TRPV

Transient receptor potential (TRP) ion channel

Identifiers

Symbol

TRP

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

TRPV is a family of transient receptor potential cation channels (TRP channels) in animals. All TRPVs are highly calcium selective.

TRP channels are a large group of ion channels, comprising six protein families, located mostly on the plasma membrane of numerous human and animal cell types, and in some fungi.^[1] TRP channels were initially discovered in the trp mutant strain of the fruit fly Drosophila ^[2] which displayed transient elevation of potential in response to light stimuli and were so named "transient receptor potential" channels.^[3] The name now refers only to a family of proteins with similar structure and function, not to the mechanism of their activation. Later, TRP channels were found in vertebrates where they are ubiquitously expressed in many cell types and tissues. There are about 28 TRP channels that share some structural similarity to each other.^[4] These are grouped into two broad groups: group 1 includes, TRPC ( "C" for canonical), TRPV ("V" for vanilloid), TRPM ("M" for melastatin), TRPN and TRPA. In group 2 there are TRPP ("P" for polycystic) and TRPML ("ML" for mucolipin).

Function

TRPV proteins respond to the taste of garlic (allicin). TRPV1 contributes to heat and inflammation sensations and mediates the pungent odor and pain sensations associated with capsaicin and piperine.

Clinical significance

Mutations in TRPs have been linked to neurodegenerative disorders, skeletal dysplasia, kidney disorders,^[1] and may play an important role in cancer. TRPs may make important therapeutic targets. There is significant clinical significance to TRPV1, TRPV2, and TRPV3's role as thermoreceptors, and TRPV4’s role as mechanoreceptors; reduction of chronic pain may be possible by targeting ion channels involved in thermal, chemical, and mechanical sensation to reduce their sensitivity to stimuli.^[5] For instance, the use of TRPV1 agonists would potentially inhibit nociception at TRPV1, particularly in pancreatic tissue where TRPV1 is highly expressed.^[6] The TRPV1 agonist capsaicin, found in chili peppers, has been indicated to relieve neuropathic pain.^[1] TRPV1 agonists inhibit nociception at TRPV1.

Role in cancer

Altered expression of TRP proteins often leads to tumorigenesis, clearly seen in TRPM1.^[6] Particularly high levels of TRPV6 in prostate cancer have been noted. Such observations could be helpful in following cancer progression and could lead to the development of drugs over activating ion channels, leading to apoptosis and necrosis. Much research remains to be done as to whether TRP channel mutations lead to cancer progression or whether they are associated mutations.

References

1 2 3 Winston, K. R.; Lutz, W (1988). "Linear accelerator as a neurosurgical tool for stereotactic radiosurgery". Neurosurgery. 22 (3): 454–64. doi:10.1097/00006123-198803000-00002. PMID 3129667.
↑ Cosens, D. J.; Manning, A (1969). "Abnormal electroretinogram from a Drosophila mutant". Nature. 224 (5216): 285–7. doi:10.1038/224285a0. PMID 5344615.
↑ Montell, C; Rubin, G. M. (1989). "Molecular characterization of the Drosophila trp locus: A putative integral membrane protein required for phototransduction". Neuron. 2 (4): 1313–23. doi:10.1016/0896-6273(89)90069-x. PMID 2516726.
↑ Islam MS, ed. (January 2011). Transient Receptor Potential Channels. Advances in Experimental Medicine and Biology. 704. Berlin: Springer. p. 700. ISBN 978-94-007-0264-6.
↑ Levine, J. D.; Alessandri-Haber, N (2007). "TRP channels: Targets for the relief of pain". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1772 (8): 989–1003. doi:10.1016/j.bbadis.2007.01.008. PMID 17321113.
1 2 Prevarskaya, N; Zhang, L; Barritt, G (2007). "TRP channels in cancer". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1772 (8): 937–46. doi:10.1016/j.bbadis.2007.05.006. PMID 17616360.

External links

Transient Receptor Potential Channels at the US National Library of Medicine Medical Subject Headings (MeSH)
"Transient Receptor Potential Channels". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
"TRIP Database". a manually curated database of protein-protein interactions for mammalian TRP channels.

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Ligand-gated	Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3

Voltage-gated	L-type/Ca_vα 1.1 1.2 1.3 1.4 N-type/Ca_vα2.2 P-type/Ca_vα 2.1 Q-type/Ca_vα2.1 R-type/Ca_vα2.3 T-type/Ca_vα 3.1 3.2 3.3 α₂δ-subunits 1 2 β-subunits β1 β2 β3 β4 γ-subunits γ1 γ2 γ3 γ4 Cation channels of sperm 1 2 3 4 Two-pore channel 1 2

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel α β γ δ

Proton-gated	Amiloride-sensitive cation channel 1 2 3 4

Voltage-gated	Na_vα 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 7A Na_vβ 1 2 3 4

K⁺: Potassium channel

Calcium-activated	BK channel α1 β1 β2 β3 β4 SK channel SK1 SK2 SK3 IK channel IK1 K_Ca 1.1 2.1 2.2 2.3 3.1 4.1 4.2 5.1

Inward-rectifier	K_ATP K_ir 1.1 2.1 2.2 2.3 2.4 2.6 GIRK/K_ir 3.1 3.2 3.3 3.4 K_ir 4.1 4.2 5.1 6.1 6.2 7.1

Tandem pore domain	K2P 1 2 3 4 5 6 7 9 10 12 13 15 16 17 18

Voltage-gated	K_vα1-6 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 2.1 2.2 3.1 3.2 3.3 3.4 4.1 4.2 4.3 5.1 6.1 6.2 6.3 6.4 K_vα7-12 7.1 7.2 7.3 7.4 7.5 8.1 8.2 9.1 9.2 9.3 10.1 10.2 11.1/hERG 11.2 11.3 12.1 12.2 12.3 K_vβ 1 2 3 KCNIP 1 2 3 4 minK/ISK minK/ISK-like MiRP 1 2 3 Shaker gene

Miscellaneous

Cl⁻: Chloride channel	Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B

H⁺: Proton channel	HVCN1

M⁺: CNG cation channel	α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4

M⁺: TRP cation channel	TRPA (1) TRPC 1 2 3 4 4AP 5 6 7 TRPM 1 2 3 4 5 6 7 8 TRPML 1 2 3 TRPN TRPP 1 2 TRPV 1 2 3 4 5 6

H₂O (+ solutes): Porin	Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family

Cytoplasm: Gap junction	Connexin: A GJA1 GJA3 GJA4 GJA5 GJA8 GJA9 GJA10 B GJB1 GJB2 GJB3 GJB4 GJB5 GJB6 GJB7 C GJC1 GJC2 GJC3 D GJD2 GJD3 GJD4) Innexin

By gating mechanism

Ion channel class	Ligand-gated Light-gated Voltage-gated Stretch-activated

see also disorders

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