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Volumn 324, Issue 4, 2004, Pages 1406-1412

Inhibition of wortmannin activities by amino compounds

Author keywords

Amino compound; Catecholamine secretion; Chromaffin cell; Myosin light chain kinase; Phosphoinositide 3 kinase; PI3K; Wortmannin

Indexed keywords

ACETIC ACID; ASPARTIC ACID; BUFFER; CATECHOLAMINE; CHOLINE; GLUTAMIC ACID; GLYCINE; GLYCINE DERIVATIVE; ISETHIONIC ACID; LYSINE; PHOSPHATIDYLINOSITOL 3 KINASE; SODIUM CHLORIDE; SODIUM DERIVATIVE; WORTMANNIN; AMINE; AMINO ACID; ANDROSTANE DERIVATIVE; ENZYME INHIBITOR; TROMETAMOL;

EID: 14344254476     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.09.200     Document Type: Article
Times cited : (6)

References (19)
  • 1
    • 0042734621 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase signalling-which way to target?
    • M.P. Wymann, M. Zvelebil, and M. Laffargue Phosphoinositide 3-kinase signalling-which way to target? Trends Pharmacol. Sci. 24 2003 366 376
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 366-376
    • Wymann, M.P.1    Zvelebil, M.2    Laffargue, M.3
  • 4
    • 0030051454 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitor wortmannin blocks mast cell exocytosis but not IL-6 production
    • D.L. Marquardt, J.L. Alongi, and L.L. Walker The phosphatidylinositol 3-kinase inhibitor wortmannin blocks mast cell exocytosis but not IL-6 production J. Immunol. 156 1996 1942 1945
    • (1996) J. Immunol. , vol.156 , pp. 1942-1945
    • Marquardt, D.L.1    Alongi, J.L.2    Walker, L.L.3
  • 5
    • 0027374488 scopus 로고
    • Inhibition of histamine secretion by wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells
    • H. Yano, S. Nakanishi, K. Kimura, N. Hanai, Y. Saitoh, Y. Fukui, Y. Nonomura, and Y. Matsuda Inhibition of histamine secretion by wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells J. Biol. Chem. 268 1993 25846 25856
    • (1993) J. Biol. Chem. , vol.268 , pp. 25846-25856
    • Yano, H.1    Nakanishi, S.2    Kimura, K.3    Hanai, N.4    Saitoh, Y.5    Fukui, Y.6    Nonomura, Y.7    Matsuda, Y.8
  • 6
    • 0032860589 scopus 로고    scopus 로고
    • Inhibition of quantal release from motor nerve by wortmannin
    • S.J. Hong, and C.C. Chang Inhibition of quantal release from motor nerve by wortmannin Br. J. Pharmacol. 128 1999 142 148
    • (1999) Br. J. Pharmacol. , vol.128 , pp. 142-148
    • Hong, S.J.1    Chang, C.C.2
  • 7
    • 0028135465 scopus 로고
    • Essential role of myosin light chain kinase in the mechanism for MgATP-dependent priming of exocytosis in adrenal chromaffin cells
    • K. Kumakura, K. Sasaki, T. Sakurai, M. Ohara Imaizumi, H. Misonou, S. Nakamura, Y. Matsuda, and Y. Nonomura Essential role of myosin light chain kinase in the mechanism for MgATP-dependent priming of exocytosis in adrenal chromaffin cells J. Neurosci. 14 1994 7695 7703
    • (1994) J. Neurosci. , vol.14 , pp. 7695-7703
    • Kumakura, K.1    Sasaki, K.2    Sakurai, T.3    Ohara Imaizumi, M.4    Misonou, H.5    Nakamura, S.6    Matsuda, Y.7    Nonomura, Y.8
  • 8
    • 0034644760 scopus 로고    scopus 로고
    • Mechanism of wortmannin-induced inhibition of secretory responses in rat adrenal medullary cells
    • A. Warashina Mechanism of wortmannin-induced inhibition of secretory responses in rat adrenal medullary cells Life Sci. 67 2000 2587 2593
    • (2000) Life Sci. , vol.67 , pp. 2587-2593
    • Warashina, A.1
  • 9
    • 0028340625 scopus 로고
    • 2+/calmodulin-dependent protein kinase in isolated bovine adrenal medullary cells
    • 2+/calmodulin- dependent protein kinase in isolated bovine adrenal medullary cells J. Pharmacol. Exp. Ther. 270 1994 104 110
    • (1994) J. Pharmacol. Exp. Ther. , vol.270 , pp. 104-110
    • Isosaki, M.1    Minami, N.2    Nakashima, T.3
  • 10
    • 0025955689 scopus 로고
    • Role of protein kinase C in catecholamine secretion from digitonin-permeabilized bovine adrenal medullary cells
    • M. Isosaki, T. Nakashima, and Y. Kurogochi Role of protein kinase C in catecholamine secretion from digitonin-permeabilized bovine adrenal medullary cells J. Biol. Chem. 266 1991 16703 16707
    • (1991) J. Biol. Chem. , vol.266 , pp. 16703-16707
    • Isosaki, M.1    Nakashima, T.2    Kurogochi, Y.3
  • 11
    • 0000010463 scopus 로고
    • The chemical estimation of adrenaline-like substances in blood
    • H. Weil-Malherbe, and A.D. Bone The chemical estimation of adrenaline-like substances in blood Biochem. J. 51 1952 311 318
    • (1952) Biochem. J. , vol.51 , pp. 311-318
    • Weil-Malherbe, H.1    Bone, A.D.2
  • 12
    • 0029965452 scopus 로고    scopus 로고
    • Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction
    • M.P. Wymann, G. Bulgarelli Leva, M.J. Zvelebil, L. Pirola, B. Vanhaesebroeck, M.D. Waterfield, and G. Panayotou Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction Mol. Cell. Biol. 16 1996 1722 1733
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1722-1733
    • Wymann, M.P.1    Bulgarelli Leva, G.2    Zvelebil, M.J.3    Pirola, L.4    Vanhaesebroeck, B.5    Waterfield, M.D.6    Panayotou, G.7
  • 13
    • 0030920653 scopus 로고    scopus 로고
    • Lipid kinase and protein kinase activities of G-protein-coupled phosphoinositide 3-kinase gamma: Structure-activity analysis and interactions with wortmannin
    • S. Stoyanova, G. Bulgarelli Leva, C. Kirsch, T. Hanck, R. Klinger, R. Wetzker, and M.P. Wymann Lipid kinase and protein kinase activities of G-protein-coupled phosphoinositide 3-kinase gamma: structure-activity analysis and interactions with wortmannin Biochem. J. 324 1997 489 495
    • (1997) Biochem. J. , vol.324 , pp. 489-495
    • Stoyanova, S.1    Bulgarelli Leva, G.2    Kirsch, C.3    Hanck, T.4    Klinger, R.5    Wetzker, R.6    Wymann, M.P.7
  • 14
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • E.H. Walker, M.E. Pacold, O. Perisic, L. Stephens, P.T. Hawkins, M.P. Wymann, and R.L. Williams Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine Mol. Cell 6 2000 909 919
    • (2000) Mol. Cell , vol.6 , pp. 909-919
    • Walker, E.H.1    Pacold, M.E.2    Perisic, O.3    Stephens, L.4    Hawkins, P.T.5    Wymann, M.P.6    Williams, R.L.7
  • 15
    • 0033856462 scopus 로고    scopus 로고
    • PI3-kinase inhibition: A target for drug development?
    • R.C. Stein, and M.D. Waterfield PI3-kinase inhibition: a target for drug development? Mol. Med. Today 6 2000 347 357
    • (2000) Mol. Med. Today , vol.6 , pp. 347-357
    • Stein, R.C.1    Waterfield, M.D.2
  • 16
    • 0018254448 scopus 로고
    • Calcium-dependent exocytosis in bovine adrenal medullary cells with leaky plasma membranes
    • P.F. Baker, and D.E. Knight Calcium-dependent exocytosis in bovine adrenal medullary cells with leaky plasma membranes Nature 276 1978 620 622
    • (1978) Nature , vol.276 , pp. 620-622
    • Baker, P.F.1    Knight, D.E.2
  • 17
    • 0024405467 scopus 로고
    • Kinetics and stoichiometry of coupled Na efflux and Ca influx (Na/Ca exchange) in barnacle muscle cells
    • H. Rasgado Flores, E.M. Santiago, and M.P. Blaustein Kinetics and stoichiometry of coupled Na efflux and Ca influx (Na/Ca exchange) in barnacle muscle cells J. Gen. Physiol. 93 1989 1219 1241
    • (1989) J. Gen. Physiol. , vol.93 , pp. 1219-1241
    • Rasgado Flores, H.1    Santiago, E.M.2    Blaustein, M.P.3
  • 18
    • 0023713760 scopus 로고
    • Intracellular acidosis of identified leech neurones produced by substitution of external sodium
    • J.W. Deitmer, and W.R. Schlue Intracellular acidosis of identified leech neurones produced by substitution of external sodium Brain Res. 462 1988 233 241
    • (1988) Brain Res. , vol.462 , pp. 233-241
    • Deitmer, J.W.1    Schlue, W.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.