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Trp proteins form store‐operated cation channels in human vascular endothelial cells
Author(s) -
Groschner Klaus,
Hingel Susanne,
Lintschinger Birgit,
Balzer Monika,
Romanin Christoph,
Zhu Xi,
Schreibmayer Wolfgang
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01212-5
Subject(s) - umbilical vein , transfection , thapsigargin , intracellular , microbiology and biotechnology , chemistry , gene isoform , biophysics , biochemistry , biology , in vitro , gene
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 Ca 2+ stores with IP 3 (100 μM) 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.