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Volumn 242, Issue 1, 1998, Pages 328-340

U73122 blocked the cGMP-induced calcium release in sea urchin eggs

Author keywords

ADP ribosyl cyclase; Aminosteroid; CGMP dependent protein kinase; Dithiothreitol; Histone; Thimerosal

Indexed keywords

1 [[6 (3 METHOXYESTRA 1,3,5(10) TRIEN 17BETA YL)AMINO]HEXYL] 1H PYRROLE 2,5 DIONE; CALCIUM CHANNEL; CYCLIC GMP; HISTONE; PHORBOL MYRISTATE; PHOSPHOLIPASE C INHIBITOR; PROTEIN SERINE THREONINE KINASE;

EID: 0031845050     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1998.4070     Document Type: Article
Times cited : (20)

References (80)
  • 1
    • 0000514087 scopus 로고
    • Ionic signaling in sea urchin egg at fertilization
    • (C. B. Metz and A. Monroy, Eds.), Academic Press, San Diego
    • Whitaker, M. J., and Steinhardt, R. A. (1985). Ionic signaling in sea urchin egg at fertilization. In "Biology of Fertilization" (C. B. Metz and A. Monroy, Eds.), Academic Press, San Diego.
    • (1985) Biology of Fertilization
    • Whitaker, M.J.1    Steinhardt, R.A.2
  • 2
    • 0020004853 scopus 로고
    • 2+ influx during fertilization of the sea urchin egg?
    • 2+ influx during fertilization of the sea urchin egg? Dev. Biol. 90, 284-290.
    • (1982) Dev. Biol. , vol.90 , pp. 284-290
    • Schmidt, T.1    Patton, C.2    Epel, D.3
  • 3
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signalling
    • Berridge, M. J., and Irvine, R. F. (1989). Inositol phosphates and cell signalling. Nature 341, 197-205.
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 4
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge, M. J. (1993). Inositol trisphosphate and calcium signalling. Nature 361, 315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 5
    • 0025663498 scopus 로고
    • Multiple stores of calcium are released in the sea urchin egg during fertilization
    • Rakow, T. L., and Shen, S. S. (1990). Multiple stores of calcium are released in the sea urchin egg during fertilization. Proc. Natl. Acad. Sci. USA 87, 9285-9289.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9285-9289
    • Rakow, T.L.1    Shen, S.S.2
  • 6
    • 0026114521 scopus 로고
    • Guanosine 5'-thiotriphosphate may stimulate phosphoinositide messenger production in sea urchin eggs by a different route than the fertilizing sperm
    • Crossley, I., Whalley, T., and Whitaker, M. J. (1991). Guanosine 5'-thiotriphosphate may stimulate phosphoinositide messenger production in sea urchin eggs by a different route than the fertilizing sperm. Cell Regul. 2, 121-133.
    • (1991) Cell Regul. , vol.2 , pp. 121-133
    • Crossley, I.1    Whalley, T.2    Whitaker, M.J.3
  • 8
    • 0028269937 scopus 로고
    • Presence of inositol 1,4,5-triphosphate receptor, calreticulin, and calsequestrin in eggs of sea urchins and Xenopus laevis
    • Parys, J. B., McPherson, S. M., Mathews, L., Cambell, K. P., and Longo, F. J. (1994). Presence of inositol 1,4,5-triphosphate receptor, calreticulin, and calsequestrin in eggs of sea urchins and Xenopus laevis. Dev. Biol. 161, 466-476.
    • (1994) Dev. Biol. , vol.161 , pp. 466-476
    • Parys, J.B.1    McPherson, S.M.2    Mathews, L.3    Cambell, K.P.4    Longo, F.J.5
  • 9
    • 0027926582 scopus 로고
    • A tale of two messengers
    • Berridge, M. J. (1993). A tale of two messengers. Nature 365, 388-389.
    • (1993) Nature , vol.365 , pp. 388-389
    • Berridge, M.J.1
  • 10
    • 0027295646 scopus 로고
    • Calcium mobilization by dual receptors during fertilization of sea urchin eggs
    • Lee, H. C., Aarhus, R., and Walseth, T. F. (1993).Calcium mobilization by dual receptors during fertilization of sea urchin eggs. Science 261, 352-355.
    • (1993) Science , vol.261 , pp. 352-355
    • Lee, H.C.1    Aarhus, R.2    Walseth, T.F.3
  • 11
    • 0027282375 scopus 로고
    • Redundant mechanisms of calcium-induced calcium release underlying calcium waves during fertilization of sea urchin eggs
    • Galione, A., McDougall, A., Busa, W. B., Willmott, N., Gillot, I., and Whitaker, M. J. (1993). Redundant mechanisms of calcium-induced calcium release underlying calcium waves during fertilization of sea urchin eggs. Science 261, 348-352.
    • (1993) Science , vol.261 , pp. 348-352
    • Galione, A.1    McDougall, A.2    Busa, W.B.3    Willmott, N.4    Gillot, I.5    Whitaker, M.J.6
  • 12
    • 0028877531 scopus 로고
    • Mechanisms of calcium regulation in sea urchin eggs and their activities during fertilization
    • Shen, S. S. (1995). Mechanisms of calcium regulation in sea urchin eggs and their activities during fertilization. Curr. Top. Dev. Biol. 30, 63-101.
    • (1995) Curr. Top. Dev. Biol. , vol.30 , pp. 63-101
    • Shen, S.S.1
  • 14
    • 21344491625 scopus 로고
    • A signaling pathway involving cyclic ADP-ribose, cGMP, and nitric oxide
    • Lee, H. C. (1994). A signaling pathway involving cyclic ADP-ribose, cGMP, and nitric oxide. News Physiol. Sci. 9, 134-137.
    • (1994) News Physiol. Sci. , vol.9 , pp. 134-137
    • Lee, H.C.1
  • 15
    • 0030602067 scopus 로고    scopus 로고
    • The cyclic GMP-mediated calcium release pathway in sea urchin eggs is not required for the rise in calcium during fertilization
    • Lee, S. J., Christenson, L., Martin, T., and Shen, S. S. (1996). The cyclic GMP-mediated calcium release pathway in sea urchin eggs is not required for the rise in calcium during fertilization. Dev. Biol. 180, 324-335.
    • (1996) Dev. Biol. , vol.180 , pp. 324-335
    • Lee, S.J.1    Christenson, L.2    Martin, T.3    Shen, S.S.4
  • 17
    • 0028085003 scopus 로고
    • Regulation of intracellular calcium in the mouse egg: Evidence for inositol trisphosphate-induced calcium release, but not calcium-induced calcium release
    • Kline, J. T., and Kline, D. (1994). Regulation of intracellular calcium in the mouse egg: Evidence for inositol trisphosphate-induced calcium release, but not calcium-induced calcium release. Biol. Reprod. 50, 193-203.
    • (1994) Biol. Reprod. , vol.50 , pp. 193-203
    • Kline, J.T.1    Kline, D.2
  • 19
    • 0021286692 scopus 로고
    • Fertilization increases the polyphosphoinositide content of sea urchin eggs
    • Turner, P. R., Sheetz, M. P., and Jaffe, L. A. (1984). Fertilization increases the polyphosphoinositide content of sea urchin eggs. Nature 310, 414-415.
    • (1984) Nature , vol.310 , pp. 414-415
    • Turner, P.R.1    Sheetz, M.P.2    Jaffe, L.A.3
  • 20
    • 0022084646 scopus 로고
    • Phosphatidylinositol metabolism during fertilization in the sea urchin egg
    • Kamel, L. C., Bailey, J., Schoenbaum, L., and Kinsey, W. (1985). Phosphatidylinositol metabolism during fertilization in the sea urchin egg. Lipids 20, 350-356.
    • (1985) Lipids , vol.20 , pp. 350-356
    • Kamel, L.C.1    Bailey, J.2    Schoenbaum, L.3    Kinsey, W.4
  • 21
  • 22
    • 0026751702 scopus 로고
    • Polyphosphoinositide metabolism during the fertilization wave in sea urchin eggs
    • Ciapa, B., Borg, B., and Whitaker, M. J. (1992). Polyphosphoinositide metabolism during the fertilization wave in sea urchin eggs. Development 115, 187-195.
    • (1992) Development , vol.115 , pp. 187-195
    • Ciapa, B.1    Borg, B.2    Whitaker, M.J.3
  • 23
    • 0022490785 scopus 로고
    • Two phases of inositol polyphosphate and diacylglycerol production at fertilization
    • Ciapa, B., and Whitaker, M. J. (1986). Two phases of inositol polyphosphate and diacylglycerol production at fertilization. FEBS Lett. 195, 347-351.
    • (1986) FEBS Lett. , vol.195 , pp. 347-351
    • Ciapa, B.1    Whitaker, M.J.2
  • 24
    • 0032518579 scopus 로고    scopus 로고
    • The calcium transient in sea urchin eggs during fertilization requires the production of inositol 1,4,5-trisphosphate
    • Lee, S.-J., and Shen, S. S. (1998). The calcium transient in sea urchin eggs during fertilization requires the production of inositol 1,4,5-trisphosphate. Dev. Biol. 193, 195-208.
    • (1998) Dev. Biol. , vol.193 , pp. 195-208
    • Lee, S.-J.1    Shen, S.S.2
  • 25
    • 0025201019 scopus 로고
    • Selective inhibition of receptor-coupled phospholipase C-dependent processes in human platelets and polymorphonuclear neutrophiles
    • Bleasdale, J. E., Thakur, N. R., Gremban, R. S., Bundy, G. L., Fitzpatrick, F. A., Smith, R. J., and Bunting, S. (1990). Selective inhibition of receptor-coupled phospholipase C-dependent processes in human platelets and polymorphonuclear neutrophiles. J. Pharmacol. Exp. Ther. 255, 756-768.
    • (1990) J. Pharmacol. Exp. Ther. , vol.255 , pp. 756-768
    • Bleasdale, J.E.1    Thakur, N.R.2    Gremban, R.S.3    Bundy, G.L.4    Fitzpatrick, F.A.5    Smith, R.J.6    Bunting, S.7
  • 26
    • 0026611036 scopus 로고
    • 2+ oscillations in response to cholecystokinin and carbachol but not JMV-180 in rat pancreatic acinar cells
    • 2+ oscillations in response to cholecystokinin and carbachol but not JMV-180 in rat pancreatic acinar cells. J. Biol. Chem. 267, 13830-13835.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13830-13835
    • Yule, D.I.1    Williams, J.A.2
  • 27
    • 0026327816 scopus 로고
    • The aminosteroid U-73122 inhibits muscarinic receptor sequestration and phosphoinositide hydrolysis in SK-N-SH neuroblastoma cells: A role for Gp in receptor compartmentation
    • Thompson, A. K., Mostafapour, S. P., Denlinger, L. C., Bleasdale, J. E., and Fisher, S. K. (1991). The aminosteroid U-73122 inhibits muscarinic receptor sequestration and phosphoinositide hydrolysis in SK-N-SH neuroblastoma cells: A role for Gp in receptor compartmentation. J. Biol. Chem. 266, 23856-23862.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23856-23862
    • Thompson, A.K.1    Mostafapour, S.P.2    Denlinger, L.C.3    Bleasdale, J.E.4    Fisher, S.K.5
  • 28
    • 0028089832 scopus 로고
    • Epidermal growth factor receptor-mediated cell motility: Phospholipase C activity is required, but mitogen-activated protein kinase activity is not sufficient for induced cell movement
    • Chen, P., Xie, H., Sekar, M. C., Gupta, K., and Wells, A. (1994). Epidermal growth factor receptor-mediated cell motility: phospholipase C activity is required, but mitogen-activated protein kinase activity is not sufficient for induced cell movement. J. Cell Biol. 127, 847-857.
    • (1994) J. Cell Biol. , vol.127 , pp. 847-857
    • Chen, P.1    Xie, H.2    Sekar, M.C.3    Gupta, K.4    Wells, A.5
  • 29
    • 0029898360 scopus 로고    scopus 로고
    • Mitogenic signaling from the EGF receptor is attenuated by a phospholipase C-gamma/ protein kinase C feedback mechanism
    • Chen, P., Xie, H., and Wells, A. (1996). Mitogenic signaling from the EGF receptor is attenuated by a phospholipase C-gamma/ protein kinase C feedback mechanism. Mol. Biol. Cell 7, 871-881.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 871-881
    • Chen, P.1    Xie, H.2    Wells, A.3
  • 30
    • 0031037686 scopus 로고    scopus 로고
    • Effects of U73122 and U73343 on human platelet calcium signalling and protein tyrosine phosphorylation
    • Heemskerk, J. W., Farndale, R. W., and Sage, S. O. (1997). Effects of U73122 and U73343 on human platelet calcium signalling and protein tyrosine phosphorylation. Biochim. Biophys. Acta 1355, 81-88.
    • (1997) Biochim. Biophys. Acta , vol.1355 , pp. 81-88
    • Heemskerk, J.W.1    Farndale, R.W.2    Sage, S.O.3
  • 36
    • 0023219685 scopus 로고
    • Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate
    • Clapper, D. L., Walseth, T. F., Dargie, P. J., and Lee, H. C. (1987). Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate. J. Biol. Chem. 262, 9561-9568.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9561-9568
    • Clapper, D.L.1    Walseth, T.F.2    Dargie, P.J.3    Lee, H.C.4
  • 37
    • 0026418298 scopus 로고
    • 2+ release in sea urchin egg homogenates: Modulation by cyclic ADP-ribose
    • 2+ release in sea urchin egg homogenates: Modulation by cyclic ADP-ribose. Science 253, 1143-1146.
    • (1991) Science , vol.253 , pp. 1143-1146
    • Galione, A.1    Lee, H.C.2    Busa, W.B.3
  • 38
    • 0020490710 scopus 로고
    • Activation of a rat liver NAD glycohydrolase by histone
    • Moss, J., Chang, A. W., and Stanley, S. J. (1982). Activation of a rat liver NAD glycohydrolase by histone. J. Biol. Chem. 257, 5755-5759.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5755-5759
    • Moss, J.1    Chang, A.W.2    Stanley, S.J.3
  • 39
    • 0028339101 scopus 로고
    • Synergistic calcium release in the sea urchin egg by ryanodine and cyclic ADP-ribose
    • Buck, W. R., Hoffmann, E. E., Rakow, T. L., and Shen, S. S. (1994). Synergistic calcium release in the sea urchin egg by ryanodine and cyclic ADP-ribose. Dev. Biol. 163, 1-10.
    • (1994) Dev. Biol. , vol.163 , pp. 1-10
    • Buck, W.R.1    Hoffmann, E.E.2    Rakow, T.L.3    Shen, S.S.4
  • 40
    • 0025329215 scopus 로고
    • A synthetic peptide of the pseudosubstrate domain of protein kinase C blocks cytoplasmic alkalinization during activation of sea urchin egg
    • Shen, S. S., and Buck, W. R. (1990). A synthetic peptide of the pseudosubstrate domain of protein kinase C blocks cytoplasmic alkalinization during activation of sea urchin egg. Dev. Biol. 140, 272-280.
    • (1990) Dev. Biol. , vol.140 , pp. 272-280
    • Shen, S.S.1    Buck, W.R.2
  • 41
    • 0024408377 scopus 로고
    • Measurement of volume injected into individual cells by quantitative fluorescence microscopy
    • Lee, G. M. (1989). Measurement of volume injected into individual cells by quantitative fluorescence microscopy. J. Cell Sci. 94, 443-447.
    • (1989) J. Cell Sci. , vol.94 , pp. 443-447
    • Lee, G.M.1
  • 43
    • 0027082726 scopus 로고
    • Internal calcium release and activation of sea urchin eggs by cGMP are independent of the phosphoinositide signaling pathway
    • Whalley, T., McDougall, A., Crossley, I., Swann, K., and Whitaker, M. J. (1992). Internal calcium release and activation of sea urchin eggs by cGMP are independent of the phosphoinositide signaling pathway. Mol. Biol. Cell 3, 373-383.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 373-383
    • Whalley, T.1    McDougall, A.2    Crossley, I.3    Swann, K.4    Whitaker, M.J.5
  • 44
    • 0025793981 scopus 로고
    • Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq
    • Smrcka, A. V., Hepler, J. R., Brown, K. O., and Sternweis, P. C. (1991). Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq. Science 251, 804-807.
    • (1991) Science , vol.251 , pp. 804-807
    • Smrcka, A.V.1    Hepler, J.R.2    Brown, K.O.3    Sternweis, P.C.4
  • 45
    • 0027452685 scopus 로고
    • Cyclic ADP-ribose: A new way to control calcium
    • Galione, A. (1993). Cyclic ADP-ribose: A new way to control calcium. Science 259, 325-326.
    • (1993) Science , vol.259 , pp. 325-326
    • Galione, A.1
  • 46
    • 0030044293 scopus 로고    scopus 로고
    • Nitric oxide-induced mobilization of intracellular calcium via the cyclic ADP-ribose signaling pathway
    • Willmott, N., Sethi, J. K., Walseth, T. F., Lee, H. C., White, A. M., and Galione, A. (1996). Nitric oxide-induced mobilization of intracellular calcium via the cyclic ADP-ribose signaling pathway. J. Biol. Chem. 271, 3699-3705.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3699-3705
    • Willmott, N.1    Sethi, J.K.2    Walseth, T.F.3    Lee, H.C.4    White, A.M.5    Galione, A.6
  • 47
    • 0027547615 scopus 로고
    • Thimerosal reveals calcium-induced calcium release in unfertilised sea urchin eggs
    • McDougall, A., Gillot, I., and Whitaker, M. (1993). Thimerosal reveals calcium-induced calcium release in unfertilised sea urchin eggs. Zygote 1, 35-42.
    • (1993) Zygote , vol.1 , pp. 35-42
    • McDougall, A.1    Gillot, I.2    Whitaker, M.3
  • 48
    • 0028179361 scopus 로고
    • 2+ release mediated by both the inositol 1,4,5-triphosphate and the ryanodine receptors in sea urchin eggs
    • 2+ release mediated by both the inositol 1,4,5-triphosphate and the ryanodine receptors in sea urchin eggs. J. Biol. Chem. 269, 11247-11253.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11247-11253
    • Tanaka, Y.1    Tashjian A.H., Jr.2
  • 49
    • 20644438657 scopus 로고    scopus 로고
    • Actions of sulfhydryl reagents on single ryanodine receptor Ca(2+)-release channels from sheep myocardium
    • Eager, K. R., Roden, L. D., and Dulhunty, A. F. (1997). Actions of sulfhydryl reagents on single ryanodine receptor Ca(2+)-release channels from sheep myocardium. Am. J. Physiol. 272, C1908-18.
    • (1997) Am. J. Physiol. , vol.272
    • Eager, K.R.1    Roden, L.D.2    Dulhunty, A.F.3
  • 50
    • 0021751197 scopus 로고
    • Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C
    • Hidaka, H., Inagaki, M., Kawamoto, S., and Sasaki, Y. (1984). Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C. Biochemistry 23, 5036-5041.
    • (1984) Biochemistry , vol.23 , pp. 5036-5041
    • Hidaka, H.1    Inagaki, M.2    Kawamoto, S.3    Sasaki, Y.4
  • 51
    • 0024390057 scopus 로고
    • + antiport during fertilization of the sea urchin egg is blocked by W-7 but is insensitive to K252a and H7
    • + antiport during fertilization of the sea urchin egg is blocked by W-7 but is insensitive to K252a and H7. Biochem. Biophys. Res. Commun. 161, 1100-1108.
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 1100-1108
    • Shen, S.S.1
  • 52
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka, Y. (1986). Studies and perspectives of protein kinase C. Science 233, 305-312.
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 53
    • 0021828929 scopus 로고
    • Stimulation of the Na/H exchanger of sea urchin eggs by phorbol ester
    • Swann, K., and Whitaker, M. (1985). Stimulation of the Na/H exchanger of sea urchin eggs by phorbol ester. Nature 314, 274-27753.
    • (1985) Nature , vol.314 , pp. 274-27753
    • Swann, K.1    Whitaker, M.2
  • 56
    • 0029100209 scopus 로고
    • Structural role of disulfide bridges in the cyclic ADP-ribose related bifunctional ectoenzyme CD38
    • Guida, L., Franco, L., Zocchi, E., and De Flora, A. (1995). Structural role of disulfide bridges in the cyclic ADP-ribose related bifunctional ectoenzyme CD38. FEBS Lett. 368, 481-484.
    • (1995) FEBS Lett. , vol.368 , pp. 481-484
    • Guida, L.1    Franco, L.2    Zocchi, E.3    De Flora, A.4
  • 57
    • 0026468136 scopus 로고
    • Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38
    • States, D. J., Walseth, T. F., and Lee, H. C. (1992). Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38. Trends. Biochem. Sci. 17, 495.
    • (1992) Trends. Biochem. Sci. , vol.17 , pp. 495
    • States, D.J.1    Walseth, T.F.2    Lee, H.C.3
  • 58
    • 0027230589 scopus 로고
    • Wide distribution of an enzyme that catalyzes the hydrolysis of cyclic ADP-ribose
    • Lee, H. C., and Aarhus, R. (1993). Wide distribution of an enzyme that catalyzes the hydrolysis of cyclic ADP-ribose. Biochim. Biophys. Acta 1164, 68-74.
    • (1993) Biochim. Biophys. Acta , vol.1164 , pp. 68-74
    • Lee, H.C.1    Aarhus, R.2
  • 59
    • 0024604307 scopus 로고
    • The sulfhydryl reagent thimerosal elicits human platelet aggregation by mobilization of intracellular calcium and secondary prostaglandin endoperoxide formation
    • Hecker, M., Brune, B., Decker, K., and Ullrich, V. (1989). The sulfhydryl reagent thimerosal elicits human platelet aggregation by mobilization of intracellular calcium and secondary prostaglandin endoperoxide formation. Biochem. Biophys. Res. Commun. 159, 961-968.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 961-968
    • Hecker, M.1    Brune, B.2    Decker, K.3    Ullrich, V.4
  • 60
    • 0025021920 scopus 로고
    • Involvement of calcium in the thimerosal-stimulated formation of leukotriene by fMLP in human polymorphonuclear leukocytes
    • Hatzelmann, A., Haurand, M., and Ullrich, V. (1990). Involvement of calcium in the thimerosal-stimulated formation of leukotriene by fMLP in human polymorphonuclear leukocytes. Biochem. Pharmacol. 39, 559-567.
    • (1990) Biochem. Pharmacol. , vol.39 , pp. 559-567
    • Hatzelmann, A.1    Haurand, M.2    Ullrich, V.3
  • 61
    • 0026084587 scopus 로고
    • Thimerosal causes calcium oscillations and sensitizes calcium-induced calcium release in unfertilized hamster eggs
    • Swann, K. (1991). Thimerosal causes calcium oscillations and sensitizes calcium-induced calcium release in unfertilized hamster eggs. FEBS Lett. 278, 175-178.
    • (1991) FEBS Lett. , vol.278 , pp. 175-178
    • Swann, K.1
  • 63
    • 0024401147 scopus 로고
    • Critical sulfhydryls regulate calcium release from sarcoplasmic reticulum
    • Abramson, J. J., and Salama, G. (1989). Critical sulfhydryls regulate calcium release from sarcoplasmic reticulum. J. Bioenerg. Biomembr. 21, 283-294.
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 283-294
    • Abramson, J.J.1    Salama, G.2
  • 64
    • 0026444081 scopus 로고
    • 2+ spikes in HeLa cells by sensitizing the inositol 1,4,5-trisphosphate receptor
    • 2+ spikes in HeLa cells by sensitizing the inositol 1,4,5-trisphosphate receptor. J. Biol. Chem. 267, 25113-25119.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25113-25119
    • Bootman, M.D.1    Taylor, C.W.2    Berridge, M.J.3
  • 65
    • 0030998836 scopus 로고    scopus 로고
    • 2+ release and directly activates ion channels in mouse pancreatic acinar cells
    • 2+ release and directly activates ion channels in mouse pancreatic acinar cells. Biochem. J. 324, 645-651.
    • (1997) Biochem. J. , vol.324 , pp. 645-651
    • Mogami, H.1    Lloyd Mills, C.2    Gallacher, D.V.3
  • 66
    • 0019332280 scopus 로고
    • Protein effects on the activity of guanosine 3′:5′-monophosphate-dependent protein kinase
    • Walton, G. M., and Gill, G. N. (1980). Protein effects on the activity of guanosine 3′:5′-monophosphate-dependent protein kinase. J. Biol. Chem. 255, 1693-1699.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1693-1699
    • Walton, G.M.1    Gill, G.N.2
  • 67
    • 0027455419 scopus 로고
    • Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase
    • Suko, J., Maurer-Fogy, I., Plank, B., Bertel, O., Wylfgang, W., Hohenegger, M., and Hellmann, G. (1993). Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase. Biochim. Biophys. Acta 1175, 193-206.
    • (1993) Biochim. Biophys. Acta , vol.1175 , pp. 193-206
    • Suko, J.1    Maurer-Fogy, I.2    Plank, B.3    Bertel, O.4    Wylfgang, W.5    Hohenegger, M.6    Hellmann, G.7
  • 68
    • 0026089312 scopus 로고
    • Regulation of the cardiac ryanodine receptor by protein kinase-dependent phosphorylation
    • Takasago, T., Imagawa, T., Frukawa, K., Ogorusu, T., and Shigekawa, M. (1991). Regulation of the cardiac ryanodine receptor by protein kinase-dependent phosphorylation. J. Biochem. Tokyo 109, 163-170.
    • (1991) J. Biochem. Tokyo , vol.109 , pp. 163-170
    • Takasago, T.1    Imagawa, T.2    Frukawa, K.3    Ogorusu, T.4    Shigekawa, M.5
  • 69
    • 0028918056 scopus 로고
    • Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from cardiac muscle
    • Hain, J., Onoue, H., Mayrleitner, M., Fleischer, S., and Schindler, H. (1995). Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from cardiac muscle. J. Biol. Chem. 270, 2074-2081.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2074-2081
    • Hain, J.1    Onoue, H.2    Mayrleitner, M.3    Fleischer, S.4    Schindler, H.5
  • 70
    • 0026799405 scopus 로고
    • Inactivation of the sarcoplasmic reticulum calcium channel by protein kinase
    • Wang, J., and Best, P. M. (1992). Inactivation of the sarcoplasmic reticulum calcium channel by protein kinase. Nature 359, 739-741.
    • (1992) Nature , vol.359 , pp. 739-741
    • Wang, J.1    Best, P.M.2
  • 71
    • 0027340424 scopus 로고
    • 2+ release channel activity by phosphorylation of the skeletal muscle ryanodine receptor
    • 2+ release channel activity by phosphorylation of the skeletal muscle ryanodine receptor. FEBS Lett. 332, 237-242.
    • (1993) FEBS Lett. , vol.332 , pp. 237-242
    • Herrmann-Frank, A.1    Varsanyi, M.2
  • 72
    • 0028941491 scopus 로고
    • Metabolism of cyclic ADP-ribose in opossum kidney renal epithelial cells
    • Beers, K. W., Chini, E. N., Lee, H. C., and Dousa, T. P. (1995). Metabolism of cyclic ADP-ribose in opossum kidney renal epithelial cells. Am. J. Physiol. 268, C741-C746. 9
    • (1995) Am. J. Physiol. , vol.268
    • Beers, K.W.1    Chini, E.N.2    Lee, H.C.3    Dousa, T.P.4
  • 73
    • 0029828803 scopus 로고    scopus 로고
    • Nicotinamide inhibits cyclic ADP-ribose-mediated calcium signalling in sea urchin eggs
    • Sethi, J. K., Empson, R. M., and Galione, A. (1996). Nicotinamide inhibits cyclic ADP-ribose-mediated calcium signalling in sea urchin eggs. Biochem. J. 319, 613-617.
    • (1996) Biochem. J. , vol.319 , pp. 613-617
    • Sethi, J.K.1    Empson, R.M.2    Galione, A.3
  • 74
    • 0027393833 scopus 로고
    • Cyclic ADP-ribose in insulin secretion from pancreatic β cells
    • Takasawa, S., Nata, K., Yonekura, H., and Okamoto, H. (1993). Cyclic ADP-ribose in insulin secretion from pancreatic β cells. Science 259, 370-373.
    • (1993) Science , vol.259 , pp. 370-373
    • Takasawa, S.1    Nata, K.2    Yonekura, H.3    Okamoto, H.4
  • 76
    • 0030061129 scopus 로고    scopus 로고
    • Streptozotocin, an inducer of NAD+ decrease, attenuates M-potassium current inhibition by ATP, bradykinin, angiotensin II, endothelin 1 and acetylcholine in NG108-15 cells
    • Higashida, H., Egorova, A., Hoshi, N., and Noda, M. (1996). Streptozotocin, an inducer of NAD+ decrease, attenuates M- potassium current inhibition by ATP, bradykinin, angiotensin II, endothelin 1 and acetylcholine in NG108-15 cells. FEBS Lett. 379, 236-238.
    • (1996) FEBS Lett. , vol.379 , pp. 236-238
    • Higashida, H.1    Egorova, A.2    Hoshi, N.3    Noda, M.4
  • 77
    • 0027471709 scopus 로고
    • Inositol 1,4,5-triphosphate mass changes from fertilization through first cleavage in Xenopus laevis
    • Stith, B. J., Goalstone, M., Silva, S., and Jaynes, C. (1993). Inositol 1,4,5-triphosphate mass changes from fertilization through first cleavage in Xenopus laevis. Mol. Biol. Cell 4, 435-443.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 435-443
    • Stith, B.J.1    Goalstone, M.2    Silva, S.3    Jaynes, C.4
  • 78
    • 0030602026 scopus 로고    scopus 로고
    • Fertilization stimulates an increase in inositol trisphosphate and inositol lipid levels in Xenopus eggs
    • Snow, P., Yim, D. L., Leibow, J. D., Saini, S., and Nuccitelli, R. (1996). Fertilization stimulates an increase in inositol trisphosphate and inositol lipid levels in Xenopus eggs. Dev. Biol. 180, 108-118.
    • (1996) Dev. Biol. , vol.180 , pp. 108-118
    • Snow, P.1    Yim, D.L.2    Leibow, J.D.3    Saini, S.4    Nuccitelli, R.5


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