References
Ali, H., Christensen, S.B., Foreman, J.C., Pearce, F.L., Piotrowski, W., Thastrup, O. 1985. The ability of thapsigargin and thapsigargicin to activate cells involved in the inflammatory response. Br. J. Pharmacol. 85:705–712
Berridge, M.J. 1993. Inositol trisphospate and calcium signalling. Nature 361:315–325
Bird, G.S., Rossier, M.F., Hughes, A.R., Shears, S.B., Armstrong, D.L., Putney, J.W. 1991. Activation of Ca2+ entry into acinar cells by a non-phosphorylatable inositol trisphosphate. Nature 352:162–165
Brandi, C.J., Green, N.M., Korczak, B., MacLennan, D.H. 1986. Two Ca2+-ATPase genes: homologies and mechanistic implications of deduced amino acid sequences. Cell 44:597–607
Burk, S.E., Lytton, J., MacLennan, D.H., Shull, G.E. 1989. cDNA cloning, functional expression, and mRNA tissue distribution of a third organellar Ca2+ pump. J. Biol. Chem. 264:18561–18568
Campbell, A.M., Kessler, P.D., Sagara, Y., Inesi, G., Fambrough, D.M. 1991. Nucleotide sequences of avian cardiac and brain SR/ER Ca2+-ATPases and functional comparisons with fast twitch Ca2+-ATPase. Calcium affinities and inhibitor effects. J. Biol. Chem. 266:16050–16055
Carafoli, E. 1987. Intracellular calcium homeostasis. Annu. Rev. Biochem. 56:395–433
Christensen, S.B. 1988. Interpretation of the NMR and circular dichroic data of the sesquiterpene lactone thapsigargin. Acta Chemica Scandinavica B42:623–628
Christensen, S.B., Andersen, A., Poulsen, J.-C.J., Treiman, M. 1993. Derivatives of thapsigargin as probes of its binding site on endoplasmic reticulum Ca2+ ATPase: Stereoselectivity and important functional groups. FEBS Lett. 335:345–348
Christensen, S.B., Larsen, I.K., Rasmussen, U. 1982. Thapsigargin and thapsigargicin, two histamine liberating sesquiterpene lactones from Thapsia garganica. X-ray analysis of the 7,11-epoxide of thapsigargin. J. Org. Chem. 47:649–652
Clementi, E., Scheer, H., Zacchetti, D., Fasolato, C., Pozzan, T., Meldolesi, J. 1992. Receptor-activated Ca2+ influx. Two independently regulated mechanisms of influx stimulation coexist in neurosecretory PC12 cells. J. Biol. Chem. 267(4):2164–2172
Ebashi, S., Lippman, F. 1962. Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle. J. Cell Biol. 14:389–400
Ghosh, T.K., Bian, J., Short, A.D., Rybak, S.L., Gill, D.L. 1991. Persistent intracellular calcium pool depletion by thapsigargin and its influence on cell growth. J. Biol. Chem. 266:24690–24697
Gill, D.L., Ghosh, T.K., Bian, J., Short, A.D., Waldron, R.T., Rybak, S.L. 1992. Function and organization of the inositol-1,4,5-triphosphate-sensitive pools. Adv. Second Mess. and Phosphoprot. Res. 26:265–308
Goeger, D.E., Riley, R.T., Dorner, J.W. 1988. Cyclopiazonic acid inhibition of the Ca2+-transport ATPase in rat skeletal muscle sarcoplasmic reticulum vesicles. Biochem. Pharmacol. 37(5):978–981
Gunteski-Hamblin, A.-M., Greeb, J., Shull, G.E. 1988. A novel Ca2+ pump expressed in brain, kidney, and stomach is encoded by an alternative transcript of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene. Identification of cDNAs encoding Ca2+ and other cation-transporting ATPases using an oligonucleotide probe derived from the ATP-binding site. J. Biol. Chem. 263: 15032–15040
Gutheil, J.C., Hart, S.R., Belani, C.P., Melera, P.W., Hussain, A. 1994. Alterations in Ca2+ transport ATPase and p-glycoprotein expression can mediate resistance to thapsigargin. J. Biol. Chem. (in press)
Hasselbach, W., Makinose, M. 1961. Die Calciumpumpe der “Erschlaffungsgrana” des Muskels and ihre Abhangigkeit von der ATP-spaltung. Biochem. Z. 333:518–528
Holzapfel, C.W. 1968. The isolation and structure of cyclopiazonic acid, a toxic metabolite of penicillium cyclopium westling. Tetrahedron 24(5):2101–2119
Hoth, M., Penner, R. 1992. Depletion of intracellular calcium stores activates a calcium current in mast cells. Nature 355:353–356
Inesi, G., Sumbilla, C., Kirtley, M.E. 1990. Relationships of molecular structure and function in the Ca2+ transport ATPase. Physiol. Rev. 70:749–760
Jackson, T.R., Patterson, S.I., Thastrup, O., Hanley, M.R. 1988. A novel tumour promoter, thapsigargin, transiently increases cytoplasmic free Ca2+ without generation of inositol phosphates in NG115–401L neuronal cells. Biochem. J. 253:81–86
Kass, G.E.N., Duddy, S.K., Moore, G.A., Orrenius, S. 1989. 2,5Di(tert-butyl)-1,4-benzohydroquinone rapidly elevates cytosolic Ca2+ concentration by mobilizing the inositol 1,4,5-triphosphatesensitive Ca2+ pool. J. Biol. Chem. 264:15192–15198
Kijima, Y., Ogunbunmi, E., Fleischer, S. 1991. Drug action of thapsigargin on the Ca2+ pump protein of sarcoplasmic reticulum. J. Biol. Chem. 266:22912–22918
Kirby, M.S., Sagara, Y., Gaa, S.T., Inesi, G., Lederer, W.J., Rogers, T.B. 1992. Thapsigargin inhibits contraction and Ca2+ transient in cardiac cells by specific inhibition of the sarcoplasmic reticulum Ca2+ pump. J. Biol. Chem. 267(18):12545–12551
Lytton, J., Westlin, M., Burk, S.E., Shull, G.E., MacLennan, D.H. 1992. Functional comparisons between isoforms of the sarcoplasmic or endoplasmic reticulum family of calcium pumps. J. Biol. Chem. 267:14483–14489
Lytton, J., Westlin, M., Hanley, M.R. 1991. Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps. J. Biol. Chem. 266:17067–17071
Lytton, J., Zarain-Herzberg, A., Periasamy, M., MacLennan, D.H. 1989. Molecular cloning of the mammalian smooth muscle sarco(endo)plasmic reticulum Ca2+-ATPases. J. Biol. Chem. 264:7059–7065
MacLennan, D.H., Brandl, C.J., Korczak, B., Green, N.M. 1985. Amino-acid sequence of a Ca2+ + Mg2+ dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 316:696–700
Moore, G.A., McConkey, D.J., Kass, G.E., O'Brien, P.J., Orrenius, S. 1987. 2,5-di(tert-butyl)-1,4-benzohydroquinone—a novel inhibitor of liver microsomal Ca2+ sequestration. FEBS Lett. 224(2): 331–336
Murphy, S.J., Schroeder, R.E., Blacker, A.M., Krasavage, W.J., English, J.C. 1992. A study of developmental toxicity of hydroquinone in the rabbit. Fund. App. Toxicol 19(2):214–221
Parekh, A.B., Terlau, H., Stühmer, W. 1993. Depletion of InsP3 stores activates a Ca2+ and K+ current by means of a phosphatase and a diffusible messenger. Nature 364:814–818
Putney, J.W. 1993. Excitement about calcium signaling in inexcitable cells. Science 262:676–678
Randriamampita, C., Tsien, R.Y. 1993. Emptying of intracellular Ca2+ stores releases a novel small messenger that stimulates Ca2+ influx. Science 364:809–814
Rasmussen, U., Christensen, S.B., Sandberg, F. 1978. Thapsigargin and thapsigargicin, two new histamine liberators from Thapsiagarganica. Acta Pharmaceut. Suec. 15:133–140
Robinson, I.M., Cheek, T.R., Burgoyne, R.D. 1992. Ca2+ influx induced by the Ca2+-ATPase inhibitors 2,5-di-(t-butyl)-1,4-benzohydroquinone and thapsigargin in bovine adrenal chromaffin cells. Biochem. J. 288:457–463
Rossier, M.F., Putney, J.W. 1991. The identity of the calcium-storing, inositol 1,4,5-triphosphate-sensitive organelle in non-muscle cells: calciosome, endoplasmic reticulum ... or both? TINS 14(7): 310–314
Sagara, Y., Fernandez-Belda, F., De Meis, L., Inesi, G. 1992a. Characterization of the inhibition of intracellular Ca2+ transport ATPases by thapsigargin. J. Biol. Chem. 267:12606–12613
Sagara Y., Inesi, G. 1991. Inhibition of the sarcoplasmic reticulum Ca2+ transport ATPase by thapsigargin at subnanomolar concentrations. J. Biol. Chem. 266:13503–13506
Sagara, Y., Wade, J.B., Inesi, G. 1992b. A conformational mechanism for formation of a dead-end complex by the sarcoplasmic reticulum ATPase with thapsigargin. J. Biol. Chem. 267:1286–1292
Scharff, O., Foder, B., Thastrup, O., Hofman, B., Miler, J., Ryder, L.P., Jacobsen, K.D., Langhoff, E., Dickweiss, E., Christensen, S.B. 1988. Effect of thapsigargin on cytoplasmic Ca2+ and proliferation of human lymphocytes in relation to AIDS. Biochim. Biophys. Acta 972:257–264
Schönthal, A., Sugarman, J., Brown, J.H., Hanley, M.R., Feramisco, J.R. 1991. Regulation of c-fos and c-jun protooncogene expression by the Ca2+-ATPase inhibitor thapsigargin. Proc. Natl. Acad. Sci. USA 88:7096–7100
Seidler, N.W., Jona, L, Vegh, M., Martonosi, A. 1989. Cyclopiazonic acid is a specific inhibitor of the Ca2+-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 264:17816–17823
Short, A.D., Bian, J., Ghosh, T.K., Waldron, R.T., Rybak, S.L., Gill, D.L. 1993. Intracellular Ca2+ pool content is linked to control of cell growth. Proc. Natl. Acad. Sci. USA 90:4986–4990
Sumbilla, C., Lu, L., Inesi, G., Ishii, T., Takeyasu, K., Fang, Y., Fambrough, D.M. 1993. Ca2+ dependent and thapsigargin-inhibited phosphorylation of Na+,K+-ATPases catalytic domain following chimeric recombination with the Ca2+-ATPase. J. Biol. Chem. 268:21185–21192
Takemura, H., Hughes, A.R., Thastrup, O., Putney, J.W., Jr. 1989. Activation of calcium enty by the tumor promoter thapsigargin in parotid acinar cells. J. Biol. Chem. 264:12266–12271
Takishima, K., Friedman, B., Fujiki, H., Rosner, M.R. 1988. Thapsigargin, a novel promoter, phosphorylates the epidermal growth factor receptor at threonine 669. Biochem. Biophys. Res. Commun. 157(2):740–746
Tao, J., Haynes D.H. 1992. Actions of thapsigargin on the Ca2+ handling systems of the human platelet. J. Biol. Chem. 267:24972–24982
Thastrup, O., Cullen, P.J., Drobak, B.K., Hanley, M.R., Dawson, A.P. 1990. Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 87:2466–2470
Thastrup, O., Foder, B., Scharff, O. 1987a. The calcium mobilizing and tumour promoting agent, thapsigargin, elevates the platelet cytoplasmic free calcium concentration to a higher steady state level. A possible mechanism of action for the tumour promotion. Biochem. Biophys. Res. Commun. 142:654–660
Thastrup, O., Linnebjerg, P.J., Bjerrum, P.J., Knudson, C.M., Christensen, S.B. 1987b. The inflammatory, tumor-promoting sesquiterpene lactone thapsigargin activates platelets by selective mobilization of calcium as shown by protein phosphorylation. Biochim. Biophys. Acta. 927:65–73
Wictome, M., Michelangeli, F., Lee, A.G., East, J.M. 1992. The inhibitors thapsigargin and 2,5-di(tert-butyl)-1,4-benzohydroquinone favour the E2 form of the Ca2+, Mg2+-ATPases. FEBS Lett. 304:109–113
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Support from the National Institutes of Health and the American Heart Association is gratefully acknowledged.
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Inesi, G., Sagara, Y. Specific inhibitors of intracellular Ca2+ transport ATPases. J. Membarin Biol. 141, 1–6 (1994). https://doi.org/10.1007/BF00232868
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DOI: https://doi.org/10.1007/BF00232868