TrpC5 is one of the seven mammalian TRPC (transient receptor potential canonical) proteins. TrpC5 is a multi-pass membrane protein and is thought to form a receptor-activated non-selective calcium permeant cation channel. The protein is active alone or as a heteromultimeric assembly with TRPC1, TRPC3, and TRPC4. It also interacts with multiple proteins including calmodulin, CABP1, enkurin, Na+–H+ exchange regulatory factor (NHERF), interferon-induced GTP-binding protein (MX1), ring finger protein 24 (RNF24), and SEC14 domain and spectrin repeat-containing protein 1 (SESTD1).[1]
TRPC4 and TRPC5 have been implicated in the mechanism of mercury toxicity[4] and neurological behavior.[5]
Activation
Homomultimeric TRPC5 and heteromultimeric TRPC5-TRPC1 channels are activated by extracellular reduced thioredoxin.[6] This channel has also been found to be involved in the action of anaesthetics such as chloroform, halothane and propofol.[7]
↑Sossey-Alaoui K, Lyon JA, Jones L, Abidi FE, Hartung AJ, Hane B, Schwartz CE, Stevenson RE, Srivastava AK (September 1999). "Molecular cloning and characterization of TRPC5 (HTRP5), the human homologue of a mouse brain receptor-activated capacitative Ca2+ entry channel". Genomics. 60 (3): 330–40. doi:10.1006/geno.1999.5924. PMID10493832.
↑Clapham DE, Julius D, Montell C, Schultz G (December 2005). "International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels". Pharmacol. Rev. 57 (4): 427–50. doi:10.1124/pr.57.4.6. PMID16382100.
↑Xu SZ, Zeng B, Daskoulidou N, Chen GL, Atkin SL, Lukhele B (January 2012). "Activation of TRPC cationic channels by mercurial compounds confers the cytotoxicity of mercury exposure". Toxicol. Sci. 125 (1): 56–68. doi:10.1093/toxsci/kfr268. PMID21984481.
↑Greka A, Navarro B, Oancea E, Duggan A, Clapham DE (August 2003). "TRPC5 is a regulator of hippocampal neurite length and growth cone morphology". Nat. Neurosci. 6 (8): 837–45. doi:10.1038/nn1092. PMID12858178.
↑Strübing C, Krapivinsky G, Krapivinsky L, Clapham DE (October 2003). "Formation of novel TRPC channels by complex subunit interactions in embryonic brain". J. Biol. Chem. 278 (40): 39014–9. doi:10.1074/jbc.M306705200. PMID12857742.