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a Department of Biochemistry and Molecular Biology, University of Texas Medical School at Houston, Houston, Texas 77030
Capacitative Ca2+ entry plays a role in thapsigargin- and oxytocin-mediated increases in intracellular free Ca2+ in human myometrium. Members of the Trp protein family have been implicated in capacitative Ca2+ entry in a number of tissues. Pregnant human myometrium and the human myometrial cell line PHM1-41 expressed mRNA for hTrp1, hTrp3, hTrp4, hTrp6, and hTrp7. A number of known splice variants of hTrp1 and hTrp4 were expressed in these cells. In addition, novel splice variants for hTrp1 and hTrp3 were discovered. hTrp1
1 and hTrp1
2 contain insertions between previously described exons 9 and 10 that would alter reading frame and produce Trp proteins truncated in the membrane spanning region if expressed. The hTrp3 variant introduces sequence between exons 8 and 9 that would insert 16 amino acids in the C-terminal region of the protein upstream of the calmodulin and inositol 1,4,5-triphosphate receptor interaction domain. hTrp1, hTrp3, and hTrp4 proteins were detected in both pregnant human myometrial and PHM1-41 membranes; a weak band consistent with hTrp6 expression was detected in pregnant human myometrium. These data are consistent with the presence of proteins that could form putative capacitative Ca2+ channels in human myometrium. Control of the activity of these channels may be important for the control of uterine contractile activity.
1 This work was supported in part by NIH-HD09618, NIH-HD38970, and Lalor Foundation Fellowships (M.Y. and A.G.).
2 Correspondence: Barbara M. Sanborn, Department of Biochemistry and Molecular Biology, University of Texas Medical School, P.O. Box 20708, Houston, TX 77225. FAX: 713 500 0652; barbara.m.sanborn{at}uth.tmc.edu
3 Current address: Lexicon Genetics, 4000 Research Forest Dr., The Woodlands, TX 77381
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