TY - JOUR
T1 - Transient receptor potential canonical 7
T2 - A diacylglycerol-activated non-selective cation channel
AU - Zhang, Xuexin
AU - Trebak, Mohamed
N1 - Publisher Copyright:
© Springer-Verlag Berlin Heidelberg 2014.
PY - 2014
Y1 - 2014
N2 - Transient receptor potential canonical 7 (TRPC7) channel is the seventh member of the mammalian TRPC channel family. TRPC7 mRNA, protein, and channel activity have been detected in many tissues and organs from the mouse, rat, and human. TRPC7 has high sequence homology with TRPC3 and TRPC6, and all three channels are activated by membrane receptors that couple to isoforms of phospholipase C (PLC) and mediate non-selective cation currents. TRPC7, along with TRPC3 and TRPC6, can be activated by direct exogenous application of diacylglycerol (DAG) analogues and by pharmacological maneuvers that increase endogenous DAG in cells. TRPC7 shows distinct properties of activation, such as constitutive activity and susceptibility to negative regulation by extracellular Ca2+ and by protein kinase C. TRPC7 can form heteromultimers with TRPC3 and TRPC6. Although TRPC7 remains one of the least studied TRPC channel, its role in various cell types and physiological and pathophysiological conditions is beginning to emerge.
AB - Transient receptor potential canonical 7 (TRPC7) channel is the seventh member of the mammalian TRPC channel family. TRPC7 mRNA, protein, and channel activity have been detected in many tissues and organs from the mouse, rat, and human. TRPC7 has high sequence homology with TRPC3 and TRPC6, and all three channels are activated by membrane receptors that couple to isoforms of phospholipase C (PLC) and mediate non-selective cation currents. TRPC7, along with TRPC3 and TRPC6, can be activated by direct exogenous application of diacylglycerol (DAG) analogues and by pharmacological maneuvers that increase endogenous DAG in cells. TRPC7 shows distinct properties of activation, such as constitutive activity and susceptibility to negative regulation by extracellular Ca2+ and by protein kinase C. TRPC7 can form heteromultimers with TRPC3 and TRPC6. Although TRPC7 remains one of the least studied TRPC channel, its role in various cell types and physiological and pathophysiological conditions is beginning to emerge.
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U2 - 10.1007/978-3-642-54215-2_8
DO - 10.1007/978-3-642-54215-2_8
M3 - Article
C2 - 24756707
AN - SCOPUS:84904883861
SN - 0171-2004
VL - 222
SP - 189
EP - 204
JO - Handbook of Experimental Pharmacology
JF - Handbook of Experimental Pharmacology
ER -