October 16, 1998FEBS Letters
Trp proteins form store‐operated cation channels in human vascular endothelial cells
Key result
Dominant negative hTrp3 fragment abolishes store-operated cation currents, indicating Trp proteins form these endothelial channels.
Why the study?
The structural basis of store-operated cation conductances in human vascular endothelial cells involving Trp proteins was not fully established.
Population
Human umbilical vein endothelial cells (HUVEC)
Comparison
N-TRP transfection vs hTrp3 transfection vs sham-transfected HUVEC
Design
Preclinical experimental study with transfection and electrophysiological assessment
Authors
Discussion
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Member takes
Implication
Trp proteins may form endothelial store-operated channels; hypothesis-generating and should not change clinical practice.
Structured PICO
P
Population
Human umbilical vein endothelial cells (HUVEC)
I
Intervention
Transfection with an N-terminal fragment of hTrp3 (N-TRP) or hTrp3, followed by depletion of intracellular Ca2+ stores with IP3 (100 microM) or thapsigargin (100 nM)
C
Comparator
Sham-transfected HUVEC
O
Outcome
Store-operated cation conductance/currentssurrogate
Trp related proteins are involved in the store-operated cation conductance of human vascular endothelial cells.
Cite This Study
Groschner et al. (1998) studied this question. Expression of an N-terminal fragment of hTrp3 (N-TRP) vs. Sham-transfected HUVEC and hTrp3-transfected HUVEC was evaluated on Store-operated cation conductance upon depletion of intracellular Ca2+ stores. Expression of a dominant negative N-terminal fragment of hTrp3 in human vascular endothelial cells abolished store-operated cation currents, indicating Trp proteins form these channels.