메뉴 건너뛰기




Volumn 127, Issue 1, 1997, Pages 1-10

Phosphates and inositol phospholipids: How big is the iceberg?

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; INOSITOL PHOSPHATE; PHOSPHATIDYLINOSITIDE; PHOSPHOLIPID; CALCIUM; INOSITOL 1,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL;

EID: 0030971956     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(96)03999-8     Document Type: Article
Times cited : (9)

References (108)
  • 1
    • 0020643801 scopus 로고
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate. Nature 306, 67-68.
    • (1983) Nature , vol.306 , pp. 67-68
    • Streb, H.1    Irvine, R.2    Berridge, M.3    Schulz, I.4
  • 2
    • 0023062987 scopus 로고
    • Inositol triphosphate and diacylglycerol: Two interacting second messengers
    • Berridge, M.J. (1987) Inositol triphosphate and diacylglycerol: two interacting second messengers. Annu. Rev. Biochem. 56, 159-193.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 159-193
    • Berridge, M.J.1
  • 3
    • 0028826727 scopus 로고
    • Capacitative calcium entry
    • Berridge, M.J. (1995) Capacitative calcium entry. Biochem. J. 312, 1-11.
    • (1995) Biochem. J. , vol.312 , pp. 1-11
    • Berridge, M.J.1
  • 4
    • 0028298064 scopus 로고
    • Spatial and temporal signalling by calcium
    • Berridge, M.J. and Dupont, G. (1994) Spatial and temporal signalling by calcium. Curr. Opin. Cell Biol. 6, 267-274.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 267-274
    • Berridge, M.J.1    Dupont, G.2
  • 11
    • 0029094146 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor in skeletal muscle: Differential expression in myofibres
    • Moschella, M.C., Watras, J., Jayaraman, T. and Marks, A.R. (1995) Inositol 1,4,5-trisphosphate receptor in skeletal muscle: Differential expression in myofibres. J. Muscle Res. Cell Motil. 16, 390-400.
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 390-400
    • Moschella, M.C.1    Watras, J.2    Jayaraman, T.3    Marks, A.R.4
  • 12
    • 0027415234 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor in heart - Evidence for its concentration in purkinje myocytes of the conduction system
    • Gorza, L., Schiaffino, S. and Volpe, P. (1993) Inositol 1,4,5-trisphosphate receptor in heart - evidence for its concentration in purkinje myocytes of the conduction system. J. Cell Biol. 121, 345-353.
    • (1993) J. Cell Biol. , vol.121 , pp. 345-353
    • Gorza, L.1    Schiaffino, S.2    Volpe, P.3
  • 13
    • 0027461948 scopus 로고
    • Different intracellular localization of inositol 1,4,5-trisphosphate and ryanodine receptors in cardiomyocytes
    • Kijima, Y., Saito, A., Jetton, T.L., Magnuson, M.A. and Fleischer, S. (1993) Different intracellular localization of inositol 1,4,5-trisphosphate and ryanodine receptors in cardiomyocytes. J. Biol. Chem. 268, 3499-3506.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3499-3506
    • Kijima, Y.1    Saito, A.2    Jetton, T.L.3    Magnuson, M.A.4    Fleischer, S.5
  • 15
    • 0025060264 scopus 로고
    • 2+ and inositol-trisphosphate mass in a human neuroblastoma cell line, SH-SY5Y
    • 2+ and inositol-trisphosphate mass in a human neuroblastoma cell line, SH-SY5Y. Biochem. J. 265, 555-562.
    • (1990) Biochem. J. , vol.265 , pp. 555-562
    • Lambert, D.G.1    Nahorski, S.R.2
  • 16
    • 0001019711 scopus 로고
    • Mass measurement of inositol 1,4,5-trisphosphate using a specific binding assay
    • Irvine, R.F., ed. Raven Press, New York
    • Palmer, S. and Wakelam, M.J.O. (1990) Mass measurement of inositol 1,4,5-trisphosphate using a specific binding assay. In: Methods in Inositide Research (Irvine, R.F., ed.) pp. 127-133, Raven Press, New York.
    • (1990) Methods in Inositide Research , pp. 127-133
    • Palmer, S.1    Wakelam, M.J.O.2
  • 17
    • 0025033371 scopus 로고
    • A competition binding assay for the determination of the inositol(1,4,5)-trisphospahte content of human leukocytes
    • Nibbering, P.H., Zomerdijk, T.P.L., van Haaster, P.J.M. and Furth, R. (1990) A competition binding assay for the determination of the inositol(1,4,5)-trisphospahte content of human leukocytes. Biochem. Biophys. Res. Commun. 170, 755-762.
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 755-762
    • Nibbering, P.H.1    Zomerdijk, T.P.L.2    Van Haaster, P.J.M.3    Furth, R.4
  • 18
    • 0025977466 scopus 로고
    • Relationship between the calcium-mobilizing action of inositol 1,4,5-trisphosphate in permeable AR4-2J cells and the estimated levels of inositol 1,4,5-trisphosphate in intact AR4-2J cells
    • Bird, G.J., Oliver, K.G., Horstman, D.A., Obie, J. and Putney, J.W. Jr. (1991) Relationship between the calcium-mobilizing action of inositol 1,4,5-trisphosphate in permeable AR4-2J cells and the estimated levels of inositol 1,4,5-trisphosphate in intact AR4-2J cells. Biochem. J. 273, 541-546.
    • (1991) Biochem. J. , vol.273 , pp. 541-546
    • Bird, G.J.1    Oliver, K.G.2    Horstman, D.A.3    Obie, J.4    Putney J.W., Jr.5
  • 19
    • 0027209844 scopus 로고
    • Triads and transverse tubules isolated from skeletal muscle contain high levels of inositol 1,4,5-trisphosphate
    • Hidalgo, C., Jorquera, J., Tapia, V. and Donoso, P. (1993) Triads and transverse tubules isolated from skeletal muscle contain high levels of inositol 1,4,5-trisphosphate. J. Biol. Chem. 268, 15111-15117.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15111-15117
    • Hidalgo, C.1    Jorquera, J.2    Tapia, V.3    Donoso, P.4
  • 20
    • 0024582989 scopus 로고
    • Inositol polyphosphate-mediated repartitioning of aldolase in skeletal muscle triads and myofibrils
    • Thieleczek, R., Mayr, G. and Brandt, N. (1989) Inositol polyphosphate-mediated repartitioning of aldolase in skeletal muscle triads and myofibrils. J. Biol. Chem. 264, 7349-7356.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7349-7356
    • Thieleczek, R.1    Mayr, G.2    Brandt, N.3
  • 21
    • 0029156476 scopus 로고
    • Inositol 1,4,5-trisphosphate binding to porcine tracheal smooth muscle aldolase
    • Baron, C.B., Ozaki, S., Watanabe, Y., Hirata, M., Labelle, E.F. and Coburn, R.F. (1995) Inositol 1,4,5-trisphosphate binding to porcine tracheal smooth muscle aldolase. J. Biol. Chem. 270, 20459-20465.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20459-20465
    • Baron, C.B.1    Ozaki, S.2    Watanabe, Y.3    Hirata, M.4    Labelle, E.F.5    Coburn, R.F.6
  • 23
    • 0028797128 scopus 로고
    • Neurohumoral modulation of the intracellular pH in the heart
    • Puceat, M. and Vassort, G. (1995) Neurohumoral modulation of the intracellular pH in the heart. Cardiovasc. Res. 29, 178-183.
    • (1995) Cardiovasc. Res. , vol.29 , pp. 178-183
    • Puceat, M.1    Vassort, G.2
  • 24
    • 0028235884 scopus 로고
    • + antiport activity and gene expression in cultured vascular smooth muscle cells - Role of protein kinase C
    • + antiport activity and gene expression in cultured vascular smooth muscle cells - Role of protein kinase C. J. Clin. Invest. 93, 2623-2631.
    • (1994) J. Clin. Invest. , vol.93 , pp. 2623-2631
    • Williams, B.1    Howard, R.L.2
  • 25
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon, M.A., Ferguson, K.M., O'Brien, R., Sigler, P.B. and Schlessinger, J. (1995) Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc. Natl. Acad. Sci. USA. 92, 10472-10476.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brien, R.3    Sigler, P.B.4    Schlessinger, J.5
  • 26
    • 0028938639 scopus 로고
    • Inositol phosphate release and metabolism in rat left atria
    • Woodcock, E., Suss, M. and Anderson, K. (1995) Inositol phosphate release and metabolism in rat left atria. Circ. Res. 76, 252-260.
    • (1995) Circ. Res. , vol.76 , pp. 252-260
    • Woodcock, E.1    Suss, M.2    Anderson, K.3
  • 27
    • 0026080005 scopus 로고
    • Purification of an inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase activity from rat liver and the evaluation of its substrate specificity
    • Nogimori, K., Hughes, P.J., Glennon, M.C., Hodson, M.E., Putney, J.W. Jr. and Shears, S.B. (1991) Purification of an inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase activity from rat liver and the evaluation of its substrate specificity. J. Biol. Chem. 266, 16499-16506.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16499-16506
    • Nogimori, K.1    Hughes, P.J.2    Glennon, M.C.3    Hodson, M.E.4    Putney J.W., Jr.5    Shears, S.B.6
  • 28
    • 0025782487 scopus 로고
    • A salt-activated inositol 1,3,4,5-tetrakisphosphate 3-phosphatase at the inner surface of the human erythrocyte membrane
    • Estradagarcia, T., Craxton, A., Kirk, C.J. and Michell, R.H. (1991) A salt-activated inositol 1,3,4,5-tetrakisphosphate 3-phosphatase at the inner surface of the human erythrocyte membrane. Proc. Royal Soc. London B. Biol. Sci. 244, 63-68.
    • (1991) Proc. Royal Soc. London B. Biol. Sci. , vol.244 , pp. 63-68
    • Estradagarcia, T.1    Craxton, A.2    Kirk, C.J.3    Michell, R.H.4
  • 29
    • 0027460280 scopus 로고
    • 4 3-phosphatase is compartmentalized inside endoplasmic reticulum
    • 4 3-phosphatase is compartmentalized inside endoplasmic reticulum. J. Biol. Chem. 268, 6161-6167.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6161-6167
    • Ali, N.1    Craxton, A.2    Shears, S.B.3
  • 30
    • 0025285223 scopus 로고
    • Inositol 1,3,4,5,6-pentak-isphosphate and inositol hexakisphosphate inhibit inositol-1,3,4,5-tetrakisphosphate 3-phosphatase in rat parotid gland
    • Hughes, P.J. and Shears, S.B. (1990) Inositol 1,3,4,5,6-pentak-isphosphate and inositol hexakisphosphate inhibit inositol-1,3,4,5-tetrakisphosphate 3-phosphatase in rat parotid gland. J. Biol. Chem. 265, 9869-9875.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9869-9875
    • Hughes, P.J.1    Shears, S.B.2
  • 31
    • 0029618911 scopus 로고
    • A novel, phospholipase C-independent pathway of inositol 1,4,5-trisphosphate formation in Dictiostelium and rat liver
    • Dijken, P.V., Haas, J.-R.D., Craxton, A., Erneux, C., Shears, S. and Haastert, P.V. (1995) A novel, phospholipase C-independent pathway of inositol 1,4,5-trisphosphate formation in Dictiostelium and rat liver. J. Biol. Chem. 270, 29724-29731.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29724-29731
    • Dijken, P.V.1    Haas, J.-R.D.2    Craxton, A.3    Erneux, C.4    Shears, S.5    Haastert, P.V.6
  • 33
    • 0023427097 scopus 로고
    • Bovine brain cytosol contains three immunologically distinct forms of inositol phospholipid-specific phospholipase C
    • Ryu, S., Suh, P.-G., Choi, K., Lee, K.-Y. and Rhee, S. (1987) Bovine brain cytosol contains three immunologically distinct forms of inositol phospholipid-specific phospholipase C. Proc. Natl. Acad. Sci. USA. 84, 6649-6653.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6649-6653
    • Ryu, S.1    Suh, P.-G.2    Choi, K.3    Lee, K.-Y.4    Rhee, S.5
  • 34
    • 0026654469 scopus 로고
    • Regulation of inositol phospholipid-specific phospholipase C isozymes
    • Rhee, S. and Choi, K. (1992) Regulation of inositol phospholipid-specific phospholipase C isozymes. J. Biol. Chem. 267, 12393-12396.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12393-12396
    • Rhee, S.1    Choi, K.2
  • 35
    • 0023000847 scopus 로고
    • Sustained diacylglycerol formation from inositol phospholipids in angiotensin II-stimulated vascular smooth muscle cells
    • M.G.
    • Greindling, K., Rittenhouse, S., Brock, T., Ekstein, L. Jr, M.G. and Alexander, R. (1986) Sustained diacylglycerol formation from inositol phospholipids in angiotensin II-stimulated vascular smooth muscle cells. J. Biol. Chem. 261, 5901-5906.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5901-5906
    • Greindling, K.1    Rittenhouse, S.2    Brock, T.3    Ekstein L., Jr.4    Alexander, R.5
  • 36
    • 0026696397 scopus 로고
    • Evidence for phosphatidylinositol hydrolysis in pancreatic islets stimulated with carbamoylcholine - Kinetic analysis of inositol polyphosphate metabolism
    • Biden, T.J., Prugue, M.L. and Davison, A. (1992) Evidence for phosphatidylinositol hydrolysis in pancreatic islets stimulated with carbamoylcholine - kinetic analysis of inositol polyphosphate metabolism. Biochem. J. 285, 541-549.
    • (1992) Biochem. J. , vol.285 , pp. 541-549
    • Biden, T.J.1    Prugue, M.L.2    Davison, A.3
  • 37
    • 0027265075 scopus 로고
    • Regulation by membrane potential of phosphatidylinositol hydrolysis in pancreatic islets
    • Biden, T.J., Davison, A. and Prugue, M.L. (1993) Regulation by membrane potential of phosphatidylinositol hydrolysis in pancreatic islets. J. Biol. Chem. 268, 11065-11072.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11065-11072
    • Biden, T.J.1    Davison, A.2    Prugue, M.L.3
  • 38
    • 0024474713 scopus 로고
    • 3H-labeled inositol bis- And monophosphates in agonist-activated rat parotid acinar cells
    • 3H-labeled inositol bis- and monophosphates in agonist-activated rat parotid acinar cells. J. Biol. Chem. 264, 9400-9407.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9400-9407
    • Hughes, A.R.1    Putney J.W., Jr.2
  • 39
    • 0025092380 scopus 로고
    • Does the inositol phosphate signalling system function in the heart? a comparison of inositol lipid turnover in cardiac and smooth muscle
    • Doggwiler, K. and Buxton, I. (1990) Does the inositol phosphate signalling system function in the heart? A comparison of inositol lipid turnover in cardiac and smooth muscle. Proc. West Pharmacol. Soc. 33, 111-115.
    • (1990) Proc. West Pharmacol. Soc. , vol.33 , pp. 111-115
    • Doggwiler, K.1    Buxton, I.2
  • 40
    • 0028224732 scopus 로고
    • Agonist-specific regulation of polyphosphoinositide metabolism in pulmonary artery smooth muscle cells
    • Button, D., Rothman, A., Bongiorno, C., Kupperman, E., Wolner, B. and Taylor, P. (1994) Agonist-specific regulation of polyphosphoinositide metabolism in pulmonary artery smooth muscle cells. J. Biol. Chem. 260, 6390-6398.
    • (1994) J. Biol. Chem. , vol.260 , pp. 6390-6398
    • Button, D.1    Rothman, A.2    Bongiorno, C.3    Kupperman, E.4    Wolner, B.5    Taylor, P.6
  • 41
    • 0029666275 scopus 로고    scopus 로고
    • Evidence that phospholipase C δ1 is the effector in the Gh (transglutaminase II)-mediated signalling
    • Feng, J.-F., Rhee, S. and Im, M.-J. (1996) Evidence that phospholipase C δ1 is the effector in the Gh (transglutaminase II)-mediated signalling. J. Biol. Chem. 271, 16451-16454.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16451-16454
    • Feng, J.-F.1    Rhee, S.2    Im, M.-J.3
  • 42
    • 0025065288 scopus 로고
    • 1-adrenergic receptor. I Identification by photolabeling of membrane and ternery complex preparations
    • 1-adrenergic receptor. I Identification by photolabeling of membrane and ternery complex preparations. J. Biol. Chem. 165, 18944-18951.
    • (1990) J. Biol. Chem. , vol.165 , pp. 18944-18951
    • Im, M.-J.1    Graham, R.2
  • 45
    • 0030043081 scopus 로고    scopus 로고
    • Identification of a phosphatidylinositol 4,5-bisphosphate-binding site in chicken skeletal muscle α-actin
    • Fukami, K., Sawada, N., Endo, T. and Takenawa, T. (1996) Identification of a phosphatidylinositol 4,5-bisphosphate-binding site in chicken skeletal muscle α-actin. J. Biol. Chem. 271, 2646-2650.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2646-2650
    • Fukami, K.1    Sawada, N.2    Endo, T.3    Takenawa, T.4
  • 47
    • 0030004951 scopus 로고    scopus 로고
    • Oxytocin receptor couples to the 80 kDa G(h alpha) family protein in human myometrium
    • Baek, K.J., Kwon, N.S., Lee, H.S., Kim, M.S., Muralidhar, P. and Im, M.J. (1996) Oxytocin receptor couples to the 80 kDa G(h alpha) family protein in human myometrium. Biochem. J. 315, 739-744.
    • (1996) Biochem. J. , vol.315 , pp. 739-744
    • Baek, K.J.1    Kwon, N.S.2    Lee, H.S.3    Kim, M.S.4    Muralidhar, P.5    Im, M.J.6
  • 50
    • 0026209437 scopus 로고
    • Inositol tetrakisphosphate as a second messenger: Confusions, contradictions, and a potential resolution
    • Irvine, R.F. (1991) Inositol tetrakisphosphate as a second messenger: confusions, contradictions, and a potential resolution. BioEssays 13, 1-9.
    • (1991) BioEssays , vol.13 , pp. 1-9
    • Irvine, R.F.1
  • 51
    • 0026915386 scopus 로고
    • 2+ entry -Toward a proliferation or a simplification
    • 2+ entry -Toward a proliferation or a simplification. FASEB J. 6, 3085-3091.
    • (1992) FASEB J. , vol.6 , pp. 3085-3091
    • Irvine, R.F.1
  • 52
    • 0025609411 scopus 로고
    • Capacitative calcium entry revisited
    • Putney, J.W. Jr. (1990) Capacitative calcium entry revisited. Cell Calcium 11, 611-624.
    • (1990) Cell Calcium , vol.11 , pp. 611-624
    • Putney J.W., Jr.1
  • 53
    • 0025667980 scopus 로고
    • Receptor-regulated calcium entry
    • Putney, J.W. Jr. (1990) Receptor-regulated calcium entry. Pharmacol. Ther. 48, 427-434.
    • (1990) Pharmacol. Ther. , vol.48 , pp. 427-434
    • Putney J.W., Jr.1
  • 55
    • 0027422088 scopus 로고
    • The signal for capacitative calcium entry
    • Putney, J.W. Jr. and Bird, G.S. (1993) The signal for capacitative calcium entry. Cell 75, 199-201.
    • (1993) Cell , vol.75 , pp. 199-201
    • Putney J.W., Jr.1    Bird, G.S.2
  • 56
    • 0027422161 scopus 로고
    • Inhibition of thapsigargin-induced calcium entry by microinjected guanine nucleotide analogues - Evidence for the involvement of a small G-protein in capacitative calcium entry
    • Bird, G.S. and Putney, J.W. Jr. (1993) Inhibition of thapsigargin-induced calcium entry by microinjected guanine nucleotide analogues - evidence for the involvement of a small G-protein in capacitative calcium entry. J. Biol. Chem. 268, 21486-21488.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21486-21488
    • Bird, G.S.1    Putney J.W., Jr.2
  • 58
    • 0028917954 scopus 로고
    • Regulation of ras-mediated signalling: More than one way to skin a cat
    • Burgering, B. and Bos, J. (1995) Regulation of ras-mediated signalling: more than one way to skin a cat. Trends Neurosci. 20, 18-22.
    • (1995) Trends Neurosci. , vol.20 , pp. 18-22
    • Burgering, B.1    Bos, J.2
  • 60
    • 0026806487 scopus 로고
    • The interconversion of inositol 1,3,4,5,6-pentakisphosphate and inositol tetrakisphosphates in AR4-2J cells
    • Oliver, K.G., Putney, J.W. Jr, Obie, J.F. and Shears, S.B. (1992) The interconversion of inositol 1,3,4,5,6-pentakisphosphate and inositol tetrakisphosphates in AR4-2J cells. J. Biol. Chem. 267, 21528-21534.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21528-21534
    • Oliver, K.G.1    Putney J.W., Jr.2    Obie, J.F.3    Shears, S.B.4
  • 61
    • 0025873258 scopus 로고
    • Effects of transformation with the v-src oncogene on inositol phosphate metabolism in rat-1 fibroblasts
    • Mattingly, R.R., Stephens, L.R., Irvine, R.F. and Garrison, J.C. (1991) Effects of transformation with the v-src oncogene on inositol phosphate metabolism in rat-1 fibroblasts. J. Biol. Chem. 266, 15144-15153.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15144-15153
    • Mattingly, R.R.1    Stephens, L.R.2    Irvine, R.F.3    Garrison, J.C.4
  • 62
    • 0029891632 scopus 로고    scopus 로고
    • Thyroid-stimulating hormone rapidly stimulates inositol polyphosphate formation in FRTL-5 thyrocytes without activating phosphoinositidase
    • Singh, J., Hunt, P., Eggo, M.C., Sheppard, M.C., Kirk, C.J. and Michell, R.H. (1996) Thyroid-stimulating hormone rapidly stimulates inositol polyphosphate formation in FRTL-5 thyrocytes without activating phosphoinositidase C. Biochem. J. 316, 175-182.
    • (1996) C. Biochem. J. , vol.316 , pp. 175-182
    • Singh, J.1    Hunt, P.2    Eggo, M.C.3    Sheppard, M.C.4    Kirk, C.J.5    Michell, R.H.6
  • 64
    • 0029938944 scopus 로고    scopus 로고
    • Inositol 3,4,5,6-tetrakisphosphate inhibits the calmodulin-dependent protein kinase II-activated chloride conductance in T84 colonic epithelial cells
    • Xie, W.W., Kaetzel, M.A., Bruzik, K.S., Dedman, J.R., Shears, S.B. and Nelson, D.J. (1996) Inositol 3,4,5,6-tetrakisphosphate inhibits the calmodulin-dependent protein kinase II-activated chloride conductance in T84 colonic epithelial cells. J. Biol. Chem. 271, 14092-14097.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14092-14097
    • Xie, W.W.1    Kaetzel, M.A.2    Bruzik, K.S.3    Dedman, J.R.4    Shears, S.B.5    Nelson, D.J.6
  • 65
    • 0028842364 scopus 로고
    • Inositol hexakisphosphate binds to clathrin assembly protein 3(AP-3/AP180) and inhibits clathrin cage assembly in vitro
    • Norris, F.A., Ungewickell, E. and Majerus, P.W. (1995) Inositol hexakisphosphate binds to clathrin assembly protein 3(AP-3/AP180) and inhibits clathrin cage assembly in vitro. J. Biol. Chem. 270, 214-217.
    • (1995) J. Biol. Chem. , vol.270 , pp. 214-217
    • Norris, F.A.1    Ungewickell, E.2    Majerus, P.W.3
  • 66
    • 0028925007 scopus 로고
    • Inhibition of clathrin assembly by high affinity binding of specific inositol polyphosphates to the synapse-specific clathrin assembly protein AP-3
    • Ye, W.L., Ali, N., Bembenek, M.E., Shears, S.B. and Lafer, E.M. (1995) Inhibition of clathrin assembly by high affinity binding of specific inositol polyphosphates to the synapse-specific clathrin assembly protein AP-3. J. Biol. Chem. 270, 1564-1568.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1564-1568
    • Ye, W.L.1    Ali, N.2    Bembenek, M.E.3    Shears, S.B.4    Lafer, E.M.5
  • 67
    • 0028859443 scopus 로고
    • Functional diversity of C2 domains of synaptotagmin family - Mutational analysis of inositol high polyphosphate binding domain
    • Fukuda, M., Kojima, T., Aruga, J., Niinobe, M. and Mikoshiba, K. (1995) Functional diversity of C2 domains of synaptotagmin family - Mutational analysis of inositol high polyphosphate binding domain. J. Biol. Chem. 270, 26523-26527.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26523-26527
    • Fukuda, M.1    Kojima, T.2    Aruga, J.3    Niinobe, M.4    Mikoshiba, K.5
  • 68
    • 0029128910 scopus 로고
    • The interaction of coatomer with inositol polyphosphates is conserved in Saccharomyces cerevisiae
    • Ali, N., Duden, R., Bembenek, M.E. and Shears, S.B. (1995) The interaction of coatomer with inositol polyphosphates is conserved in Saccharomyces cerevisiae. Biochem. J. 310, 279-284.
    • (1995) Biochem. J. , vol.310 , pp. 279-284
    • Ali, N.1    Duden, R.2    Bembenek, M.E.3    Shears, S.B.4
  • 69
    • 0027536427 scopus 로고
    • The detection, purification, structural characterization, and metabolism of diphosphoinositol pentakisphosphate(s) and bisdiphosphoinositol tetrakisphosphate(s)
    • Stephens, L., Radenberg, T., Thiel, U., Vogel, G., Khoo, K.H., Dell, A., Jackson, T.R., Hawkins, P.T. and Mayr, G.W. (1993) The detection, purification, structural characterization, and metabolism of diphosphoinositol pentakisphosphate(s) and bisdiphosphoinositol tetrakisphosphate(s). J. Biol. Chem. 268, 4009-4015.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4009-4015
    • Stephens, L.1    Radenberg, T.2    Thiel, U.3    Vogel, G.4    Khoo, K.H.5    Dell, A.6    Jackson, T.R.7    Hawkins, P.T.8    Mayr, G.W.9
  • 70
    • 0027456498 scopus 로고
    • Turnover of inositol polyphosphate pyrophosphate in pancreatoma cells
    • Menniti, F.S., Miller, R.N., Putney, J.W. Jr. and Shears, S.B. (1993) Turnover of inositol polyphosphate pyrophosphate in pancreatoma cells. J. Biol. Chem. 268, 3850-3856.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3850-3856
    • Menniti, F.S.1    Miller, R.N.2    Putney J.W., Jr.3    Shears, S.B.4
  • 71
    • 0029975911 scopus 로고    scopus 로고
    • Purified inositol hexakisphosphate kinase is an ATP synthase: Diphosphoinositol pentakisphosphate as a high-energy phosphate donor
    • Voolmaier, S., Bembenek, M., Kaplin, A., Dorman, G., Olszewski, J., Prestwich, G. and Snyder, S. (1996) Purified inositol hexakisphosphate kinase is an ATP synthase: diphosphoinositol pentakisphosphate as a high-energy phosphate donor. Proc. Natl. Acad. Sci. USA 93, 4305-4310.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4305-4310
    • Voolmaier, S.1    Bembenek, M.2    Kaplin, A.3    Dorman, G.4    Olszewski, J.5    Prestwich, G.6    Snyder, S.7
  • 72
    • 0030133894 scopus 로고    scopus 로고
    • Intracellular signalling - Inositol phosphates - whither bound?
    • Irvine, R. and Cullen, P. (1996) Intracellular signalling - inositol phosphates - whither bound? Curr. Biol. 6, 537-540.
    • (1996) Curr. Biol. , vol.6 , pp. 537-540
    • Irvine, R.1    Cullen, P.2
  • 73
    • 0023693795 scopus 로고
    • Activation of a low specific activity form of DNa polymerase a by inositol-1,4-bisphosphate
    • Silvia, V., Curtin, G., Norman, J., Stec, J. and Busbee, D. (1988) Activation of a low specific activity form of DNA polymerase a by inositol-1,4-bisphosphate. Cell. 54, 651-658.
    • (1988) Cell , vol.54 , pp. 651-658
    • Silvia, V.1    Curtin, G.2    Norman, J.3    Stec, J.4    Busbee, D.5
  • 74
    • 0028083206 scopus 로고
    • Inositol polyphosphate 1-phosphatase is present in the nucleus and inhibits DNA synthesis
    • York, J.D., Saffitz, J.E. and Majerus, P.W. (1994) Inositol polyphosphate 1-phosphatase is present in the nucleus and inhibits DNA synthesis. J. Biol. Chem. 269, 19992-19999.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19992-19999
    • York, J.D.1    Saffitz, J.E.2    Majerus, P.W.3
  • 75
    • 0027759357 scopus 로고
    • Unclear or nuclear - Another role for the phosphatidylinositol cycle?
    • Divecha, N., Banfic, H. and Irvine, R.F. (1993) Unclear or nuclear - another role for the phosphatidylinositol cycle? Biochem. Soc. Trans. 21, 877-878.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 877-878
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 77
    • 0030060695 scopus 로고    scopus 로고
    • Arrhythmogenic action of thrombin during myocardial reperfusion via release of inositol 1,4,5-triphosphate
    • Jacobsen, A., Du, X.-J., Lambert, K., Dart, A. and Woodcock, E. (1996) Arrhythmogenic action of thrombin during myocardial reperfusion via release of inositol 1,4,5-triphosphate. Circulation 93, 23-26.
    • (1996) Circulation , vol.93 , pp. 23-26
    • Jacobsen, A.1    Du, X.-J.2    Lambert, K.3    Dart, A.4    Woodcock, E.5
  • 78
    • 0028908265 scopus 로고
    • Effects of dietary fat supplementation on inositol phosphate release and metabolism in rat left atria
    • Woodcock, E., Anderson, K., Du, X.-J. and Dart, A. (1995) Effects of dietary fat supplementation on inositol phosphate release and metabolism in rat left atria. J. Mol. Cell. Cardiol. 27, 867-872.
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 867-872
    • Woodcock, E.1    Anderson, K.2    Du, X.-J.3    Dart, A.4
  • 80
    • 0027209418 scopus 로고
    • Inositides and the nucleus and inositides in the nucleus
    • Divecha, N., Banfic, H. and Irvine, R.F. (1993) Inositides and the nucleus and inositides in the nucleus. Cell 74, 405-407.
    • (1993) Cell , vol.74 , pp. 405-407
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 81
    • 0026040577 scopus 로고
    • The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase-C to the nucleus
    • Divecha, N., Banfic, H. and Irvine, R.F. (1991) The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase-C to the nucleus. EMBO J. 10, 3207-3214.
    • (1991) EMBO J. , vol.10 , pp. 3207-3214
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 82
    • 0027536483 scopus 로고
    • Nuclear diacylglycerol is increased during cell proliferation in vivo
    • Banfic, H., Zizak, M., Divecha, N. and Irvine, R.F. (1993) Nuclear diacylglycerol is increased during cell proliferation in vivo. Biochem. J. 291, 633-636.
    • (1993) Biochem. J. , vol.291 , pp. 633-636
    • Banfic, H.1    Zizak, M.2    Divecha, N.3    Irvine, R.F.4
  • 83
    • 0027739726 scopus 로고
    • Nuclear localization of protein kinase-C
    • Leach, K.L. and Raben, D.M. (1993) Nuclear localization of protein kinase-C. Biochem. Soc. Trans. 21, 879-883.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 879-883
    • Leach, K.L.1    Raben, D.M.2
  • 84
    • 0029926108 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor is located to the inner nuclear membrane vindicating regulation of nuclear calcium signalling by inositol 1,4,5-trisphosphate. Discrete distribution of inositol phosphate receptors to inner and outer nuclear membranes
    • Humbert, J.P., Matter, N., Artault, J.C., Koppler, P. and Malviya, A.N. (1996) Inositol 1,4,5-trisphosphate receptor is located to the inner nuclear membrane vindicating regulation of nuclear calcium signalling by inositol 1,4,5-trisphosphate. Discrete distribution of inositol phosphate receptors to inner and outer nuclear membranes. J. Biol. Chem. 271, 5278-5287.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5278-5287
    • Humbert, J.P.1    Matter, N.2    Artault, J.C.3    Koppler, P.4    Malviya, A.N.5
  • 85
    • 0023810588 scopus 로고
    • An inositol tetrakisphosphate-containing phospholipid in activated neutrophils
    • Traynor-Kaplan, A.E., Harris, A.L., Thompson, B.L., Taylor, P. and Sklar, L.A. (1988) An inositol tetrakisphosphate-containing phospholipid in activated neutrophils. Nature 334, 353-356.
    • (1988) Nature , vol.334 , pp. 353-356
    • Traynor-Kaplan, A.E.1    Harris, A.L.2    Thompson, B.L.3    Taylor, P.4    Sklar, L.A.5
  • 86
    • 0024419434 scopus 로고
    • Polyphosphoinositides produced by phosphatidylinositol 3-kinase are poor substrates for phospholipases C from rat liver and bovine brain
    • Serunian, L.A., Haber, M.T., Fukui, T., Kim, J.W., Rhee, S.G., Lowenstein, J.M. and Cantley, L.C. (1989) Polyphosphoinositides produced by phosphatidylinositol 3-kinase are poor substrates for phospholipases C from rat liver and bovine brain. J. Biol. Chem. 264, 17809-17815.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17809-17815
    • Serunian, L.A.1    Haber, M.T.2    Fukui, T.3    Kim, J.W.4    Rhee, S.G.5    Lowenstein, J.M.6    Cantley, L.C.7
  • 87
    • 0025917376 scopus 로고
    • Novel polyphosphoinositides in cell growth and activation
    • Auger, K.R. and Cantley, L.C. (1991) Novel polyphosphoinositides in cell growth and activation. Cancer Cells 3, 263-269.
    • (1991) Cancer Cells , vol.3 , pp. 263-269
    • Auger, K.R.1    Cantley, L.C.2
  • 90
    • 0027309278 scopus 로고
    • Phospho-inositide 3-kinase is activated by phosphopeptides that bind to the SH2 domains of the 85 kDa subunit
    • Carpenter, C., Auger, K., Chanudhuri, M., Yoakim, M., Schaffhausen, B., Shoelson, S. and Cantley, L. (1993) Phospho-inositide 3-kinase is activated by phosphopeptides that bind to the SH2 domains of the 85 kDa subunit. J. Biol. Chem. 268, 9478-9483.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9478-9483
    • Carpenter, C.1    Auger, K.2    Chanudhuri, M.3    Yoakim, M.4    Schaffhausen, B.5    Shoelson, S.6    Cantley, L.7
  • 91
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein βγ subunits
    • Stephens, L., Smrcka, A., Cooke, F., Jackson, T., Sternwise, P. and Hawkins, P. (1994) A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein βγ subunits. Cell 77, 83-93.
    • (1994) Cell , vol.77 , pp. 83-93
    • Stephens, L.1    Smrcka, A.2    Cooke, F.3    Jackson, T.4    Sternwise, P.5    Hawkins, P.6
  • 93
    • 0025731596 scopus 로고
    • Pathway of phosphatidylinositol(3,4,5)-trisphosphate synthesis in activated neutrophils
    • Stephens, L.R., Hughes, K.T. and Irvine, R.F. (1991) Pathway of phosphatidylinositol(3,4,5)-trisphosphate synthesis in activated neutrophils. Nature 351, 33-39.
    • (1991) Nature , vol.351 , pp. 33-39
    • Stephens, L.R.1    Hughes, K.T.2    Irvine, R.F.3
  • 94
    • 0028892253 scopus 로고
    • 3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins
    • 3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins. Cell 83, 812-830.
    • (1995) Cell , vol.83 , pp. 812-830
    • Rameth, L.1    Chen, C.-S.2    Cantley, L.3
  • 97
    • 0029160069 scopus 로고
    • Protein kinase B (cAKT) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, B. and Coffer, P. (1995) Protein kinase B (cAKT) in phosphatidylinositol-3-OH kinase signal transduction. Nature 599-602.
    • (1995) Nature , pp. 599-602
    • Burgering, B.1    Coffer, P.2
  • 98
    • 0028986738 scopus 로고
    • Normal activation of P70 S6 kinase by insulin in cells overexpressing dominant negative 85 kD subunit of phosphoinosititde 3-kinase
    • Hara, K., Yonezawa, K., Sakaue, S., Kotani, K., Kotani, K., Kojima, A., Waterfield, M. and Kasuga, M. (1995) Normal activation of P70 S6 kinase by insulin in cells overexpressing dominant negative 85 kD subunit of phosphoinosititde 3-kinase. Biochem. Biophys. Res. Commun. 208, 735-741.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 735-741
    • Hara, K.1    Yonezawa, K.2    Sakaue, S.3    Kotani, K.4    Kotani, K.5    Kojima, A.6    Waterfield, M.7    Kasuga, M.8
  • 100
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate
    • Gilmore, A.P. and Burridge, K. (1996) Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Nature 381, 531-535.
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 101
    • 0029943493 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is an early intermediate in the G beta gamma-mediated mitogen-activated protein kinase signalling pathway
    • Hawes, B.E., Luttrell, L.M., van Biesen, T. and Lefkowitz, R.J. (1996) Phosphatidylinositol 3-kinase is an early intermediate in the G beta gamma-mediated mitogen-activated protein kinase signalling pathway. J. Biol. Chem. 271, 12133-12136.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12133-12136
    • Hawes, B.E.1    Luttrell, L.M.2    Van Biesen, T.3    Lefkowitz, R.J.4
  • 102
    • 0029808103 scopus 로고    scopus 로고
    • A functional phosphatidylinositol 3,4,5-trisphosphate/phosphoinositide binding domain in the clathrin adaptor AP-2 alpha subunit - Implications for the endocytic pathway
    • Gaidarov, I., Chen, Q., Falck, J.R., Reddy, K.K. and Keen, J.H. (1996) A functional phosphatidylinositol 3,4,5-trisphosphate/phosphoinositide binding domain in the clathrin adaptor AP-2 alpha subunit - implications for the endocytic pathway. J. Biol. Chem. 271, 20922-20929.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20922-20929
    • Gaidarov, I.1    Chen, Q.2    Falck, J.R.3    Reddy, K.K.4    Keen, J.H.5
  • 103
    • 0029899011 scopus 로고    scopus 로고
    • Phosphoinositides and phosphoinositide-utilizing enzymes in detergent-insoluble lipid domains
    • Hope, H.R. and Pike, L.J. (1996) Phosphoinositides and phosphoinositide-utilizing enzymes in detergent-insoluble lipid domains. Mol. Biol. Cell. 7, 843-851.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 843-851
    • Hope, H.R.1    Pike, L.J.2
  • 104
    • 0029086047 scopus 로고
    • A phosphatidylinositol 4,5-bisphosphate-sensitive casein kinase 1a associates with synaptic vesicles and phosphorylates a subset of vesicle proteins
    • Gross, S., Hoffman, D., Fisette, P., Baas, P. and Anderson, R. (1995) A phosphatidylinositol 4,5-bisphosphate-sensitive casein kinase 1a associates with synaptic vesicles and phosphorylates a subset of vesicle proteins. J. Cell. Biol. 130, 711-724.
    • (1995) J. Cell. Biol. , vol.130 , pp. 711-724
    • Gross, S.1    Hoffman, D.2    Fisette, P.3    Baas, P.4    Anderson, R.5
  • 105
    • 0029091623 scopus 로고
    • Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate - A comparison with protein kinase C isotypes
    • Palmer, R.H., Dekker, L.V., Woscholski, R., Legood, J.A., Gigg, R. and Parker, P.J. (1995) Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate - a comparison with protein kinase C isotypes. J. Biol. Chem. 270, 22412-22416.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22412-22416
    • Palmer, R.H.1    Dekker, L.V.2    Woscholski, R.3    Legood, J.A.4    Gigg, R.5    Parker, P.J.6
  • 106
    • 0027965240 scopus 로고
    • Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D
    • Liscovitch, M., Chalifa, V., Pertile, P., Chen, C.S. and Cantley, L.C. (1994) Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D. J. Biol. Chem. 269, 21403-21406.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21403-21406
    • Liscovitch, M.1    Chalifa, V.2    Pertile, P.3    Chen, C.S.4    Cantley, L.C.5
  • 108
    • 0028919213 scopus 로고
    • Inositol phosphate release and metabolism during myocardial ischemia and reperfusion in rat heart
    • Anderson, K., Dart, A. and Woodcock, E. (1995) Inositol phosphate release and metabolism during myocardial ischemia and reperfusion in rat heart. Circ. Res. 76, 261-268.
    • (1995) Circ. Res. , vol.76 , pp. 261-268
    • Anderson, K.1    Dart, A.2    Woodcock, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.