostate as a whole, RNA for CB1 is measured at a low level and for CB2 at a very low level. The prostate is a walnut-sized gland that adds fluid to semen. In human prostate tissue, both the RNA and the protein of the CB1 receptor were found; the amount of protein was comparable to the receptor in the cerebellum, and the receptor was seen mainly in the secreting inner lining of the gland, the epithelium. Another study found CB1 in both epithelial cells and smooth muscle cells, while TRPV1, another target of cannabinoids, was only in mucosal cells. A third study showed CB1 and CB2 in the nerve fibers entering the gland: they were present in fibers carrying nitric oxide, acetylcholine or CGRP, and absent from fibers carrying adrenaline.
Endocannabinoids often work opposite to the usual signal, from the receiving cell back to the sending terminal, and briefly brake a connection that is overactive.
The signal arrives. An electrical signal reaches the sending (presynaptic) nerve ending. Calcium enters the ending, and the messenger substance in the vesicles, such as glutamate or GABA, is released into the gap between the two cells. Kreitzer and Regehr 2001AnimalCastillo 2012ReviewTwitchell 1997AnimalCell / labStudent and expert level
An action potential reaches the presynaptic terminal; voltage-gated calcium channels open, and calcium entry triggers release of the vesicle contents (glutamate or GABA) into the synaptic cleft. The channels regulated by cannabinoids in hippocampal neurons are N-type and P/Q-type; these are mainly located presynaptically and are required for stimulus-evoked release.
Method: Twitchell 1997: whole-cell voltage clamp in cultured rat hippocampal neurons, Ba2+ current; channel subtypes were distinguished by sensitivity to ω-conotoxin GVIA (N) and MVIIC (P/Q).
The messenger substance excites the postsynaptic cell, and intracellular calcium rises. Depolarized hippocampal neurons rapidly release anandamide and 2-AG in a calcium-dependent manner; if postsynaptic calcium is buffered with BAPTA, the suppression disappears. At some synapses, the calcium rise and activation of group I metabotropic glutamate receptors work together.
Method: Hashimotodani 2013: mouse hippocampal, striatal and cerebellar slices; DSI is the "purely calcium-dependent" form; the trigger can be a Ca2+ rise, activation of a Gq/11-coupled receptor, or a combination of the two.
Made on demand. The receiving cell makes endocannabinoids from fat molecules in its membrane: at most synapses 2-AG (with the enzyme DGLα), at some anandamide. These substances are not stored in advance; they are made when needed. Tanimura 2010AnimalHashimotodani 2013AnimalLu and Mackie 2016ReviewStudent and expert level
In mice lacking diacylglycerol lipase α (DGLα), endocannabinoid-mediated retrograde suppression is completely absent in the cerebellum, hippocampus and striatum; it is preserved in mice lacking DGLβ. Acute application of a DGL inhibitor blocks retrograde signaling; this indicates that 2-AG is synthesized "on demand" rather than drawn from a pre-stored pool. 2-AG and anandamide are made and broken down by different enzyme pathways.
Method: Tanimura 2010: DGLα and DGLβ knockout mice, patch-clamp and 2-AG measurement; in DGLα deficiency, basal 2-AG was markedly low, with no stimulus-induced rise. Hashimotodani 2013: acute pharmacological blockade (OMDM-188).
Traveling backward. The endocannabinoid crosses the gap in the opposite direction and binds to the CB1 receptor on the sending terminal. The signal flows against the usual direction. Wilson and Nicoll 2001AnimalKano 2009ReviewCastillo 2012ReviewStudent and expert level
It is now widely accepted that endocannabinoids are released from the postsynaptic neuron, activate presynaptic CB1 and cause a transient and long-lasting reduction in transmitter release; retrograde signaling is the main route for short- and long-term plasticity at excitatory and inhibitory synapses.
Method: Wilson and Nicoll 2001: the original experiment showing retrograde signaling (rat hippocampal slices). Castillo 2012: non-retrograde signaling routes also exist; this diagram shows only the retrograde route.
The brake. Activated CB1 reduces calcium entry into the terminal through the Gi protein inside the cell; release of the messenger substance drops for tens of seconds. Kreitzer and Regehr 2001AnimalTwitchell 1997AnimalCell / labHua 2020Molecular structure (lab)Student and expert level
Activated CB1 inhibits presynaptic N- and P/Q-type calcium channels through the pertussis toxin–sensitive Gi/o protein; calcium entry and transmitter release decrease for tens of seconds. Cryo-electron microscopy structures show CB1 and CB2 in complex with the Gi protein.
Method: Twitchell 1997: WIN 55,212-2 inhibited the Ba2+ current reversibly and in a concentration-dependent manner (K1/2 = 21 nM, pertussis toxin–sensitive); the CB1 antagonist SR141716 reduced this, and the inactive enantiomer WIN 55,212-3 had no effect.
Breakdown. 2-AG is broken down in the sending terminal by MAGL, and anandamide in the receiving cell by the enzyme FAAH. The two enzymes sit in different cells; the signal ends with breakdown. Dinh 2002AnimalGulyas 2004AnimalCravatt 1996AnimalStudent and expert level
2-AG is broken down by monoacylglycerol lipase (MAGL), and anandamide by fatty acid amide hydrolase (FAAH). In the rat hippocampus, cerebellum and amygdala, FAAH is mainly postsynaptic, whereas MAGL is presynaptic (in terminals of granule cells, CA3 pyramidal cells and some interneurons). MAGL mRNA is highest in regions where CB1 is also present, and MAGL is the main route by which 2-AG is inactivated in intact neurons.
Method: Gulyas 2004: immunoelectron microscopy, rats; FAAH on intracellular organelle membranes. Dinh 2002: cloning of MAGL (303 amino acids); in rat cortical neurons transfected with MAGL, evoked 2-AG accumulation decreased and anandamide was unaffected. Cravatt 1996: the first molecular characterization of FAAH, from rat liver.
The CB1 receptor and the Gi protein: the real structure
Structure determined by cryo-electron microscopy at 3.0 Å resolution: the CB1 receptor is bound to the Gi protein inside the cell, with a synthetic cannabinoid (AM841) in its pocket. The antibody fragment added to stabilize the structure (scFv16) is not shown. Hua 2020Molecular structure (lab)PDB 6KPGMolecular structure (lab)
CBD is not in this structure. A study combining a computer model with mutation experiments suggested that CBD may bind to a site on CB1's inner (intracellular) face, between the second, sixth and seventh helices and the eighth helix (residues 153, 156, 337, 341, 401, 403). This proposal has not yet been confirmed by a structure. Pandey 2025Computer modelCell / lab
Expert level: method notes
Method note
Hua 2020: the Gi complexes of CB1 and CB2 bound to synthetic cannabinoids were solved by cryo-electron microscopy, and agonist-bound CB2 by X-ray crystallography; the results showed a diversified activation mechanism and an unexpected interaction of cholesterol with CB1 (the authors propose a role as an endogenous allosteric modulator). Resolution and ligand name (8D0 = AM841) from the PDB entry. Hua 2020Molecular structure (lab)PDB 6KPGMolecular structure (lab)
Pandey 2025: molecular docking, molecular dynamics and metadynamics simulations, binding free energy and site-directed mutagenesis. The proposed site lies between TMH 2, 6 and 7 and helix 8: Y153(2.40), I156(2.43), M337(6.29), L341(6.33), S401(8.47), D403(8.49). The S401A and D403A mutations increased [3H]-SR141716A binding. The simulations also showed the extracellular site of ORG27569 as possible. Pandey 2025Computer modelCell / lab
The TRPV2 channel and CBD: a structure imaged with CBD bound
Structure determined by cryo-electron microscopy at 3.2 Å resolution: the rat TRPV2 ion channel, made of four identical subunits, with one CBD molecule in each subunit. CBD sits in a fat-loving pocket between the membrane helices of neighboring subunits. This is one of the structures in which CBD has been imaged bound to one of its targets; the channel is a rat channel, and there is no CBD-bound structure of human TRPV2. Pumroy 2019Molecular structure (lab)PDB 6U88Molecular structure (lab)
Expert level: method notes
Method note
Pumroy 2019: full-length rat TRPV2 in nanodiscs, ligand-free and CBD-bound states; 6U88 state 2 (3.2 Å), 6U8A state 1 (3.4 Å); bound ligand P0T = cannabidiol. CBD sits in a hydrophobic pocket between the S5 and S6 helices of neighboring subunits; this pocket differs from the ligand and lipid sites known in other TRP channels; the S4–S5 linker is decisive for gate opening. In the scene, the channel's symmetry axis is drawn vertically; the position of the membrane was estimated approximately from the average of the long helices. Pumroy 2019Molecular structure (lab)PDB 6U88Molecular structure (lab)
Five molecules: two endocannabinoids, three plant cannabinoids
You can rotate each one in 3D in the map's Molecule view. Formula and weight come from the PubChem record; the 3D shapes are computed. PubChemComputer model
Anandamide is a fat-derived messenger molecule that the body makes itself. It was found in pig brain in 1992, during a search for a substance that binds to the receptor that compounds in cannabis bind to. It switches the receptor on, but not at full strength. When its job is done, an enzyme called FAAH breaks it down and ends its effect.
2-AG is the second of the body's own cannabinoids. It was found in 1995 by two separate teams working independently: one in dog intestine, the other in rat brain. In most experiments, it switches cannabinoid receptors on at full strength, and when its job is done it is broken down mainly by an enzyme called MAGL.
THC is the main mind-altering (psychoactive) component of cannabis. Its chemical structure was described in Israel in a 1964 paper published by Yehiel Gaoni and Raphael Mechoulam. It switches on the body's CB1 and CB2 receptors, but only partly, not at full strength.
CBD is a molecule found in cannabis whose chemical structure was described in 1963 by Raphael Mechoulam and Yuval Shvo. It is made of the same atoms as THC, but because one of its rings is open, its shape is different. It does not switch on the CB1 and CB2 receptors the way THC does; it binds to these receptors much more weakly.
CBN is the first cannabinoid isolated in pure form from cannabis: it was isolated in Cambridge at the end of the 19th century. The plant does not make it directly; it forms when THC reacts with air and slowly degrades, which is why there is more of it in cannabis that has been stored for a long time. It binds to the CB1 receptor more weakly than THC.
CBD binds weakly to the CB1 and CB2 receptors; unlike THC, it does not directly stimulate CB1. Thomas 2007Cell / labLu and Mackie 2016ReviewThomas 2007: [35S]GTPγS binding assay, mouse brain membranes (CB1) and CHO cells transfected with human CB2; CBD antagonized agonists more potently than expected from its low affinity and behaved like an inverse agonist at CB2. No numerical KB value in the abstract.
In cell experiments, it behaved like a "negative allosteric modulator" of CB1: it bound to a different site on the receptor and reduced the effect of 2-AG and THC. Laprairie 2015Cell / labPandey 2025Computer modelCell / labLaprairie 2015: HEK 293A cells transfected with CB1 and the striatal neuron model STHdh(Q7/Q7); CBD lowered the efficacy and potency of 2-AG and THC on PLCβ3 and ERK1/2 signaling and reduced arrestin2 recruitment; the effect depended on residues 98 and 107 in the extracellular end of CB1; conclusion: non-competitive negative allosteric modulator.
It has other targets as well: effects on the serotonin 5-HT1A receptor, the TRPV1 channel and the GPR55 receptor have been shown in the lab. Russo 2005Cell / labBisogno 2001Cell / labRyberg 2007Cell / labRusso 2005: cloned human 5-HT1A, CHO cells; "modest affinity agonist". Bisogno 2001: CBD stimulated TRPV1 (VR1) with EC50 3.2–3.5 µM. Ryberg 2007: cells transfected with GPR55; GPR55 couples to Gα13.
In the lab, it weakly slowed the breakdown of anandamide. In a clinical study in schizophrenia, anandamide levels rose in the blood of people taking CBD. Bisogno 2001Cell / labLeweke 2012Human · clinical studyBisogno 2001: anandamide hydrolysis IC50 27.5 µM, uptake IC50 22.0 µM ("weak"). Leweke 2012: double-blind, randomized study with an amisulpride comparison; significant rise in serum anandamide in the CBD arm (biomarker finding).
According to a review, more than 65 targets have been reported for CBD; most effects were seen only at high concentrations that are hard to reach in the body, and it is unlikely that its neurological effects work through the endocannabinoid system. Ibeas Bih 2015ReviewIbeas Bih 2015: systematic search of original papers on the molecular pharmacology of CBD; the plausible targets left after screening (such as VDAC1, GPR55, CaV3.x) relate to the regulation of intracellular calcium.
Whether a result holds in humans is shown by the strength of evidence on the condition pages: evidence map.
CBD's other targets
Many targets have been reported for CBD; one review counted more than 65. This list does not mean "CBD does these things": most of the effects were seen only in the lab, at high concentrations that are hard to reach in the body. The five targets below are the most studied. For none of them has it been shown that an effect of CBD in humans works through that target. Ibeas Bih 2015Review
Student and expert level
Ibeas Bih 2015 systematically searched original papers on the molecular pharmacology of CBD: more than 65 separate targets had been reported, and relatively few passed plausibility criteria. For some targets, effects were seen only at high, non-physiological concentrations; CBD's bioavailability is relatively low; and several targets had been proposed only on the basis of experimental designs showing correlation. Ibeas Bih 2015ReviewIbeas Bih 2015 (review): the plausible targets left after screening (such as VDAC1, GPR55, CaV3.x) relate to the regulation of intracellular calcium or to responses to calcium changes. The authors judged it very unlikely that CBD's neurological effects work through the endocannabinoid system.
Concentrations at which lab effects were seen, and the level in blood (µM, logarithmic axis). Dashed line: the highest level measured in blood.
Peak blood level with regular use (healthy volunteers): about 1.7 µM Human · clinical study
Halving of anandamide breakdown (IC50): 27.5 µM Cell / lab
5-HT1A effect in human brain tissue (no effect up to 10 µM): 100 µM Human tissue
110100
In a Phase 1 study of the approved CBD medicine, when healthy volunteers took the drug regularly for one week at the study's highest repeated dose, the mean peak blood level was 541 ng/mL; by calculation, this is about 1.7 µM. In the same study, when a single dose was taken with a high-fat breakfast, the mean peak rose to 1,628 ng/mL (about 5.2 µM). All of the laboratory effects below were seen at concentrations above the level reached with regular use; the TRPV1 and TRPV2 values stay below the highest mean seen with a single dose taken with a high-fat meal. The blood level is not exactly the same as the tissue level, and CBD travels in the blood largely bound to proteins; still, if an effect appears only at many times the blood level, separate evidence is needed before assuming it also happens in humans. Taylor 2018Human · clinical studyEpidiolex label (FDA)Official drug label
Expert level: study and drug label details
In a Phase 1 study of the approved CBD medicine, when healthy volunteers took the drug regularly for one week at the study's highest repeated dose, the mean peak blood level was 541 ng/mL; by calculation, this is about 1.7 µM. In the same study, when a single dose was taken with a high-fat breakfast, the mean peak rose to 1,628 ng/mL (about 5.2 µM). All of the laboratory effects below were seen at concentrations above the level reached with regular use; the TRPV1 and TRPV2 values stay below the highest mean seen with a single dose taken with a high-fat meal. The blood level is not exactly the same as the tissue level, and CBD travels in the blood largely bound to proteins; still, if an effect appears only at many times the blood level, separate evidence is needed before assuming it also happens in humans. Taylor 2018Human · clinical studyEpidiolex label (FDA)Official drug labelTaylor 2018: Phase 1, randomized, double-blind, placebo-controlled. In the multiple-dose arm, 1,500 mg twice daily; on day 7 (steady state), geometric mean Cmax 541.2 ng/mL, AUCτ 3,236 ng·h/mL; 1,385 ng/mL after the evening dose on day 1. In the single-dose arms, Cmax 782 ng/mL at the highest dose, 6,000 mg; in the food arm, 1,500 mg gave 1,628 ng/mL fed and 335.4 ng/mL fasted (Tables 6–8). Exposure increased less than dose-proportionally. The µM conversion is ours (molecular weight 314.46 g/mol): 541.2 ng/mL ≈ 1.72 µM, 1,628 ng/mL ≈ 5.18 µM. Label section 12.3 does not give an absolute Cmax; with a high-fat meal, Cmax increased 5-fold and AUC 4-fold, and protein binding in vitro is above 94%. Label 12.1: mechanism of action unknown; does not appear to work through cannabinoid receptors.
In the lab, CBD bound to and activated the receptor in cells engineered to carry the human 5-HT1A receptor; the authors called it "a modest affinity agonist". In membranes prepared from human brain tissue, however, the interaction was very weak: no effect was seen up to 10 µM, and at 100 µM the receptor's spontaneous activity decreased. In rats, some behavioral effects of CBD disappeared with a substance that blocks 5-HT1A.
In the lab, CBD opened this channel: in cells carrying human TRPV1, half of the effect was seen at 3.2–3.5 µM, and its maximum effect was close to that of capsaicin. At 10 µM, it desensitized the channel to capsaicin; that is, it first opened the channel and then silenced it. In human colon tissue removed during surgery, the anti-inflammatory effect of CBD disappeared with a substance that blocks TRPV1 (in tissue in the lab, not in living people).
GPR55Long an "orphan" receptor · in the cell membrane
In the first study, CBD showed activity at GPR55; most later studies, however, used CBD as a blocker here. CBD reduced the effect of GPR55 activators in human and mouse bone-resorbing cells; in rodent hippocampal slices, it abolished the effect of GPR55 activation on the synapse. CBD's role at this receptor is not fully clear.
In the lab, CBD bound to this receptor and increased its gene-switching activity; it turned mouse precursor cells into fat cells. It caused the same change in human and mouse stem cells, and a substance that blocks PPARγ greatly reduced this effect. In rat blood vessels, part of CBD's relaxing effect appeared to depend on PPARγ, but according to the authors most of it came from blocking calcium channels.
In cell experiments, CBD was the strongest activator of this channel among the cannabinoids tested: half of the effect was seen at 3.7 µM (14 µM for THC). The structure in which CBD has been imaged bound to one of its targets is also here: cryo-electron microscopy solved the CBD-bound structure of rat TRPV2 and showed CBD sitting in a fat-loving pocket between neighboring subunits.
On the map, Lesson mode goes through the stops below in order; at each stop the camera moves to the relevant region. Classroom mode puts the map in full screen, hides the panel and makes the text large enough to read on a projector; use the right and left arrow keys to move on. To start from a specific stop, add something like ?ders=3 to the link.
The body's own cannabinoid system. The endocannabinoid system is made up of cannabinoids the body makes itself, the receptors they bind to (mainly CB1 and CB2), and the enzymes that make and break them down. Solid lights show the level of CB1 measured in human tissue, and rings show the level of CB2; each region has its own color. Lu and Mackie 2016ReviewHuman Protein AtlasHuman tissue
Where CB1 is densest: the cerebral cortex. CB1 is measured at its highest level in the cerebral cortex. It is densest in the areas of the frontal and limbic lobes where higher-level thinking takes place, and sparsest in the primary sensory and motor areas. Human Protein AtlasHuman tissueGlass 1997Human tissue
A brake in the hippocampus. In the hippocampus, CB1 clusters on the terminals of inhibitory nerve cells. At these terminals, endocannabinoids briefly reduce GABA release; the signal travels backward from the receiving cell. Katona 1999AnimalWilson and Nicoll 2001Animal
Backward signaling at the synapse. The receiving cell makes endocannabinoids when needed. They cross the gap in the opposite direction and bind to CB1 on the sending terminal; calcium entry into the terminal decreases, and release of the messenger substance drops for tens of seconds. Wilson and Nicoll 2001AnimalKreitzer and Regehr 2001AnimalTanimura 2010Animal
Spinal cord: the gateway for pain signals. In the rat spinal cord, CB1 was seen mostly in the surface layers of the dorsal horn, where pain signals are first processed. The endocannabinoid system is considered one of the body's own pain control systems; most of this knowledge comes from animal studies. Farquhar-Smith 2000AnimalWoodhams 2017Review
Fat tissue and energy balance. In fat tissue, CB1 RNA is measured at a level very close to that of the cerebral cortex. Human fat cells carry CB1 and CB2 and make their own endocannabinoids. Human Protein AtlasHuman tissueRoche 2006Human tissueCell / labGonthier 2007Cell / lab
Immunity: CB2's main home. CB2 was identified from immune cells of the spleen. In human tissues, CB2 is 10–100 times more abundant than CB1 in immune organs; it is found most in B lymphocytes. Munro 1993AnimalCell / labGaliègue 1995Human tissue
Where on the receptor does CBD bind?. CBD binds weakly to CB1 and CB2 and does not directly stimulate CB1 the way THC does. In cell experiments, it bound to a different site on the receptor and reduced the effect of 2-AG and THC; the proposed binding site has not yet been confirmed. Thomas 2007Cell / labLaprairie 2015Cell / labPandey 2025Computer modelCell / lab
Journey · Routes of entry. CBD and THC can enter the body by swallowing, inhaling, through the lining of the mouth and through the skin. An inhaled substance travels from the lungs to the heart and from there to the whole body; when THC was smoked, the blood level peaked at minute 9. A swallowed substance, by contrast, passes through the liver first. StatPearls: Routes of AdministrationReviewStatPearls: Lung VeinsReviewHuestis 1992aHuman · clinical study
Journey · First pass through the liver. CBD taken by mouth is absorbed from the intestine and reaches the liver first through the portal vein. The liver converts most of the absorbed amount into other molecules; it is estimated that only about 6 percent of the amount taken on an empty stomach reaches the blood. With the approved CBD medicine, a high-fat meal increased the peak blood level about 5-fold. StatPearls: Portal Venous SystemReviewPerucca 2020ReviewEpidiolex label (FDA)Official drug label
Journey · Changes in the liver. In the liver, THC is converted first into the active 11-OH-THC, then into THC-COOH, which has no THC-like effect. When THC is taken by mouth, a lot of 11-OH-THC forms as it passes through the liver: its blood level ranges from half of THC's level to the same level. Oral THC capsule label (FDA)Official drug labelWall 1983Human · clinical studyHuestis 1992bHuman · clinical study
Journey · Distribution to tissues and fat. THC that enters the blood spreads into tissues and fat tissue, and from there slowly returns to the blood. This is why the blood level does not always reflect the effect at that moment: in a small human study, the effect lagged behind the blood level. Johansson 1989bHuman tissueSativex product information (UK)Official drug labelCocchetto 1981Human · clinical study
Journey · Elimination and how long it stays in the body. CBD leaves the body mostly in the stool; when the approved CBD medicine was taken regularly for one week, its half-life was 56–61 hours. Most of THC's breakdown products pass into the stool through bile; THC-COOH, which urine tests look for, can be detected for days. Epidiolex label (FDA)Official drug labelEpidyolex product information (EMA)Official drug labelOral THC capsule label (FDA)Official drug labelLowe 2009Human · clinical study
You can save the view as an image with an attribution line using the Download PNG button, or add it to your own page with the Embed button (CC BY-SA 4.0).
Human Protein Atlas v25, tissue RNA consensus data (CB1, CB2 and 15 more genes in the layer selector) and brain region data (nTPM), CC BY 4.0; data from v25.proteinatlas.org. Uhlén et al., Science 2015 (PMID 25613900).
Molecular structure
RCSB PDB 6KPG (Hua et al., Cell 2020, PMID 32004463) and 6U88 (Pumroy et al., eLife 2019, PMID 31566564). PDB data CC0 1.0.
Small molecules
National Center for Biotechnology Information, PubChem Compound: formula, weight, IUPAC name, InChIKey and computed 3D conformers for THC, CBD and CBN (NLM public data, attribution requested). 3D forms for anandamide and 2-AG were generated with RDKit.
Banner image
Margaret I. Davis, Cell Image Library CIL:14971 (UC San Diego Library), mouse hippocampus, CB1 antibody staining; CC0 1.0. The channels were mapped to the site's colors.
Text and scene
cbd.com.tr Editorial Team, October 24, 2026. The synapse scene is schematic; scale and shapes are illustrative. The flowing lights in the nerves and spinal cord are illustrative.
Downloaded images and embedding
PNG images downloaded from the map and the embedded map may be used under CC BY-SA 4.0. Attribution: cbd.com.tr, 3D Endocannabinoid System Map; model BodyParts3D (DBCLS), Z-Anatomy and HuBMAP HRA; data Human Protein Atlas.
Evidence type labels: Human · clinical study, Human · observational study, Human · case report, Human tissue, Human · genetic study, Animal, Cell / lab, Molecular structure (lab), Chemistry lab, Review, Research on publications, Official drug label, Agency opinion, Computer model. Each label was checked against the subject headings (MeSH) of the source in PubMed.
Cite this page: cbd.school editorial team. Endocannabinoid system 3D map. . https://cbd.school/learn/endocannabinoid-system-map/
Review and researchers
This map was compiled by the cbd.school editorial team from published research; the source of every sentence is shown next to it, and each source was checked in its PubMed record for retraction. An independent expert review has not been done yet; it is planned, and the reviewer’s name will appear here once it is done.
The first and last authors of the studies the map is based on are listed below, with the institutions given in their PubMed records. These researchers did not review the map; they are named because their work is cited. If you spot an error or something missing, you can let us know through the contact page.
Researchers in the sources (387 people, alphabetical)
Abood ME Showalter 1996
Abu-Shaar M Munro 1993
Adami M · Institute of Pharmacology, University of Parma, 43100 Parma, Italy Adami 2002
Ameloot K · Department of Internal Medicine, University Hospital Gasthuisberg, University of Leuven, Belgium Ameloot 2010
Anand P Mukerji 2010
Andersen CU · Department of Clinical Pharmacology, Aarhus University Hospital, Aarhus, Denmark Sønderskov 2025
Andersson KE Gratzke 2009 · Füllhase 2014 · Campeau 2014
Arceri L · Center for Stem Cells and Regenerative Medicine, USA Arceri 2023
Arkell TR · Lambert Initiative for Cannabinoid Therapeutics, The University of Sydney, Sydney, New South Wales, Australia Arkell 2020
Aseer KR · National Institute on Aging, United States Aseer and Egan 2021
Atieh J · Clinical Enteric Neuroscience and Translational and Epidemiological Research (CENTER), USA Atieh 2022
Auboeuf D · Institut National de la Santé et de la Recherche Medicale (INSERM) U.449 and Lyon Human Nutrition Research Center, France Auboeuf 1997
Baar K · University of California, USA Langer 2022
Bab I · Bone Laboratory, The Hebrew University of Jerusalem, Jerusalem, Israel Bab and Zimmer 2008 · Ofek 2006 · Kogan 2015
Bakali E · Prolapse and Incontinence Research Group, University of Leicester, Leicester, UK Bakali 2013 · Bakali 2016
Barna I · Institute of Experimental Medicine, 1083 Budapest, P.O. Box 67, Hungary Barna 2004
Barutta F · Diabetic Nephropathy Laboratory, Department of Internal Medicine, University of Turin, Turin, Italy Barutta 2010 · Barutta 2011
Bateman DN Bateman 1983
Bátkai S · National Institute on Alcohol Abuse & Alcoholism, USA Bátkai 2004
Bermúdez-Silva FJ · Fundación IMABIS, Hospital Carlos Haya, Avenida Carlos Haya 82, 7a Planta, Pabellón A, 29010 Málaga, Spain Bermúdez-Silva 2008
Bezuglov E · Sechenov First Moscow State Medical University of the Ministry of Health of the Russian Federation, Russia Bezuglov 2024
Bíró T · University of Debrecen, Hungary Bíró 2009 · Dobrosi 2008 · Oláh 2014
Bisogno T · Istituto per la Chimica di Molecole di Interesse Biologico, Italy Bisogno 2001
Blaner WS · Institute of Human Nutrition, USA Lee 2020
Blüher M · University of Leipzig, Medical Department III, Philipp-Rosenthal-Str. 27, 04103 Leipzig, Germany Blüher 2006
Blumberg B · Department of Developmental and Cell Biology, USA Chang 2022
Bodor AL · Institute of Experimental Medicine, Hungary Bodor 2005
Boini K · Virginia Commonwealth University School of Medicine, VA Ritter 2016
Bolton EE · National Center for Biotechnology Information, USA Bolton 2011
Brown DR Kulkarni-Narla and Brown 2000
Bryant SH Bolton 2011 · Kim 2013
Burdyga G · Physiological Laboratory, University of Liverpool, Liverpool L69 3BX, United Kingdom Burdyga 2004
Calignano A · Department of Pharmacology, University of Naples, Italy Calignano 2000
Camilleri M · Clinical Enteric Neuroscience and Translational and Epidemiological Research (CENTER), USA Atieh 2022 · Zheng 2023
Campeau L · Wake Forest Institute for Regenerative Medicine, North Carolina Campeau 2014
Capasso R · University of Naples Federico II, Italy Capasso 2011
Caprioglio D · University of Piemonte Orientale, Italy Maioli 2022
Carayon P · Immunology Department, Sanofi Recherche, Montpellier, France Carayon 1998
Casellas P Galiègue 1995 · Carayon 1998
Castillo PE · Dominick P. Purpura Department of Neuroscience, Albert Einstein College of Medicine, Bronx, NY 10461, USA Castillo 2012
Caterina MJ · Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143-0450, USA Caterina 1997 · Caterina 1999
Cavuoto P · Royal Adelaide Hospital, Australia Cavuoto 2007a · Cavuoto 2007b
Cervero F Walczak 2009
Chandra V · and Center for Molecular Design, USA Chandra 2008
Chang RC · Department of Developmental and Cell Biology, USA Chang 2022
Chen J · Department of Biological Sciences, Allergan Inc., Irvine, CA, USA Chen 2005
Cheng S · Department of Health Sciences, University of Jyväskylä, Jyväskylä, Finland Pekkala 2015
Chiellini G · Department of Pathology, University of Pisa, 56100 Pisa, Italy Saponaro 2021
Chittiboyina AG · National Center for Natural Products Research, United States Pandey 2025
Christie S · College of Medicine and Public Health, Australia Christie 2021
Civan MM · Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA, USA Civan and Macknight 2004
Claff T Claff 2025
Cochrane-Snyman KC · Department of Health and Human Performance, Concordia University Chicago, River Forest, IL Cochrane-Snyman 2021
Coles M · Department of Kinesiology, California State University, Fresno, Fresno, CA Cochrane-Snyman 2021
Compton DR Mechoulam 1995
Contreras-Duarte S · School of Nutrition and Dietetics, Chile Elgueta 2026
Corroon J · The Center for Medical Cannabis Education, Del Mar, California, USA Corroon 2021
Coruzzi G · Pharmacology and Forensic Medicine, Parma Coruzzi 2006
Cota D · Clinical Neuroendocrinology Group, Max-Planck-Institute of Psychiatry, Munich, Germany Cota 2003 · Cota 2007
Couch DG · School of Medicine, Royal Derby Hospital, University of Nottingham, Derby DE22 3DT, U.K Couch 2017
Cravatt BF · Department of Chemistry, The Scripps Research Institute, La Jolla, California 92307, USA Cravatt 1996
da Veiga MA · Instituto de Biofísica Carlos Chagas Filho, Brazil da Veiga 2008
Dalle S · 3001, Leuven, Belgium Dalle and Koppo 2021
De Pasquale R Germanò 2001
de Wit H Phan 2008
Delwel R Rayman 2004 · Valk 1997
Denovan-Wright EM · Departments of Pharmacology, Dalhousie University, Halifax, NS, Canada Laprairie 2015
Desai S · School of Medicine, USA Desai 2022
Deutsch DG · Department of Biochemistry & Cell Biology, State University of New York, Stony Brook, New York 11794, USA Deutsch 1997
Devane WA · Department of Natural Products, Medical Faculty, Hebrew University, Jerusalem, Israel Devane 1992
Devillier P Grassin-Delyle 2014
Devinsky O · From New York University Langone Comprehensive Epilepsy Center, New York (O.D.) Devinsky 2018
Di Marzo V · Istituto per la Chimica di Molecole di Interesse Biologico, Italy Di Marzo 2001 · Chen 2005 · Bisogno 2001 · Iannotti 2014b · Iannotti 2019
Didik S · Department of Molecular Pharmacology and Physiology, University of South Florida, Tampa, FL, 33602, USA Didik 2025
Diel P · Institute for Cardiovascular Research and Sports Medicine, Germany Isenmann 2021
Dinh TP · Department of Pharmacology, University of California, Irvine, CA 92697-4625, USA Dinh 2002
Dobrosi N · University of Debrecen, Hungary Dobrosi 2008
Dockray GJ Burdyga 2004
Dudášová A · School of Life Sciences, University of Hertfordshire, CP Snow Building, Hatfield, UK Dudášová 2013
Eckardt K · Institute of Clinical Biochemistry and Pathobiochemistry, Germany Eckardt 2009
Eckel J Eckardt 2009
Egan JM · National Institute on Aging, USA González-Mariscal 2016 · Aseer and Egan 2021 · González-Mariscal and Egan 2018
Eggan SM · Department of Neuroscience, University of Pittsburgh, Pittsburgh, PA 15213, USA Eggan and Lewis 2007 · Eggan 2010
Ehrhart-Bornstein M Ziegler 2010
Einicker-Lamas M · Instituto de Biofísica Carlos Chagas Filho, UFRJ, Rio de Janeiro, Brazil Sampaio 2015
Elgueta S · School of Nutrition and Dietetics, Chile Elgueta 2026
Elphick MR Farquhar-Smith 2000
Engeli S · Franz Volhard Clinical Research Center, Charité Campus Buch, 13125 Berlin, Germany Engeli 2005
Erman A · Institute of Cell Biology, Faculty of Medicine, University of Ljubljana, 1000 Ljubljana, Slovenia Peskar 2026
Esfandyari T · Clinical Enteric Neuroscience Translational and Epidemiological Research (CENTER) Program, USA Esfandyari 2006
Facchin F · University of Bologna, Italy Petrocelli 2025
Fairbairn JW Fairbairn 1976
Fantauzzi MF · Firestone Institute for Respiratory Health - Division of Respirology, Canada Fantauzzi 2020
Farquhar-Smith WP · Imperial College School of Medicine, United Kingdom Farquhar-Smith 2000
Faull RL Glass 1997
Fekete C · Laboratory of Integrative Neuroendocrinology, Institute of Experimental Medicine, Budapest, Hungary Kővári 2022
Felder CC · Laboratory of Cell Biology, National Institute of Mental Health, Bethesda, Maryland 20892, USA Felder 1995
Festy F Roche 2006
Flores CM Qin 2008
François H · 1] INSERM Unité 1014, France Lecru 2015
Freund TF Katona 1999 · Katona 2001 · Bodor 2005 · Vizi 2001 · Gulyas 2004
Füllhase C · Department of Urology, Klinikum Großhadern, Munich, Germany Füllhase 2014
Fusar-Poli P · Institute of Psychiatry, England Fusar-Poli 2009
Fuss J · Institute for Sex Research, Germany Siebers 2021
Gaitán AV · Louisiana State University and Louisiana State University Agricultural Center, Baton Rouge, LA 70803, USA Gaitán 2018 · Gaitán 2021
Galiègue S · Sanofi Recherche, Immunopharmacology Department, Montpellier, France Galiègue 1995
Gerdle B Ghafouri 2011
Germanò MP · Pharmaco-Biological Department, School of Pharmacy, University of Messina, Italy Germanò 2001
Ghafouri N · Faculty of Health Sciences, Sweden Ghafouri 2011
Gilula NB Cravatt 1996
Gkoumassi E · University Centre for Pharmacy, The Netherlands Gkoumassi 2007
Glass M · Department of Anatomy, School of Medicine, University of Auckland, New Zealand Glass 1997
Gochman A · Porter Neuroscience Research Center, United States Gochman 2023
Gokoh M Sugiura 2006
Gonsiorek W · Department of Immunology, Schering-Plough Research Institute, Kenilworth, NJ 07033-0539, USA Gonsiorek 2000
Gonthier MP · Université de La Réunion, France Gonthier 2007
González-Mariscal I · National Institute on Aging, USA González-Mariscal 2016 · González-Mariscal and Egan 2018
Gorzalka BB Hill 2009
Grandes P · Department of Neurosciences, Faculty of Medicine and Nursing, University of the Basque CountryLeioa, Spain Mendizabal-Zubiaga 2016
Grassin-Delyle S · Laboratoire de Pharmacologie Respiratoire, UPRES EA220, Hôpital Foch, Suresnes, France Grassin-Delyle 2014
Gratzke C · Wake Forest Institute for Regenerative Medicine, Winston-Salem, North Carolina, USA Gratzke 2009
Greasley PJ Ryberg 2007
Gruden G Barutta 2010 · Barutta 2011
Guan DW · China Medical University School of Forensic Medicine Shenyang 110122, P. R. China Zhang 2015
Guimarães FS Resstel 2009
Gulyas AI · Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, PO Box 67, H-1450, Hungary Gulyas 2004
GWPCARE3 Study Group Devinsky 2018
GWPCARE4 Study Group Thiele 2018
Gyires K · Semmelweis University, Hungary Gyires and Zádori 2016
Hall H · Karolinska Institutet, Department of Clinical Neuroscience, Karolinska Hospital, Stockholm, Sweden Hall 1997
Hashimotodani Y · Graduate School of Medicine, Japan Castillo 2012 · Hashimotodani 2013
Hedlund P Strittmatter 2012 · Hedlund 2014
Herkenham M · Unit on Functional Neuroanatomy, National Institute of Mental Health, Bethesda, MD 20892 Herkenham 1990 · Westlake 1994 · Hohmann and Herkenham 1999
Herring AC · Department of Pharmacology & Toxicology, Michigan State University, East Lansing 48824, USA Herring 1998
Hill MN · Department of Psychology, University of British Columbia, Vancouver, BC, Canada Hill 2009 · Hill 2010
Hillard CJ · and Neuroscience Research Center, USA Patel and Hillard 2001 · Patel 2004 · Hillard 2016
Hipkin RW Gonsiorek 2000
Hirota JA · Firestone Institute for Respiratory Health - Division of Respirology, Canada Fantauzzi 2020
Hohmann AG · Section on Functional Neuroanatomy, National Institute of Mental Health, Bethesda, MD 20892-4070, USA Hohmann and Herkenham 1999
Hornby PJ Krowicki 1999
Horvath TL · Yale University School of Medicine, USA Koch 2015
Howlett AC · Wake Forest University Health Sciences, USA Mechoulam 2014
Hryciw DH Jenkin 2013
Hua T · iHuman Institute, ShanghaiTech University, Shanghai 201210, China Hua 2020
Hundal H · 1 The Biomedical Research Centre, King's College London, UK Hundal 2018
Iannotti FA · Institute of Biomolecular Chemistry (ICB), 80078 Pozzuoli (NA) Italy Iannotti 2014a · Iannotti 2014b · Iannotti 2019
Ibeas Bih C · School of Chemistry, UK Ibeas Bih 2015
Isenmann E · Institute for Cardiovascular Research and Sports Medicine, Germany Isenmann 2021
Ishima Y Sugiura 1999
Izzo AA · University of Naples Federico II and Endocannabinoid Research Group, Naples, Italy Izzo and Sharkey 2010 · Capasso 2011
James LJ · National Centre for Sport and Exercise Medicine, United Kingdom Johnson 2026
Jamshidi N · Victorian College of Pharmacy, Australia Jamshidi and Taylor 2001
Jara-Oseguera A · College of Natural Sciences, United States Gochman 2023
Jenkin KA · Victoria University, Australia Jenkin 2013
Johnson DA · National Centre for Sport and Exercise Medicine, United Kingdom Johnson 2026
Jordan J Engeli 2005
Jourdan T · Laboratory of Physiologic Studies, Section on Neuroendocrinology, and Jourdan 2014
Juan-Picó P · Instituto de Bioingeniería, Spain Juan-Picó 2006
Julius D Caterina 1997 · Caterina 1999
Kaminski NE · Institute for Integrative Toxicology, Michigan State University, MI, USA Khan 2026 · Herring 1998
Kano M · Department of Neurophysiology, The University of Tokyo, Tokyo, Japan Kano 2009 · Tanimura 2010 · Hashimotodani 2013
Kapralova E · Sechenov First Moscow State Medical University of the Ministry of Health of the Russian Federation, Russia Bezuglov 2024
Karsak M · Department of Molecular Psychiatry, University of Bonn, Germany Karsak 2007 · Karsak 2005
Katona I · Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, H-1450, Hungary Katona 1999 · Katona 2001
Kelly ME McIntosh 2007
Kendall DA O'Sullivan 2009
Khan DMIO · Institute for Integrative Toxicology, Michigan State University, MI, USA Khan 2026
Kim S · National Center for Biotechnology Information, USA Kim 2013
Koch M · Yale University School of Medicine, Germany Koch 2015
Koethe D Leweke 2012
Kogan NM · Bone Laboratory, Hebrew University of Jerusalem, Jerusalem, Israel Kogan 2015
Koppo K · 3001, Leuven, Belgium Dalle and Koppo 2021 · Schouten 2022
Korf HW Yasuo 2010
Korkusuz P · Department of Histology and Embryology, Faculty of Medicine, Hacettepe University, Ankara, Turkey Köse 2018
Köse S · Institute of Health Sciences, Turkey Köse 2018
Koura Y · Internal Medicine, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan Koura 2004
Kővári D · Laboratory of Integrative Neuroendocrinology, Institute of Experimental Medicine, Budapest, Hungary Kővári 2022
Kreitzer AC · Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA Kreitzer and Regehr 2001
Krowicki ZK · Louisiana State University Medical Center, USA Krowicki 1999
Kulkarni-Narla A · University of Minnesota, Department of Veterinary Pathobiology, Saint Paul 55108-6010, USA Kulkarni-Narla and Brown 2000
Kunos G · Laboratory of Physiologic Studies, Section on Neuroendocrinology, and Di Marzo 2001 · Osei-Hyiaman 2005 · Liu 2000 · Bátkai 2004 · Jourdan 2014
Kuret T · Institute of Cell Biology, Faculty of Medicine, University of Ljubljana, 1000 Ljubljana, Slovenia Kuret 2023
Lammi-Keefe CJ · Louisiana State University and Louisiana State University Agricultural Center, Baton Rouge, LA 70803, USA Gaitán 2018 · Gaitán 2021
Langer HT · University of California, USA Langer 2022
McPartland JM · Department of Molecular Biology, GW Pharmaceuticals, Salisbury, Wiltshire, UK McPartland 2007
Mechoulam R · Faculty of Medicine, Hebrew University, Jerusalem, Israel Devane 1992 · Mechoulam 1995 · Mechoulam and Shvo 1963 · Mechoulam 2014
Mendizabal-Zubiaga J · Department of Neurosciences, Faculty of Medicine and Nursing, University of the Basque CountryLeioa, Spain Mendizabal-Zubiaga 2016
Milburn MV Nolte 1998
Mitchell RL Felder 1995
Moiseenkova-Bell VY · Perelman School of Medicine, United States Pumroy 2019
Moore LC Deutsch 1997
Moreira AC Zuardi 1993
Morrison G · GW Research Ltd, Cambridge, UK Taylor 2018 · Tayo 2020
Morrison PD · 1 The Biomedical Research Centre, King's College London, UK Hundal 2018
Mukerji G · Peripheral Neuropathy Unit, Hammersmith Hospital and Imperial College, London, United Kingdom Mukerji 2010
Munro S · MRC Laboratory of Molecular Biology, Cambridge, UK Munro 1993
Nadal A Juan-Picó 2006
Nelemans SA Gkoumassi 2007
Neuberger A · Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA Neuberger 2023
Neugebauer V · Center of Excellence for Translational Neuroscience and Therapeutics, USA Woodhams 2017
Nicoll RA Wilson and Nicoll 2001
Niederhoffer N · Institut für Experimentelle und Klinische Pharmakologie und Toxikologie, Germany Niederhoffer 2001
Nolte RT · Glaxo Wellcome Research and Development, USA Nolte 1998
Nording ML · Department of Chemistry, Umeå University, 901 87 Umeå, Sweden Wu 2016
O'Dowd BF Sawzdargo 1999
O'Sullivan SE · School of Medicine, University of Nottingham, Royal Derby Hospital, Derby, DE22 3DT, UK Stanley 2016 · Stanley and O'Sullivan 2014 · Stanley 2015 · Couch 2017 · O'Sullivan 2009
Ofek O · Bone Laboratory, Hebrew University of Jerusalem, Jerusalem 91120, Israel Ofek 2006
Oláh A Oláh 2014
Osei-Hyiaman D · National Institute on Alcohol Abuse & Alcoholism, NIH, Bethesda, Maryland 20892, USA Osei-Hyiaman 2005
Pacher P Bíró 2009 · Pan 2009
Pagano C · University of Padova, Italy Pagano 2007 · Pagano 2008
Page CP Dudášová 2013
Pagotto U · Neuroendocrinology Group, Max Planck Institute of Psychiatry, 80804 Munich, Germany Cota 2003 · Pagotto 2001 · Pagotto 2006 · Cota 2007
Pan H · The First Affiliated Hospital, China Pan 2009
Pandey P · National Center for Natural Products Research, United States Pandey 2025
Pani L Porcella 2000 · Porcella 2002
Parker KK Russo 2005
Parker LA Rock 2012
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