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Revisiting TRPC1 and TRPC6 mechanosensitivity

TLDR
Although several TRPC channel members, including TRPC1 and TRPC6, have been recently proposed to form MscCa in vertebrate cells, the functional expression of these TRPC subunits in heterologous systems remains problematic.
Abstract
This article addresses whether TRPC1 or TRPC6 is an essential component of a mammalian stretch-activated mechano-sensitive Ca2+ permeable cation channel (MscCa). We have transiently expressed TRPC1 and TRPC6 in African green monkey kidney (COS) or Chinese hamster ovary (CHO) cells and monitored the activity of the stretch-activated channels using a fast pressure clamp system. Although both TRPC1 and TRPC6 are highly expressed at the protein level, the amplitude of the mechano-sensitive current is not significantly altered by overexpression of these subunits. In conclusion, although several TRPC channel members, including TRPC1 and TRPC6, have been recently proposed to form MscCa in vertebrate cells, the functional expression of these TRPC subunits in heterologous systems remains problematic.

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Journal ArticleDOI

Physiology of cell volume regulation in vertebrates.

TL;DR: Current knowledge regarding the molecular identity of these transport pathways and their regulation by, e.g., membrane deformation, ionic strength, Ca(2+), protein kinases and phosphatases, cytoskeletal elements, GTP binding proteins, lipid mediators, and reactive oxygen species are reviewed.
Journal ArticleDOI

Transient Receptor Potential Channels as Drug Targets: From the Science of Basic Research to the Art of Medicine

TL;DR: An overview of the functional properties of mammalian TRP channels is given, their roles in acquired and hereditary diseases are described, and their potential as drug targets for therapeutic intervention is discussed.
Journal ArticleDOI

The Role of Transient Receptor Potential Cation Channels in Ca2+ Signaling

TL;DR: This review focuses on three major tasks of TRP channels: the function of TRp channels as Ca2+ entry channels; the electrogenic actions of TRPs; and (3) TRPs asCa2+ release channels in intracellular organelles.
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Role of Ion Channels and Transporters in Cell Migration

TL;DR: After presenting general principles by which transport proteins affect cell migration, the role of channels and transporters involved in cell migration is discussed systematically.
Journal ArticleDOI

Renal autoregulation in health and disease.

TL;DR: A combination of vascular and tubular mechanisms, novel to the kidney, provides for high autoregulatory efficiency that maintains RBF and GFR, stabilizes sodium excretion, and buffers transmission of RPP to sensitive glomerular capillaries, thereby protecting against hypertensive barotrauma.
References
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Journal ArticleDOI

Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol.

TL;DR: The molecular mechanism of store-depletion-independent activation of a subfamily of mammalian TRPC channels is described and it is found that hTRPC6 is a non-selective cation channel that is activated by diacylglycerol in a membrane-delimited fashion, independently of protein kinases C activated bydiacyl Glycerol.
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Stretch-activated single ion channel currents in tissue-cultured embryonic chick skeletal muscle.

TL;DR: The membrane of tissue‐cultured chick pectoral muscle contains an ionic channel which is activated by membrane stretch, and appears to gather force from a large area of membrane, probably by a cytochalasin‐resistant cytoskeletal network.
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TRPC1 and TRPC5 form a novel cation channel in mammalian brain.

TL;DR: It is demonstrated here that TRPC1 and TRPC5 are subunits of a heteromeric neuronal channel, and proposed that many TRPC heteromers form diverse receptor-regulated nonselective cation channels in the mammalian brain.
Journal ArticleDOI

Subunit composition of mammalian transient receptor potential channels in living cells

TL;DR: This work investigates the combinatorial rules of TRPC assembly by pursuing four independent experimental approaches and shows that TRPC2 does not interact with any known TRPC protein andTRPC1 has the ability to form channel complexes together with TRPC4 and TRPC5.
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