Dominant role of Orai1 with STIM1 on the cytosolic entry and cytotoxicity of lead ions

Toxicological Sciences

Volumn 110, Issue 2, 2009, Pages 353-362

  Chiu, Tai Yu ^a,b   Teng, Hsiao Chuan ^a   Huang, Ping Chun ^a,b   Kao, Fu Jen ^b   Yang, De Ming ^a,b  

^a TAIPEI VETERANS GENERAL HOSPITAL   (Taiwan)

^b NATIONAL YANG MING UNIVERSITY   (Taiwan)

Author keywords

Fluorescence lifetime imaging; HEK293 cells; Indo 1; Orai1; Pb2+; STIM1; Store operated Ca2+ channels

Indexed keywords

CALCIUM CHANNEL; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL 1; LEAD; MEMBRANE PROTEIN; STROMAL INTERACTING PROTEIN 1; UNCLASSIFIED DRUG;

ARTICLE; CALCIUM TRANSPORT; CELL STRAIN HEK293; CELL TRANSPORT; CELL VIABILITY; CONTROLLED STUDY; CYTOTOXICITY; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; ION TRANSPORT; MUTATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION;

ANIMALS; BIOLOGICAL TRANSPORT; BLOTTING, WESTERN; CALCIUM; CALCIUM CHANNELS; CELL PROLIFERATION; CELL SEPARATION; CELL SURVIVAL; CYTOSOL; ENDOPLASMIC RETICULUM; ENZYME INHIBITORS; FLOW CYTOMETRY; HUMANS; LEAD; MEMBRANE PROTEINS; MICROSCOPY, CONFOCAL; MICROSCOPY, FLUORESCENCE; MUTATION; NEOPLASM PROTEINS; PC12 CELLS; RATS; RECOMBINANT FUSION PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES; SPECTROPHOTOMETRY, ATOMIC; THAPSIGARGIN; TIME FACTORS; TRANSFECTION;

EID: 67650723485     PISSN: 10966080     EISSN: 10960929     Source Type: Journal    
DOI: 10.1093/toxsci/kfp099     Document Type: Article

References (40)

1. Alicia, S., Anǵelica, Z., Carlos, S., Alfonso, S., and Luis, V. (2008). STIM1 converts TRPC1 form a receptor-operated to a store-operated channel: Moving TRPC1 in and out of lipid rafts. Cell Calcium. doi:10.1016/j.ceca.2008.03.001
2. Ambudkar, I. S., Ong, H. L., Liu, X., Bandyopadhyay, B. C., and Cheng, K. T. (2007). TRPC1: The link between functionally distinct store-operated calcium channels. Cell Calcium 42, 213-223.
3. Bridges, C. C., and Zalups, R. K. (2005). Molecular and ionic mimicry and the transport of toxic metals. Toxicol. Appl. Pharmacol. 204, 274-308.
4. Burtis, C. A., and Ashwood, E. R. (1999). Tietz Textbook of Clinical Chemistry, 3rd ed. WB Saunders, Philadelphia, PA.
5. 2+ entry in living cells. Toxicol. Appl. Pharmacol. 227 430-439.
6. Chen, C. T., and Huang, W. P. (2002). A highly selective fluorescent chemosensor for lead ions. J. Am. Chem. Soc. 124, 6246-6247.
7. Chen, Y., Mills, J. D., and Periasamy, A. (2003). Protein localization in living cells and tissues using FRET and FLIM. Differentiation 71, 528-541.
8. Cheng, K. T., Liu, X., Ong, H. L., and Ambudkar, I. S. (2008). Functional requirement for Orai1 in store-operated TRPC1-STIM1 channels. J. Biol. Chem. 283, 12935-12940.
9. Feske, S., Gwack, Y., Prakriya, M., Srikanth, S., Puppel, S. H., Tanasa, B., Hogan, P. G., Lewis, R. S., Daly, M., and Rao, A. (2006). A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function. Nature 441, 179-184.
10. Garza, A., Vega, R., and Soto, E. (2006). Cellular mechanisms of lead neurotoxicity. Med. Sci. Monit. 12, RA57-RA65.
11. Godwin, H. A. (2001). The biological chemistry of lead. Curr. Opin. Chem. Biol. 5, 223-227.
12. Gwack, Y., Srikanth, S., Feske, S., Cruz-Guilloty, F., Oh-hora, M., Neems, D. S., Hogan, P. G., and Rao, A. (2007). Biochemical and functional characterization of Orai proteins. J. Biol. Chem. 282, 16232-16243.
13. Järup, L. (2003). Hazards of heavy metal contamination. Br. Med. Bull. 68, 167-182.
14. Kerper, L. E., and Hinkle, P. M. (1997a). Cellular uptake of lead is activated by depletion of intracellular calcium stores. J. Biol. Chem. 272, 8346-8352.
15. Kerper, L. E., and Hinkle, P. M. (1997b). Lead uptake in brain capillary endothelial cells: Activation by calcium store depletion. Toxicol. Appl. Pharmacol. 146, 127-133.
16. Lee, J. D., Chang, Y. F., Kao, F.-J., Kao, L. S., Lin, C. C., Lu, A. C., Shyyu, B.-C., Chiou, S.-H., and Yang, D.-M. (2008a). Detection of the interaction between SNAP25 and rabphilin in neuroendocrine PC12 cells using the FLIM/FRET technique. Microsc. Res. Technol. 71, 26-34.
17. Lee, J. D., Huang, P. C., Lin, Y. C., Kao, L. S., Huang, C. C. Kao, F. J., Lin, C. C., and Yang, D.-M. (2008b). In-depth fluorescence lifetime imaging analysis revealing SNAP25A-rabphilin 3A interactions. Microsc. Microanal. 14, 507-518.
18. 2+ channel activation. J. Biol. Chem. 282, 29448-29456.
19. Liao, Y., Erxleben, C., Abramowitz, J., Flockerzi, V., Zhu, M. X., Armstrong, D. L., and Birnbaumer, L. (2008). Functional interactions among Orai1, TRPCs, and STIM1 suggest a STIM-regulated heteromeric Orai/ TRPC model for SOCE/Icrac channels. Proc. Nat. Acad. Sci. U. S. A. 105, 2895-2900.
20. Liao, Y., Erxleben, C., Yildirim, E., Abramowitz, J., Armstrong, D. L., and Birnbaumer, L. (2007). Orai proteins interact with TRPC channels and confer responsiveness to store depletion. Proc. Nat. Acad. Sci. U. S. A. 104, 4682-4687.
21. 2+ channels with distinct functional properties. Curr. Biol. 17, 794-800.
22. 2+ entry: Local activation of CRAC channels by STIM1 at ER-plasma membrane junctions. J. Cell Biol. 174, 815-825.
23. 2+ and degranulation in a rat mast cell line. J. Immun. 180, 2233-2239.
24. Muik, M., Frischauf, I., Derler, I., Fahrner, M., Bergsmann, J., Eder, P., Schindl, R., Hesch, C., Polzinger, B., Fritsch, R., et al. (2008). Dynamic coupling of the putative coiled-coil domain of ORAI1 with STIM1 mediates ORAI1 channel activation. J. Biol. Chem. 283, 8014-8022.
25. Ong, H. L., Cheng, K. T., Liu, X., Bandyopadhyay, B. C., Paria, B. C., Soboloff, J., Pani, B., Gwack, Y., Srikanth, S., Singh, B. B., et al. (2007). Dynamic assembly of TRPC1-STIM1-Orai1 ternary complex is involved in store-operated calcium influx. Evidence for similarities in store-operated and calcium release-activated calcium channel components. J. Biol. Chem. 282, 9105-9116.
26. Palmer, A. E., and Tsien, R. Y. (2006). Measuring calcium signaling using genetically targetable fluorescent indicators. Nat. Protoc. 1, 1057-1065.
27. Parekh, A. B., and Putney, J. W. (2005). Store-operated calcium channels. Physiol. Rev. 85, 757-810.
28. Peter, M., Ameer-Beg, S. M., Hughes, M. K. Y., Keppler, M. D., Prag, S., Marsh, M., Vojnovic, B., and Ng, T. (2005). Multiphoton-FLIM quantification of the EGFP-mRFP1 FRET pair for localization of membrane receptor-kinase interactions. Biophys. J. 88, 1224-1237.
29. Prakriya, M., Feske, S., Gwack, Y., Srikanth, S., Rao, A., and Hogan, P.G. (2006). Orai1 is an essential pore subunit of the CRAC channel. Nature 443, 230-233.
30. 2+ entry. J. Cell. Sci. 120, 1959-1965.
31. Shih, R. A., Hu, H., Weisskopf, M. G., and Schwartz, B. S. (2007). Cumulative lead dose and cognitive function in adults: A review of studies that measured both blood lead and bone lead. Environ. Health Perspect. 115, 483-492.
32. Soblic, I. (2006). Common mechanisms in nephropathy induced by toxic metals. Nephron. Physiol. 104, 107-114.
33. Suzkiw, J. B. (2004). Presynaptic distribution of transmitter release by lead. Neurotoxicology 25, 599-604.
34. Vig, M., Beck, A., Billingsley, J. M., Lis, A., Parves, S., Peinelt, C., Koomoa, D. L., Soboloff, J., Gill, D. L., Fleig, A., et al. (2006). CRACM1 multimers form the ion-selective pore of the CRAC channel. Curr. Biol. 16, 2073-2079.
35. Vogel, S. S., Thaler, C., and Koushik, S. V. (2006). Fathful FRET. Science 331, re2.
36. Warren, M. J., Cooper, J. B., Wood, S. P., and Shoolingin-Jordan, P. M. (1998). Lead poisoning, haem synthesis and 5-aminolaevulinic acid dehydratase. Trends Biochem. Sci. 23, 217-221.
37. Wedel, B., Boyles, R. R., Putney, J. W., Jr., and Bird, G. S. (2007). Role of the store-operated calcium entry proteins Stim1 and Orai1 in muscarinic cholinergic receptor-stimulated calcium oscillations in human embryonic kidney cells. J. Physiol. 579, 679-689.
38. 2+ store depletion. Am. J. Physiol. Cell Physiol. 294, 1323-1331.
39. 2+ signaling of human thyroid carcinoma cell lines. Anticancer Res. 24, 1617-1624.
40. Yang, D. M., Huang, C. C., Lin, H. Y., Tsai, D. P., Kao, L. S., Chi, C. W., and Lin, C. C. (2003). Tracking of secretory vesicles of PC12 cells using total internal reflection fluorescence microscopy. J. Microsc. 209, 223-227.