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-induced TRPC1 expression amplifies store-operated Ca2+ influx and endothelial permeability
1 Department of Pharmacology, University of Illinois, Chicago, IL, USA
* To whom correspondence should be addressed. E-mail: tiruc{at}uic.edu.
We determined the effects of TNF-
on the expression of TRPC homologues in human vascular endothelial cells and the consequences of TRPC expression on the
endothelial permeability response. We observed that TNF- exposure increased TRPC1 expression without significantly altering expression of other TRPC isoforms in human pulmonary artery endothelial cells (HPAEC). Because TRPC1 belongs to the storeoperated cation channel family, we measured the Ca2+ store depletion-mediated Ca2+ influx in response to thrombin exposure. We observed that thrombin-induced Ca2+ influx
in TNF--stimulated HPAEC was 2-fold greater than in control cells. To address the relationship between store-operated Ca2+ influx and TRPC1 expression, we
overexpressed TRPC1 by 3- to 4-fold in human dermal microvascular endothelial cell line (HMEC) using the TRPC1cDNA. Thrombin-induced store Ca2+ depletion in these cells caused ~2-fold greater increase in Ca2+ influx than in control cells. Further, the IP3- sensitive store-operated cationic current was increased greater than 2-fold in TRPC1- transfected cells compared to control. To address the role of Ca2+ influx via TRPC1 in signaling endothelial permeability, we measured actin-stress fiber formation and transendothelial monolayer electrical resistance (TER) in the TRPC1cDNA-transfected HMEC and TNF--challenged HPAEC. Both thrombin-induced actin-stress fiber formation and decrease in TER were augmented in TRPC1-overexpressing HMEC
compared to control cells. TNF--induced increased TRPC1 expression in HPAEC also resulted in marked endothelial barrier dysfunction in response to thrombin. These findings indicate the expression level of TRPC1 in endothelial cells is a critical determinant of Ca2+ influx and signaling of the increase in endothelial permeability.
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