Premium
Specificity of TRPC5 Calcium Channel Activation by Lipid Signalling Molecules
Author(s) -
Bahnasi Yahya M,
Zeng Fanning,
Dedman Alexandra M,
Naylor Jaqueline,
Beech David J,
Bateson Alan N
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.lb18-c
Subject(s) - trpc5 , chemistry , lipidome , microbiology and biotechnology , receptor , transient receptor potential channel , biochemistry , trpc , biology , lipidomics
TRPC5, a member of the classical transient receptor potential ion channel family, is widely expressed in different tissues being most abundant in the brain where it regulates neurite length (Greka et al, 2003, Nature Neuro. 6.8, 837–845). TRPC5 is activated by a multiplicity of signals including receptor‐activation, store‐depletion and lanthanides (Zeng et al, 2004, J.Physiol. 559.3, 739–750). We also showed recently that TRPC5 senses lysophosphatidylcholine (Flemming et al, 2005, J. Biol. Chem., in press). In this study, we further explored the specificity of TRPC5 activation by testing a broader range of signalling lipid molecules. Real‐time 96‐well plate assays on tetracycline induced (Tet+) TRPC5‐expressing HEK293 cells showed that TRPC5 could be activated by several lysophospholipids, galactosylsphingosine and gangliosides (10 μM). TRPC5 non‐expressing cells (Tet‐) were not activated by those lipids. TRPC5 was not stimulated by other lipids including sphingosine, ceramide, ceramide‐1‐phosphate, sphingomyelin, cholesterol or anandamide. Our data suggest specificity of TRPC5's lipid‐sensing capability but also sensitivity to more than one class of lipids. Work supported by the Wellcome Trust and The Egyptian Ministry of Higher Education.