The TRP superfamily of channels (nomenclature agreed by NC-IUPHAR; [16,118]), whose founder member is the Drosophila Trp channel, exists in mammals as six families; TRPC, TRPM, TRPV, TRPA, TRPP and TRPML based on amino acid homologies. TRP subunits contain six putative transmembrane domains and assemble as homo- or hetero-tetramers to form cation selective channels with diverse modes of activation and varied permeation properties (reviewed by [82]). Established, or potential, physiological functions of the individual members of the TRP families are discussed in detail in the recommended reviews and a compilation edited by Islam [42]. The established, or potential, involvement of TRP channels in disease is reviewed in [49,75] and [76], together with a special edition of Biochemica et Biophysica Acta on the subject [75]. The pharmacology of most TRP channels is poorly developed [118]. Broad spectrum agents are listed in the tables along with more selective, or recently recognised, ligands that are flagged by the inclusion of a primary reference. Most TRP channels are regulated by phosphoinostides such as PtIns(4,5)P₂ and IP₃ although the effects reported are often complex, occasionally contradictory, and likely be dependent upon experimental conditions (reviewed by [77,94,110]). Such regulation is generally not included in the tables.

TRPA (ankyrin) family
TRPA1 is the sole mammalian member of this group (reviewed by [31]). In some [6,44,97,101], but not other [43,71], studies TRPA1 is activated by noxious cold. One study suggests that activation of TRPA1 is secondary to a cold-induced elevation of [Ca²⁺]_i [124], but this has been refuted [44]. Additionally, TRPA1 has been proposed to be a component of a mechanosensitive transduction channel of vertebrate hair cells [18,71], but TRPA1^(-/-) mice demonstrate no impairment in hearing, or vestibular function [10,54]. There is consensus that TRPA1 acts as a nociceptor for environmental irritants [7].

TRPC (canonical) family
Members of the TRPC subfamily (reviewed by [1-2,13-14,30,47,84,92]) fall into the subgroups outlined below. TRPC2 (not tabulated) is a pseudogene in man. It is generally accepted that all TRPC channels are activated downstream of G_q/11-coupled receptors, or receptor tyrosine kinases (reviewed by [89,104,118]). A comprehensive listing of G-protein coupled receptors that activate TRPC channels is given in [1]. Hetero-oligomeric complexes of TRPC channels and their association with proteins to form signalling complexes are detailed in [2] and [48]. TRPC channels have frequently been proposed to act as store-operated channels (SOCs) (or compenents of mulimeric complexes that form SOCs), activated by depletion of intracellular calcium stores (reviewed by [2,15,85,90,96,121]), but this is controversial. All members of the TRPC family are blocked by 2-APB and SKF96356 [37-38]. Activation of TRPC channels by lipids is discussed by [13].

TRPC1/C4/C5 subgroup
TRPC4/C5 may be distinguished from other TRP channels by their potentiation by micromolar concentrations of La³⁺.

TRPC3/C6/C7 subgroup
All members are activated by diacylglycerol independent of protein kinase C stimulation [38].

TRPM (melastatin) family
Members of the TRPM subfamily (reviewed by [29,37,85,123]) fall into the five subgroups outlined below.

TRPM1/M3 subgroup
TRPM1 exists as five splice variants and is involved in normal melanocyte pigmentation [80] and is also a visual transduction channel in retinal ON bipolar cells [53]. TRPM3 (reviewed by [81]) exists as multiple splice variants four of which (mTRPM3α1, mTRPM3α2, hTRPM3a and hTRPM3₁₃₂₅) have been characterised and found to differ significantly in their biophysical properties. TRPM3 has recently been found to contribute to the detection of noxious heat [113].

TRPM2
TRPM2 functions as a sensor of redox status in cells and is also activated by heat (reviewed by [120]). Numerous splice variants of TRPM2 exist which differ in their activation mechanisms [26].

TRPM4/5 subgroup
TRPM4 and TRPM5 are thermosensitive and have the distinction within all TRP channels of being impermeable to Ca²⁺ [118]. A splice variant of TRPM4 (i.e.TRPM4b) and TRPM5 are molecular candidates for endogenous calcium-activated cation (CAN) channels [34]. TRPM4 has been shown to be an important regulator of Ca²⁺ entry in to mast cells [106] and dendritic cell migration [8]. TRPM5 in taste receptor cells of the tongue appears essential for the transduction of sweet, amino acid and bitter stimuli [59].

TRPM6/7 subgroup
TRPM6 and 7 combine channel and enzymatic activities (‘chanzymes’) and are involved in Mg²⁺ homeostasis (reviewed by [9,86,95]).

TRPM8
Is a channel activated by cooling and pharmacological agents evoking a ‘cool’ sensation and participates in the thermosensation of cold temperatures [12,17,24] reviewed by [52,61,70,111].

TRPML (mucolipin) family
The TRPML family [91,93,122] consists of three mammalian members (TRPML1-3). TRPML channels are probably restricted to intracellular vesicles and mutations in the gene (MCOLN1) encoding TRPML1 (mucolipin-1) are the cause of the neurodegenerative disorder mucolipidosis type IV (MLIV) in man. TRPML1 is a cation selective ion channel that is important for sorting/transport of endosomes in the late endocytotic pathway and specifically fusion between late endosome-lysosome hybrid vesicles. TRPML2 (MCLN2) remains to be functionally characterised in detail. TRPML3 is important for hair cell maturation, stereocilia maturation and intracellular vesicle transport. A naturally occurring gain of function mutation in TRPML3 (i.e. A419P) results in the varitint waddler (Va) mouse phenotype (reviewed by [78,93]).

TRPP (polycystin) family
The TRPP family (reviewed by [21,23,32,40,116]) subsumes the polycystins that are divided into two structurally distinct groups, polycystic kidney disease 1-like (PKD1-like) and polycystic kidney disease 2-like (PKD2-like). Members of the PKD1-like group, in mammals, include PKD1 (reclassified as TRPP1), PDKREJ, PKD1L1, PKD1L2 and PKD1L3. The PKD2-like members comprise PKD2, PKD2L1 and PKD2L2, which have renamed TRPP2, TRPP3 and TRPP5, respectively [68]. PKDREJ (ENSG00000130943), PKD1L1 (ENSG00000158683), PKD1L2 (ENSMUS00000034416), PKD1L3 (ENSG00000187008) and TRPP5 (ENSG00000078795) are not listed in the table due to lack of functional data. Similarly, TRPP1 (ENSG00000008710) is also omitted because although one study [5] has reported the induction of a cation conductance in CHO cells transfected with TRPP1, there is no unequivocal evidence that TRPP1 is a channel per se and in other studies (e.g. [22,36]) TRPP1 is incapable of producing currents.

TRPV (vanilloid) family
Members of the TRPV family (reviewed by [107]) can broadly be divided into the theromosensitive, non-selective cation channels, TRPV1-4 and the calcium selective channels TRPV5 and TRPV6.

TRPV1-V4 subfamily
TRPV1 is involved in the development of thermal hyperalgesia following inflammation and may contribute to the detection of noxius heat (reviewed by [88,100,102]). Numerous splice variants of TRPV1 have been described, some of which modulate the activity of TRPV1, or act in a dominant negative manner when co-expressed with TRPV1 [98]. The pharmacology of TRPV1 channels is discussed in detail in [35] and [112]. TRPV2 is probably not a thermosensor in man [83], but has recently been implicated in innate immunity [60]. TRPV3 and TRPV4 are both thermosensitive, with the latter also having a mechanosensing function [27].

TRPV5/V6 subfamily
Under physiological conditions, TRPV5 and TRPV6 are calcium selective channels involved in the absorption and reabsorption of calcium across intestinal and kidney tubule epithelia (reviewed by [20,115]).

TRPA (ankyrin) family
Agents activating TRPA1 in a covalent manner are thiol reactive electrophiles that bind to cysteine and lysine residues within the cytoplasmic domain of the channel [39,62]. TRPA1 is activated by a wide range of endogenous and exogenous compounds and only a few representative examples are mentioned in the table: an exhaustive listing can be found in [7]. In addition, TRPA1 is potently activated by intracellular zinc (EC₅₀ = 8 nM) [4,41].

TRPM (melastatin) family
Ca²⁺ activates all splice variants of TRPM2, but other activators listed are effective only at the full length isoform [26]. Inhibition of TRPM2 by clotrimazole, miconazole, econazole, flufenamic acid is largely irreversible. TRPM4 exists as multiple spice variants: data listed are for TRPM4b. The sensitivity of TRPM4b and TRPM5 to activation by [Ca²⁺]_i demonstrates a pronounced and time-dependent reduction following excision of inside-out membrane patches [105]. The V_½ for activation of TRPM4 and TRPM5 demonstrates a pronounced negative shift with increasing temperature. Activation of TRPM8 by depolarization is strongly temperature-dependent via a channel-closing rate that decreases with decreasing temperature. The V_½ is shifted in the hyperpolarizing direction both by decreasing temperature and by exogenous agonists, such as menthol [109] whereas antagonists produce depolarizing shifts in V_½ [69]. The V_½ for the native channel is far more positive than that of heterologously expressed TRPM8 [69]. It should be noted that menthol and structurally related compounds can elicit release of Ca²⁺ from the endoplasmic reticulum independent of activation of TRPM8 [63]. Intracellular pH modulates activation of TRPM8 by cold and icilin, but not menthol [3].

TRPML (mucolipin) family
Data in the table are for TRPML proteins mutated (i.e TRPML1^Va, TRPML2^Va and TRPML3^Va) at loci equivalent to TRPML3 A419P to allow plasma membrane expression when expressed in HEK-293 cells and subsequent characterisation by patch-clamp recording [25,33,45,72,119]. Data for wild type TRPML3 are also tabulated [45-46,72,119]. It should be noted that alternative methodologies, particularly in the case of TRPML1, have resulted in channels with differing biophysical characteristics (reviewed by [91]).

TRPP (polycystin) family
Data in the table are extracted from [19,23] and [99]. Broadly similar single channel conductance, mono- and di-valent cation selectivity and sensitivity to blockers are observed for TRPP2 co-expressed with TRPP1 [22]. Ca²⁺, Ba²⁺ and Sr²⁺ permeate TRPP3, but reduce inward currents carried by Na⁺. Mg²⁺ is largely impermeant and exerts a voltage dependent inhibition that increases with hyperpolarization.

TRPV (vanilloid) family
Activation of TRPV1 by depolarisation is strongly temperature-dependent via a channel opening rate that increases with increasing temperature. The V_½ is shifted in the hyperpolarizing direction both by increasing temperature and by exogenous agonists [109]. The sensitivity of TRPV4 to heat, but not 4α-PDD is lost upon patch excision. TRPV4 is activated by anandamide and arachidonic acid following P450 epoxygenase-dependent metabolism to 5,6-epoxyeicosatrienoic acid (reviewed by [79]). Activation of TRPV4 by cell swelling, but not heat, or phorbol esters, is mediated via the formation of epoxyeicosatrieonic acids. Phorbol esters bind directly to TRPV4. TRPV5 preferentially conducts Ca²⁺ under physiological conditions, but in the absence of extracellular Ca²⁺, conducts monovalent cations. Single channel conductances listed for TRPV5 and TRPV6 were determined in divalent cation-free extracellular solution. Ca²⁺-induced inactivation occurs at hyperpolarized potentials when Ca²⁺ is present extracellularly. Single channel events cannot be resolved (probably due to greatly reduced conductance) in the presence of extracellular divalent cations. Measurements of P_Ca/P_Na for TRPV5 and TRPV6 are dependent upon ionic conditions due to anomalous mole fraction behaviour. Blockade of TRPV5 and TRPV6 by extracellular Mg²⁺ is voltage-dependent. Intracellular Mg²⁺ also exerts a voltage dependent block that is alleviated by hyperpolarization and contributes to the time-dependent activation and deactivation of TRPV6 mediated monovalent cation currents. TRPV5 and TRPV6 differ in their kinetics of Ca²⁺-dependent inactivation and recovery from inactivation. TRPV5 and TRPV6 function as homo- and hetero-tetramers.

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