The ionotropic glutamate receptors comprise members of the NMDA (N-methyl-D-aspartate), AMPA (α-amino-3-hydroxy-5-methyl- 4-isoxazoleproprionic acid) and kainate receptor classes, named originally according to their preferred, synthetic, agonist [11,33,53]. Receptor heterogeneity within each class arises from the homo-oligomeric, or hetero-oligomeric, assembly of distinct subunits into cation-selective tetramers. Each subunit of the tetrameric complex comprises an extracellular amino terminal domain (ATD), an extracellular ligand binding domain (LBD), a transmembrane domain (TMD) composed of three membrane spans (M1, M3 and M4) with a channel lining re-entrant ‘p-loop’ (M2) located between M1 and M3 and an intracellular carboxy- terminal domain (CTD) [26,36,39,53]. The X-ray structure of a homomeric ionotropic glutamate receptor (GluA2 – see below) has recently been solved at 3.6Å resolution [50] and although providing the most complete structural information current available may not representative of the subunit arrangement of, for example, the heteromeric NMDA receptors [27]. It is beyond the scope of this supplement to discuss the pharmacology of individual ionotropic glutamate receptor isoforms in detail; such information can be gleaned from [6,10-11,14,24-25,28,42] and [53] . Agents that discriminate between subunit isoforms are, where appropriate, noted in the tables and additional compounds that distinguish between receptor isoforms are indicated in the text below.

The classification of glutamate receptor subunits has been recently been re-addressed by NC-IUPHAR [8]. The scheme developed recommends a revised nomenclature for ionotropic glutamate receptor subunits that is adopted here.

NMDA receptors
NMDA receptors assemble as obligate heteromers that may be drawn from GluN1, GluN2A, GluN2B, GluN2C, GluN2D, GluN3A and GluN3B subunits. Alternative splicing can generate eight isoforms of GluN1 with differing pharmacological properties. Various splice variants of GluN2B, 2C, 2D and GluN3A have also been reported. Activation of NMDA receptors containing GluN1 and GluN2 subunits requires the binding of two agonists, glutamate to the S1 and S2 regions of the GluN2 subunit and glycine to S1 and S2 regions of the GluN1 subunit [7,13]. The minimal requirement for efficient functional expression of NMDA receptors in vitro is a di-heteromeric assembly of GluN1 and at least one GluN2 subunit variant, as a dimer of heterodimers arrangement in the extracellular domain [18,27,36]. However, more complex tri-heteromeric assemblies, incorporating multiple subtypes of GluN2 subunit, or GluN3 subunits, can be generated in vitro and occur in vivo. The NMDA receptor channel commonly has a high relative permeability to Ca²⁺ and is blocked, in a voltage-dependent manner, by Mg²⁺ such that at resting potentials the response is substantially inhibited.

AMPA and Kainate receptors
AMPA receptors assemble as homomers, or heteromers, that may be drawn from GluA1, GluA2, GluA3 and GluA4 subunits. Transmembrane AMPA receptor regulatory proteins (TARPs) of class I (i.e. γ2, γ3, γ4 and γ8) act, with variable stoichiometry, as auxiliary subunits to AMPA receptors and influence their trafficking, single channel conductance gating and pharmacology (reviewed in [15,23,37,51]). Functional kainate receptors can be expressed as homomers of GluK1, GluK2 or GluK3 subunits. GluK1-3 subunits are also capable of assembling into heterotetramers (e.g. GluK1/K2; [30,44-45]). Two additional kainate receptor subunits, GluK4 and GluK5, when expressed individually, form high affinity binding sites for kainate, but lack function, but can form heteromers when expressed with GluK1-3 subunits (e.g. GluK2/K5; reviewed in [25,44-45]). Kainate receptors may also exhibit ‘metabotropic’ functions [30,47]. As found for AMPA receptors, kainate receptors are modulated by auxiliary subunits (Neto proteins, [31,44]). An important function difference between AMPA and kainate receptors is that the latter require extracellular Na+ and Cl- for their activation [3,46]. RNA encoding the GluA2 subunit undergoes extensive RNA editing in which the codon encoding a p-loop glutamine residue (Q) is converted to one encoding arginine (R). This Q/R site strongly influences the biophysical properties of the receptor. Recombinant AMPA receptors lacking RNA edited GluA2 subunits are: (1) permeable to Ca²⁺; (2) blocked by intracellular polyamines at depolarized potentials causing inward rectification (the latter being reduced by TARPs); (3) blocked by extracellular argiotoxin and Joro spider toxins and (4) demonstrate higher channel conductances than receptors containing the edited form of GluA2 [22,48]. GluK1 and GluK2, but not other kainate receptor subunits, are similarly edited and broadly similar functional characteristics apply to kainate receptors lacking either an RNA edited GluK1, or GluK2, subunit [30,44]. Native AMPA and kainate receptors displaying differential channel conductances, Ca²⁺ permeabilites and sensitivity to block by intracellular polyamines have been identified [9,22,32]. GluA1-4 can exist as two variants generated by alternative splicing (termed ‘flip’ and ‘flop’) that differ in their desensitization kinetics and their desensitization in the presence of cyclothiazide which stabilises the nondesensitized state. TARPs also stabilise the non-desensitized conformation of AMPA receptors and facilitate the action of cyclothiazide [37]. Splice variants of GluK1-3 also exist which affects their trafficking [30,44].

NMDA receptors
Potency orders unreferenced in the table are from [6,12,14,29,42,53]. In addition to the glutamate and glycine binding sites documented in the table, physiologically important inhibitory modulatory sites exist for Mg²⁺, Zn²⁺, and protons [10-11,53]. Voltage-independent inhibition by Zn²⁺ binding with high affinity within the ATD is highly subunit selective (GluN2A >> GluN2B > GluN2C ≥ GluN2D; [42,53]). The receptor is also allosterically modulated, in both positive and negative directions, by endogenous neuroactive steroids in a subunit dependent manner [21,35]. Tonic proton blockade of NMDA receptor function is alleviated by polyamines and the inclusion of exon 5 within GluN1 subunit splice variants, whereas the non-competitive antagonists ifenprodil and CP101606 (traxoprodil) increase the fraction of receptors blocked by protons at ambient concentration. Inclusion of exon 5 also abolishes potentiation by polyamines and inhibition by Zn²⁺ that occurs through binding in the ATD [52]. Ifenprodil, CP101606, haloperidol, felbamate and Ro8-4304 discriminate between recombinant NMDA receptors assembled from GluN1 and either GluN2A, or GluN2B, subunits by acting as selective, non-competitive, antagonists of heterooligomers incorporating GluN2B through a binding site at the ATD GluN1/GluN2B subunit interface [27]. LY233536 is a competitive antagonist that also displays selectivity for GluN2B over GluN2A subunit-containing receptors. Similarly, CGP61594 is a photoaffinity label that interacts selectively with receptors incorporating GluN2B versus GluN2A, GluN2D and, to a lesser extent, GluN2C subunits. In addition to influencing the pharmacological profile of the NMDA receptor, the identity of the GluN2 subunit co-assembled with GluN1 is an important determinant of biophysical properties that include sensitivity to block by Mg²⁺, single-channel conductance and maximal open probablity and channel deactivation time [10,13,19]. Incorporation of the GluN3A subunit into tri-heteromers containing GluN1 and GluN2 subunits is associated with decreased single-channel conductance, reduced permeability to Ca²⁺ and decreased susceptibility to block by Mg²⁺ [4,20]. Reduced permeability to Ca²⁺ has also been observed following the inclusion of GluN3B in tri-heteromers. The expression of GluN3A, or GluN3B, with GluN1 alone forms, in Xenopus laevis oocytes, a cation channel with unique properties that include activation by glycine (but not NMDA), lack of permeation by Ca²⁺ and resistance to blockade by Mg²⁺ and NMDA receptor antagonists [5]. The function of heteromers composed of GluN1 and GluN3A is enhanced by Zn²⁺, or glycine site antagonists, binding to the GluN1 subunit [34]. Zn²⁺ also directly activates such complexes. The co-expression of GluN1, GluN3A and GluN3B appears to be required to form glycine-activated receptors in mammalian cell hosts [49].

AMPA and Kainate receptors
All AMPA receptors are additionally activated by kainate (and domoic acid) with relatively low potency, (EC₅₀ ~ 100 µM). Inclusion of TARPs within the receptor complex increases the potency and maximal effect of kainate [23,37]. AMPA is weak partial agonist at GluK1 and at heteromeric assemblies of GluK1/GluK2, GluK1/GluK5 and GluK2/GluK5 [25]. Quinoxalinediones such as CNQX and NBQX show limited selectivity between AMPA and kainate receptors. LY293558 also has kainate (GluK1) receptor activity as has GYKI53655 (GluK3 and GluK2/GluK3) [25]. ATPO is a potent competitive antagonist of AMPA receptors, has a weaker antagonist action at kainate receptors comprising GluK1 subunits, but is devoid of activity at kainate receptors formed from GluK2 or GluK2/GluK5 subunits. The pharmacological activity of ATPO resides with the (S)-enantiomer. ACET and UBP310 may block GluK3, in addition to GluK1 [1,43]. (2S,4R)-4-methylglutamate (SYM2081) is equipotent in activating (and desensitising) GluK1 and GluK2 receptor isoforms and, via the induction of desensitisation at low concentrations, has been used as a functional antagonist of kainate receptors. Both (2S,4R)-4-methylglutamate and LY339434 have agonist activity at NMDA receptors. (2S,4R)-4-methylglutamate is also an inhibitor of the glutamate transporters EAAT1 and EAAT2.

Delta subunits
GluD1 and GluD2 comprise, on the basis of sequence homology, an ‘orphan’ class of ionotropic glutamate receptor subunit. They do not form a functional receptor when expressed solely, or in combination with other ionotropic glutamate receptor subunits, in transfected cells [54]. However, GluD2 subunits bind D-serine and glycine and GluD2 subunits carrying the mutation A654T form a spontaneously open channel that is closed by D-serine [40].

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