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TRP channels in platelet function.
Authi, K S.
Affiliation
  • Authi KS; Cardiovascular Division, King's College London, New Hunts House, Guy's Campus, London SE1 1UL, UK. kalwant.authi@kcl.ac.uk
Handb Exp Pharmacol ; (179): 425-43, 2007.
Article in En | MEDLINE | ID: mdl-17217071
ABSTRACT
Ca2+ entry forms an essential component of platelet activation; however, the mechanisms associated with this process are not understood. Ca2+ entry upon receptor activation occurs as a consequence of intracellular store depletion (referred to as store-operated Ca2+ entry or SOCE), a direct action of second messengers on cation entry channels or the direct occupancy of a ligand-gated P2(Xi) receptor. The molecular identity of the SOCE channel has yet to be established. Transient receptor potential (TRP) proteins are candidate cation entry channels and are classified into a number of closely related subfamilies including TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPP (polycystin) and TRPML (mucolipins). From the TRPC family, platelets have been shown to express TRPC6 and TRPC1, and are likely to express other TRPC and other TRP members. TRPC6 is suggested to be involved with receptor-activated, diacyl-glycerol-mediated cation entry. TRPC1 has been suggested to be involved with SOCE, though many of the suggested mechanisms remain controversial. As no single TRP channel has the properties described for SOCE in platelets, it is likely that it is composed of a heteromeric association of TRP and related subunits, some of which may be present in intracellular compartments in the resting cell.
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Collection: 01-internacional Database: MEDLINE Main subject: Blood Platelets / Transient Receptor Potential Channels Limits: Animals / Humans Language: En Journal: Handb Exp Pharmacol Year: 2007 Document type: Article Affiliation country: Reino Unido
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Blood Platelets / Transient Receptor Potential Channels Limits: Animals / Humans Language: En Journal: Handb Exp Pharmacol Year: 2007 Document type: Article Affiliation country: Reino Unido