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References
Hansen, C.A.; Mah, S.; Williamson, J.R.: Formation and metabolism of inositol 1,3,4,5-tetrakisphosphate in liver. J. Biol. Chem., 261, 8100–8103 (1986)
Irvine, R.F.; Letcher, A.J.; Heslop, J.P.; Berridge, M.J.: The inositol tris/tetra-kisphosphate pathway-demonstration of Ins(l,4,5)P3 3-kinase activity in animal tissues. Nature, 320, 631–634 (1986)
Communi, D.; Vanweyenberg, V.; Erneux, C: Purification and biochemical properties of a high-molecular-mass inositol 1, 4,5-trisphosphate 3-kinase isoenzyme in human platelets. Biochem. J., 298, 669–673 (1994)
Lin, A.; Wallace, R.W; Barnes, S.: Purification and properties of a human platelet inositol 1,4,5-trisphosphate 3-kinase. Arch. Biochem. Biophys., 303, 412–420 (1993)
Johanson, R.A.; Hansen, C.A.; Williamson, J.R.: Purification of D-myo-ino-sitol 1,4,5-trisphosphate 3-kinase from rat brain. J. Biol. Chem., 263, 7465–7471 (1988)
Lee, S.Y.; Sim, S.S.; Kim, J.W; Moon, K.H.; Kim, J.H.; Rhee, S.G.: Purification and properties of D-myo-inositol 1,4,5-trisphosphate 3-kinase from rat brain. Susceptibility to calpain. J. Biol. Chem., 265, 9434–9440 (1990)
Takazawa, K.; Lemos, M.; Delvaux, A.; Leieune, C; Dumont, J.E.; Erneux, C: Rat brain inositol 1,4,5-trisphosphate 3-kinase. Ca2+-sensitivity, purification and antibody production. Biochem. J., 268, 213–217 (1990)
Takazawa, K.; Passareiro, H.; Dumont, J.E.; Erneux, C: Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase in rat and bovine brain tissues. Biochem. Biophys. Res. Commun., 153, 632–641 (1988)
Biden, T.J.; Comte, M.; Cox, J.A.; Wollheim, C.B.: Calcium-calmodulin stimulates inositol 1,4,5-trisphosphate kinase activity from insulin-secreting RINmSF cells. J. Biol. Chem., 262, 9437–9440 (1987)
Takazawa, K.; Erneux, C: Inhibition of inositol 1,4,5-trisphosphate by heparin: basal and Ca2+/calmodulin-stimulated activity. Biochem. J., 261, 1059 (1989)
Takazawa, K.; Passareiro, H.; Dumont, J.E.; Erneux, C: Purification of bovine brain inositol 1,4,5-trisphosphate 3-kinase. Identification of the enzyme by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Biochem. J., 261, 483–488 (1989)
Yamaguchi, K.; Hirata, M.; Kuriyama, H.: Purification and characterization of inositol 1,4,5-trisphosphate 3-kinase from pig aortic smooth muscle. Biochem. J., 251, 129–134 (1988)
Yamaguchi, K.; Hirata, M.; Kuriyama, H.: Calmodulin activates inositol 1,4,5-trisphosphate 3-kinase activity in pig aortic smooth muscle. Biochem. J., 244, 787–791 (1987)
Morris, A.J.; Downes, C.P.; Harden, T.K.; Michell, R.H.: Turkey erythrocytes possess a membrane-associated inositol 1,4,5-trisphosphate 3-kinase that is activated by Ca2+ in the presence of calmodulin. Biochem. J., 248, 489–493 (1987)
Kimura, Y.; Hirata, M.; Yamaguchi, K.; Koga, T.: Activation by calmodulin of inositol-l,4,5-trisphosphate 3-kinase in guinea pig peritoneal macrophages. Arch. Biochem. Biophys., 257, 363–369 (1987)
Collin, T.: Serotonin induces an increase in D-myo-inositol (l,4,5)-trisphos-phate 3-kinase activity in rat brainstem slices. Neurosci. Lett., 255, 67–70 (1998)
Carrasco, M.A.; Figueroa, S.: Inositol 1,4,5-trisphosphate 3-kinase activity in frog skeletal muscle. Comp. Biochem. Physiol. B, 110, 747–753 (1995)
Choi, G.; Chang, Y.-T.; Chung, S.-K.; Choi, K.Y.: Molecular interactions of all possible regioisomers of synthetic myo-inositol phosphates with inositol 1,4,5-trisphosphate 3-kinase. Bioorg. Med. Chem. Lett, 7, 2709–2714 (1997)
Shin, Y.S.; Choi, G.; Choi, K.Y.: Overexpression, purification and characterization of inositol 1,4,5-triphosphate 3-kinase from rat brain. Mol. Cells, 5, 348–353 (1995)
Wang, X.-L.; Akhtar, R.A.; Abdel-Latif, A.A.: Purification and properties of D-myo-inositol 1,4,5-trisphosphate 3-kinase from bovine iris sphincter smooth muscle: effects of protein phosphorylation in vitro and in intact muscle. Biochem. J., 308(Pt 3), 1009–1016 (1995)
Vanweyenberg, V.; Communi, D.; D’Santos, C.S.; Erneux, C: Tissue-and cell-specific expression of Ins(l,4,5)P3 3-kinase isoenzymes. Biochem. J., 306 (Pt 2), 429–435 (1995)
Irvine, R.F.; Schell, M.J.: Back in the water: The return of the inositol phosphates. Nat. Rev. Mol. Cell Biol, 2, 327–338 (2001)
Takazawa, K.; Go, M.; Endo, T.; Erneux, C; Onaya, T.: Inositol 1,4,5-trisphosphate 3-kinase activity in FRTL-5 cells: regulation of the enzyme activity by TSH. J. Endocrinol, 144, 527–532 (1995)
Hague, E; Matifat, E; Brule, G.; Collin, T.: The inositol (l,4,5)-trisphosphate 3-kinase of Xenopus oocyte is activated by CaMKII and involved in the regulation of InsP3-mediated Ca2+ release. FEBS Lett, 449, 71–74 (1999)
Dewaste, V.; Moreau, C; De Smedt, E; Bex, E; De Smedt, H.; Wuytack, E; Missiaen, L.; Erneux, C: The three isoenzymes of human inositol-1,4,5-trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in COS-7 cells. Biochem. J., 374 41–49 (2003)
Communi, D.; Vanweyenberg, V.; Erneux, C: D-myo-inositol 1,4,5-trisphosphate 3-kinase A is activated by receptor activation through a calciumxal-modulin-dependent protein kinase II phosphorylation mechanism. EMBO J., 16, 1943–1952 (1997)
Millard, T.H.; Cullen, P.J.; Banting, G.: Effects of elevated expression of inositol 1,4,5-trisphosphate 3-kinase B on Ca2+ homoeostasis in HeLa cells. Biochem. J., 352 (Pt 3), 709–715 (2000)
Communi, D.; Dewaste, V.; Erneux, C: Calcium-calmodulin-dependent protein kinase II and protein kinase C-mediated phosphorylation and activation of D-myo-inositol 1,4, 5-trisphosphate 3-kinase B in astrocytes. J. Biol. Chem., 274, 14734–14742 (1999)
Woodring, P.J.; Garrison, J.C.: Expression, purification, and regulation of two isoforms of the inositol 1,4,5-trisphosphate 3-kinase. J. Biol. Chem., 272, 30447–30454 (1997)
Schell, M.J.; Erneux, C; Irvine, R.E: Inositol bd1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus. J. Biol. Chem., 276, 37537–37546 (2001)
Nalaskowski, M.M.; Bertsch, U.; Fanick, W.; Stockebrand, M.C.; Schmale, H.; Mayr, G.W.: Rat inositol 1,4,5-trisphosphate 3-kinase C is enzymatically specialized for basal cellular inositol trisphosphate phosphorylation and shuttles actively between nucleus and cytoplasm. J. Biol. Chem., 278, 19765–19776 (2003)
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(2007). Inositol-trisphosphate 3-kinase. In: Schomburg, D., Scomburg, I., Chang, A. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 37. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-47818-8_15
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