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1 Division of Pulmonary and Critical Care Medicine, Department of Medicine, University of California, San Diego, San Diego, CA, USA
* To whom correspondence should be addressed. E-mail: xiyuan{at}ucsd.edu.
Transient receptor potential (TRP) cation channels are a critical pathway for Ca2+ entry during pulmonary artery (PA) smooth muscle contraction. However, whether canonical TRP subunits and which TRP channel isoforms are involved in store depletion-induced pulmonary vasoconstriction in vivo remains unclear. This study was designed to test whether overexpression of the human TRPC1 gene (hTRPC1) in rat PA enhances pulmonary vasoconstriction due to store depletion-mediated Ca2+ influx. The hTRPC1 was infected into rat PA rings with an adenoviral vector. RT-PCR and Western blot analyses confirmed the mRNA and protein expression of hTRPC1 in the arterial rings. The amplitude of active tension induced by 40 mM K+ (40K) in PA rings infected with an empty adenoviral vector (647±88 mg/mg) was similar to that in PA rings infected with hTRPC1 (703±123 mg/mg; P=0.3). However, the active tension due to capacitative Ca2+ entry (CCE) induced by cyclopiazonic acid, was significantly enhanced in PA rings overexpressing hTRPC1 (91±13% of 40K-induced contraction) compared to rings infected with an empty adenoviral vector (61±14%; P<0.001). Endothelial expression of hTRPC1 was not involved since the CCE-induced vasoconstriction was also enhanced in endothelium-denuded PA rings infected with the adenoviral vector carrying hTRPC1. These observations demonstrate that human TRPC1 is an important Ca2+-permeable channel that mediates pulmonary vasoconstriction when PA smooth muscle cell intracellular Ca2+ stores are depleted.
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