Transient receptor potential (Trp) channels have been implicated in mediating store- and receptor-activated Ca2 influx. Different properties of this influx in various cell types may stem from the assembly of these Trp proteins into homo- or heterotetramers or association with other regulatory proteins. We examined the properties of endogenous capacitative Ca2 entry in PHM1 immortalized human myometrial cells that express endogenous hTrpCs 1, 3, 4, 6, and 7 mRNA and in primary human myocytes. In PHM1 cells, activation of the oxytocin receptor or depletion of intracellular Ca2 stores with the endoplasmic reticulum calcium pump-inhibitor thapsigargin induced capacitative Ca2 entry, which was inhibited both by SKF 96365 and gadolinium (Gd3 ). Whereas unstimulated cells did not exhibit Sr2 entry, oxytocin and thapsigargin enhanced Sr2 entry that was also inhibited by SKF 96365 and Gd3 . In contrast, Ba2 , a poor substrate for Ca2 pumps, accumulated in these cells in the absence of the capacitative entry stimulus and also after oxytocin and thapsigargin treatment. Both types of entry were markedly decreased by SKF 96365 and Gd3 . The membrane-permeant derivative of diacylglycerol, 1-oleoyl-2-acetyl-sn-glycerol (OAG), elicited oscillatory increases in PHM1 intracellular Ca2 that were dependent on extracellular Ca2 . These properties were also observed in primary human myocytes. Overexpression of hTrpC3 in PHM1 cells enhanced thapsigargin-, oxytocin-, and OAG-induced Ca2 entry. These data are consistent with the expression of endogenous hTrpC activity in myometrium. Capacitative Ca2 entry can potentially contribute to Ca2 dynamics controlling uterine smooth muscle contractile activity.
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