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Trp proteins form store‐operated cation channels in human vascular endothelial cells
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 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.
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Cited by
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The TRP Superfamily of Cation Channels
Montell, C. (2005) · Science's STKE · doi:10.1126/stke.2722005re3 · Cited by 989
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Nilius, B., & Droogmans, G. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.4.1415 · Cited by 868
Li, Y., Jia, Y.-C., Cui, K., Li, N., Zheng, Z.-Y., Wang, Y.-Z., & Yuan, X.-B. (2005) · Nature · doi:10.1038/nature03477 · Cited by 450
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Metadata
- Authors
- Groschner, K., Hingel, S., Lintschinger, B., Balzer, M., Romanin, C., Zhu, X., & Schreibmayer, W.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1998-10-16
- Volume
- 437
- Issue
- 1-2
- Pages
- 101-106
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2059674419
- Cited by
- 161
- References
- 0
- FWCI
- 6.29
- Type
- journal article
- Language
- en
- Open access
- closed
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- Groschner, K., Hingel, S., Lintschinger, B., Balzer, M., Romanin, C., Zhu, X., & Schreibmayer, W. (1998). Trp proteins form store‐operated cation channels in human vascular endothelial cells. FEBS Letters. https://doi.org/10.1016/s0014-5793(98)01212-5
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