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, 437 (1-2), 101-6

Trp Proteins Form Store-Operated Cation Channels in Human Vascular Endothelial Cells

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Trp Proteins Form Store-Operated Cation Channels in Human Vascular Endothelial Cells

K Groschner et al. FEBS Lett.

Erratum in

  • FEBS Lett 1999 Jan 8;442(1):122

Abstract

Members of the Trp protein family have been suggested as the structural basis of store-operated cation conductances. With this study, we provide evidence for the expression of three isoforms of Trp (hTrp1, 3 and 4) in human umbilical vein endothelial cells (HUVEC). The role of Trp proteins in store regulation of endothelial membrane conductances was tested by expression of an N-terminal fragment of hTrp3 (N-TRP) which exerts a dominant negative effect on Trp channel function presumably due to suppression of channel assembly. Depletion of intracellular Ca2+ stores with IP3 (100 microM) or thapsigargin (100 nM) induced a substantial cation conductance in sham-transfected HUVEC as well as in HUVEC transfected with hTrp3. In contrast, HUVEC transfected with N-TRP failed to exhibit store-operated currents. Our results suggest the involvement of Trp related proteins in the store-operated cation conductance of human vascular endothelial cells.

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