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Originally published In Press as doi:10.1074/jbc.M205541200 on July 11, 2002

J. Biol. Chem., Vol. 277, Issue 37, 34375-34382, September 13, 2002
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Erythropoietin Modulates Calcium Influx through TRPC2*

Xin ChuDagger , Joseph Y. CheungDagger §, Dwayne L. Barber||, Lutz Birnbaumer**, Lawrence I. RothblumDagger , Kathleen ConradDagger , Virginia AbrasonisDagger , Yiu-mo ChanDagger , Richard StahlDagger , David J. CareyDagger , and Barbara A. MillerDagger Dagger Dagger §§

From Dagger  The Henry Hood Research Program, The Sigfried and Janet Weis Center for Research, and the Departments of § Medicine and Dagger Dagger  Pediatrics, the Geisinger Clinic, Danville, Pennsylvania 17822, the  Division of Cellular and Molecular Biology, Ontario Cancer Institute, Toronto, Ontario M5G 2M9, Canada, and the ** Division of Intramural Research, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709

Mammalian isoforms of calcium-permeable Drosophila transient receptor potential channels (TRPC) are involved in the sustained phase of calcium entry in nonexcitable cells. Erythropoietin (Epo) stimulates a rise in intracellular calcium ([Ca]i) via activation of voltage-independent calcium channel(s) in erythroid cells. Here, involvement of murine orthologs of classical TRPC in the Epo-modulated increase in [Ca]i was examined. RT-PCR of TRPC 1-6 revealed high expression of only TRPC2 in Epo-dependent cell lines HCD-57 and Ba/F3 Epo-R, in which Epo stimulates a rise in [Ca]i. Using RT-PCR, Western blotting, and immunolocalization, expression of the longest isoform of mTRPC2, clone 14, was demonstrated in HCD-57 cells, Ba/F3 Epo-R cells, and primary murine erythroblasts. To determine whether erythropoietin is capable of modulating calcium influx through TRPC2, CHO cells were cotransfected with Epo-R subcloned into pTracer-CMV and either murine TRPC2 clone 14 or TRPC6, a negative control, into pQBI50. Successful transfection of Epo-R was verified in single cells by detection of green fluorescent protein from pTracer-CMV using digital video imaging, and successful transfection of TRPC was confirmed by detection of blue fluorescent protein fused through a flexible linker to TRPC. [Ca]i changes were simultaneously monitored in cells loaded with Rhod-2 or Fura Red. Epo stimulation of CHO cells cotransfected with Epo-R and TRPC2 resulted in a rise in [Ca]i above base line (372 ± 71%), which was significantly greater (p <=  0.0007) than that seen in cells transfected with TRPC6 or empty pQBI50 vector. This rise in [Ca]i required Epo and extracellular calcium. These results identify a calcium-permeable channel, TRPC2, in erythroid cells and demonstrate modulation of calcium influx through this channel by erythropoietin.

* This work was supported by National Institutes of Health Grants DK 46778 (to B. A. M), HL 58672 (to J. Y. C.), GM 46991 (to L. I. R.), and NS 21925, NS 37716, and NS 41363 (to D. J. C.) and grants from the Geisinger Foundation (to B. A. M., J. Y. C., L. I. R., Y. C., and D. J. C.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| Research Scientist of the National Cancer Institute of Canada.

§§ To whom correspondence should be addressed: The Henry Hood Research Program, The Sigfried and Janet Weis Center for Research, Geisinger Clinic, 100 N. Academy Ave., Danville, PA 17822-2616. Tel.: 570-271-6675; Fax: 570-271-6701; E-Mail: bamiller1{at}geisinger.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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