By Veit M. Flockerzi (Editor), Bernd Nilius (Editor)
During this fast paced box the most target of this quantity is to supply up to date details at the molecular and useful homes and pharmacology of mammalian TRP channels. top specialists within the box have written 35 essays which describe houses of a unmarried TRP protein/channel or painting extra basic rules of TRP functionality and significant pathological occasions associated with mutations of TRP genes or their altered expression. Thereby this quantity on brief Receptor strength (TRP) Channels presents worthwhile info for readers with various expectancies and backgrounds, in case you are imminent this box of study in addition to for these desirous to make a visit to TRPs, from pharmacologists and physiologists to doctors, different scientists, scholars and academics. It fills a spot among pharmacology textbooks and most recent manuscripts in medical periodicals.
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Additional resources for Transient Receptor Potential (TRP) Channels (Handbook of Experimental Pharmacology)
5 Modulation of TRPC1 Function While the mechanism of activation of TRPC1 is not yet clearly deﬁned, it remains difﬁcult to distinguish the pathway or pathways central to the activation mechanism from those pathways which may be involved in modulation or regulation of the TRPC1 channel. The activation and/or activity of TRPC1 is modulated by Ca2+ and calmodulin (Singh et al. 2002), protein kinase C (Ahmmed et al. 2004; Larsson et al. 2005) and other protein kinases, (reviewed in Beech 2005). Like many of the other TRPC proteins, TRPC1 is inhibited by Ca2+ and calmodulin, and this is thought to be part of a feedback inhibition mechanism (Tang et al.
A schematic representation of the TRPC1 polypeptide as an integral protein in the plasma membrane. It is hypothesised that the endogenous nonselective cation channels formed from TRPC1 polypeptides are heterotetramers composed of a mixture of TRPC1 and one or more other TRPC polypeptides. The LFW hydrophobic domain of TRPC1 contributes to the channel pore. Features of the membrane-spanning domains and sequences with known functions are shown. References are given in the text. ANK 1–3, ankyrin-like repeats 1 to 3; CC-N and CC-C, N- and C- terminal coiled-coil domains, respectively; CIRB, calmodulin/InsP3 receptor (IP3 R) binding region; LFW, amino acid motif conserved in the hydrophobic putative pore region TRPC1 Ca2+ -Permeable Channels in Animal Cells 27 28 G.
46 References . . . . . . . . . . . . . . . . . . . . 47 . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Abstract The full-length transient receptor (TRPC)1 polypeptide is composed of about 790 amino acids, and several splice variants are known. The predicted structure and topology is of an integral membrane protein composed of six transmembrane domains, and a cytoplasmic C- and N-terminal domain. The N-terminal domain includes three ankyrin repeat motifs.
Transient Receptor Potential (TRP) Channels (Handbook of Experimental Pharmacology) by Veit M. Flockerzi (Editor), Bernd Nilius (Editor)