메뉴 건너뛰기




Volumn 53, Issue 9, 1997, Pages 1239-1247

Effect of protein kinase inhibitors on activity of mammalian small heat- shock protein (HSP25) Kinase

Author keywords

Ehrlich ascites tumor cells; Heat shock protein; HSP25; Inhibitors; Phosphorylation; Protein serine threonine kinase

Indexed keywords

HEAT SHOCK PROTEIN; PROTEIN KINASE; PROTEIN KINASE INHIBITOR; QUERCETIN; STAUROSPORINE; TYRPHOSTIN;

EID: 0030739229     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(96)00877-5     Document Type: Article
Times cited : (35)

References (43)
  • 1
    • 0028832107 scopus 로고
    • Characterization of 45-kDa/54-kDa HSP27 kinase, a stress-sensitive kinase which may activate the phosphorylation-dependent protective function of mammalian 27-kDa heat-shock protein HSP27
    • Huot J, Lambert H, Lavoie JN, Guimond A, Houle F and Landry J, Characterization of 45-kDa/54-kDa HSP27 kinase, a stress-sensitive kinase which may activate the phosphorylation-dependent protective function of mammalian 27-kDa heat-shock protein HSP27. Eur J Biochem 227: 416-427, 1995.
    • (1995) Eur J Biochem , vol.227 , pp. 416-427
    • Huot, J.1    Lambert, H.2    Lavoie, J.N.3    Guimond, A.4    Houle, F.5    Landry, J.6
  • 2
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization inhibiting activity
    • Benndorf R, Hayess K, Ryazantsev S, Wieske M, Behlke J and Lutsch G, Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization inhibiting activity. J Biol Chem 269: 20780-20784, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6
  • 3
    • 0028924759 scopus 로고
    • Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27
    • Lavoie JN, Lambert H, Hickey E, Weber LA and Landry J, Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol Cell Biol 15: 505-516, 1995.
    • (1995) Mol Cell Biol , vol.15 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3    Weber, L.A.4    Landry, J.5
  • 4
    • 0027118212 scopus 로고
    • Cell-free phosphorylation of the murine small heat shock protein hsp25 by an endogenous kinase from Ehrlich ascites tumor cells
    • Benndorf R, Hayess K, Stahl J and Bielka H, Cell-free phosphorylation of the murine small heat shock protein hsp25 by an endogenous kinase from Ehrlich ascites tumor cells. Biochim Biophys Acta 1136: 203-207, 1992.
    • (1992) Biochim Biophys Acta , vol.1136 , pp. 203-207
    • Benndorf, R.1    Hayess, K.2    Stahl, J.3    Bielka, H.4
  • 5
    • 0027739284 scopus 로고
    • The substrate specificity and structure of mitogen-activated protein (MAP) kinase-activated protein kinase-2
    • Stokoe D, Caudwell B, Cohen PTW and Cohen P, The substrate specificity and structure of mitogen-activated protein (MAP) kinase-activated protein kinase-2. Biochemical J 296: 843-849, 1993.
    • (1993) Biochemical J , vol.296 , pp. 843-849
    • Stokoe, D.1    Caudwell, B.2    Cohen, P.T.W.3    Cohen, P.4
  • 6
    • 0027516631 scopus 로고
    • Interleukin 1 and tumor necrosis factor stimulate two novel protein kinases that phosphorylate the heat shock protein hsp27 and beta-casein
    • Guesdon F, Freshney N, Waller RJ, Rawlinson L and Saklatvala J, Interleukin 1 and tumor necrosis factor stimulate two novel protein kinases that phosphorylate the heat shock protein hsp27 and beta-casein. J Biol Chem 268: 4236-4243, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 4236-4243
    • Guesdon, F.1    Freshney, N.2    Waller, R.J.3    Rawlinson, L.4    Saklatvala, J.5
  • 8
    • 0027454318 scopus 로고
    • The MAP kinase-activated protein kinase 2 contains a proline-rich SH3-binding domain
    • Engel K, Plath K and Gaestel M, The MAP kinase-activated protein kinase 2 contains a proline-rich SH3-binding domain. FEBS Lett 336: 143-147, 1994.
    • (1994) FEBS Lett , vol.336 , pp. 143-147
    • Engel, K.1    Plath, K.2    Gaestel, M.3
  • 9
    • 0026457201 scopus 로고
    • Identification of MAPKAP kinase-2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins
    • Stokoe D, Engel K, Campbell DG, Cohen P and Gaestel M, Identification of MAPKAP kinase-2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett 313: 307-313, 1992.
    • (1992) FEBS Lett , vol.313 , pp. 307-313
    • Stokoe, D.1    Engel, K.2    Campbell, D.G.3    Cohen, P.4    Gaestel, M.5
  • 10
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse J, Cohen P, Trigon S, Morange M, Alonso-Llamazares A, Zamanillo D, Hunt T and Nebreda AR, A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell 78: 1027-1037, 1994.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso-Llamazares, A.5    Zamanillo, D.6    Hunt, T.7    Nebreda, A.R.8
  • 13
    • 0026047320 scopus 로고
    • Use of erbstatin as protein-tyrosine kinase inhibitor
    • Umezawa K and Imoto M, Use of erbstatin as protein-tyrosine kinase inhibitor. Methods Enzymol 201: 379-385, 1991.
    • (1991) Methods Enzymol , vol.201 , pp. 379-385
    • Umezawa, K.1    Imoto, M.2
  • 15
  • 16
    • 0026059319 scopus 로고
    • Pseudosubstrate-based peptide inhibitors
    • Kemp BE, Pearson RB and House C, Pseudosubstrate-based peptide inhibitors. Methods Enzymol 201: 287-316, 1991.
    • (1991) Methods Enzymol , vol.201 , pp. 287-316
    • Kemp, B.E.1    Pearson, R.B.2    House, C.3
  • 17
    • 0028875318 scopus 로고
    • Constitutive activation of mitogen-activated protein kinase-activated protein kinase 2 by mutation of phosphorylation sites and an A-helix motif
    • Engel K, Schultz H, Martin F, Kotlyarov A, Plath K, Hahn M, Heinemann U and Gaestel M, Constitutive activation of mitogen-activated protein kinase-activated protein kinase 2 by mutation of phosphorylation sites and an A-helix motif. J Biol Chem 270: 1-9, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 1-9
    • Engel, K.1    Schultz, H.2    Martin, F.3    Kotlyarov, A.4    Plath, K.5    Hahn, M.6    Heinemann, U.7    Gaestel, M.8
  • 18
    • 0023555557 scopus 로고
    • Protein kinase C contains a pseudo-substrate prototope in its regulatory domain
    • House C and Kemp BE, Protein kinase C contains a pseudo-substrate prototope in its regulatory domain. Science 238: 1726-1728, 1987.
    • (1987) Science , vol.238 , pp. 1726-1728
    • House, C.1    Kemp, B.E.2
  • 19
    • 0023932685 scopus 로고
    • Calcium/calmodulin-dependent protein kinase II. Characterization of distinct calmodulin binding and inhibitory domains
    • Payne ME, Fong YL, Ono T, Colbran RJ, Kemp BE, Soderling TR and Means AR, Calcium/calmodulin-dependent protein kinase II. Characterization of distinct calmodulin binding and inhibitory domains. J Biol Chem 263: 7190-7195, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 7190-7195
    • Payne, M.E.1    Fong, Y.L.2    Ono, T.3    Colbran, R.J.4    Kemp, B.E.5    Soderling, T.R.6    Means, A.R.7
  • 20
    • 0023664006 scopus 로고
    • Bagchi IC and Means AR, The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudo-substrate sequence
    • Kemp BE, Pearson RB, Guerriero V Jr, Bagchi IC and Means AR, The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudo-substrate sequence. J Biol Chem 262: 2542-2548, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 2542-2548
    • Kemp, B.E.1    Pearson, R.B.2    Guerriero V., Jr.3
  • 21
    • 0028883299 scopus 로고
    • Characterization of an auto-inhibitory domain in human mitogen-activated protein kinase-activated protein kinase-2
    • Zu YL, Ai YX and Huang CK, Characterization of an auto-inhibitory domain in human mitogen-activated protein kinase-activated protein kinase-2. J Biol Chem 270: 202-206, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 202-206
    • Zu, Y.L.1    Ai, Y.X.2    Huang, C.K.3
  • 22
    • 0023830647 scopus 로고
    • Growth phase-dependent proteins of the Ehrlich ascites tumor analyzed by one- and two-dimensional electrophoresis
    • Benndorf R, Nürnberg P and Bielka H, Growth phase-dependent proteins of the Ehrlich ascites tumor analyzed by one- and two-dimensional electrophoresis. Exp Cell Res 174: 130-138, 1988.
    • (1988) Exp Cell Res , vol.174 , pp. 130-138
    • Benndorf, R.1    Nürnberg, P.2    Bielka, H.3
  • 23
    • 0023811016 scopus 로고
    • Purification of the growth-related protein p25 of the Ehrlich ascites tumor and analysis of its isoforms
    • Benndorf R, Kraft R, Otto A, Stahl J, Böhm H and Bielka H, Purification of the growth-related protein p25 of the Ehrlich ascites tumor and analysis of its isoforms. Biochem Int 17: 225-234, 1988.
    • (1988) Biochem Int , vol.17 , pp. 225-234
    • Benndorf, R.1    Kraft, R.2    Otto, A.3    Stahl, J.4    Böhm, H.5    Bielka, H.6
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli UK, Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0020972355 scopus 로고
    • Assays of protein kinase
    • Roskoski R Jr, Assays of protein kinase. Methods Enzymol 99: 3-6, 1983.
    • (1983) Methods Enzymol , vol.99 , pp. 3-6
    • Roskoski R., Jr.1
  • 26
    • 0028129125 scopus 로고
    • Characterization of the proline-rich region of mouse MAPKAP kinase 2: Influence on catalytic properties and binding to the c-abl SH3 domain in vitro
    • Plath K, Engel K, Schwedersky G and Gaestel M, Characterization of the proline-rich region of mouse MAPKAP kinase 2: Influence on catalytic properties and binding to the c-abl SH3 domain in vitro. Biochem Biophys Res Commun 203: 1188-1194, 1994.
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 1188-1194
    • Plath, K.1    Engel, K.2    Schwedersky, G.3    Gaestel, M.4
  • 28
    • 0026570931 scopus 로고
    • Human hsp27 is phosphorylated by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II
    • Landry J, Lambert H, Zhou M, Lavoie JN, Hickey E, Weber LA and Anderson CW, Human hsp27 is phosphorylated by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II. J Biol Chem 267: 794-803, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 794-803
    • Landry, J.1    Lambert, H.2    Zhou, M.3    Lavoie, J.N.4    Hickey, E.5    Weber, L.A.6    Anderson, C.W.7
  • 30
    • 0025900919 scopus 로고
    • On the role of protein kinases in regulating neutrophil actin association with the cytoskeleton
    • Niggli V and Keller H, On the role of protein kinases in regulating neutrophil actin association with the cytoskeleton. J Biol Chem 266: 7927-7932, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 7927-7932
    • Niggli, V.1    Keller, H.2
  • 32
    • 0025305025 scopus 로고
    • KT5926, a potent and selective inhibitor of myosin light chain kinase
    • Nakanishi S, Yamada K, Iwahashi K, Kuroda K and Kase H, KT5926, a potent and selective inhibitor of myosin light chain kinase. Mol Pharmacol 37: 482-488, 1990.
    • (1990) Mol Pharmacol , vol.37 , pp. 482-488
    • Nakanishi, S.1    Yamada, K.2    Iwahashi, K.3    Kuroda, K.4    Kase, H.5
  • 34
    • 0026845466 scopus 로고
    • Inhibition of rat liver cyclic AMP-dependent protein kinase by flavonoids
    • Jinsart W, Ternai B and Polya GM, Inhibition of rat liver cyclic AMP-dependent protein kinase by flavonoids. Biol Chem Hoppe-Seyler 373: 205-211, 1992.
    • (1992) Biol Chem Hoppe-Seyler , vol.373 , pp. 205-211
    • Jinsart, W.1    Ternai, B.2    Polya, G.M.3
  • 35
    • 0021804387 scopus 로고
    • Partial purification and characterization of the calcium-dependent and phospholipid-dependent protein kinase C from chick oviduct
    • Horn F, Gschwendt M and Marks-F, Partial purification and characterization of the calcium-dependent and phospholipid-dependent protein kinase C from chick oviduct. Eur J Biochem 148: 533-538, 1985.
    • (1985) Eur J Biochem , vol.148 , pp. 533-538
    • Horn, F.1    Gschwendt, M.2    Marks, F.3
  • 36
    • 0020635362 scopus 로고
    • The effect of quercetin on the phosphorylation activity of the Rous sarcoma virus transforming gene product in vitro and in vivo
    • Graziani Y, Erikson E and Erikson RL, The effect of quercetin on the phosphorylation activity of the Rous sarcoma virus transforming gene product in vitro and in vivo. Eur J Biochem 135: 583-589, 1983.
    • (1983) Eur J Biochem , vol.135 , pp. 583-589
    • Graziani, Y.1    Erikson, E.2    Erikson, R.L.3
  • 37
    • 0027521388 scopus 로고
    • Purification and biochemical characterization of the protein kinase encoded by the US3 gene of herpes simplex virus type 2
    • Daikoku T, Yamashita Y, Tsurumi T, Maeno K and Nishiyama Y, Purification and biochemical characterization of the protein kinase encoded by the US3 gene of herpes simplex virus type 2. Virology 197: 685-694, 1993.
    • (1993) Virology , vol.197 , pp. 685-694
    • Daikoku, T.1    Yamashita, Y.2    Tsurumi, T.3    Maeno, K.4    Nishiyama, Y.5
  • 38
    • 0025077256 scopus 로고
    • Inhibition of protein kinase C by the tyrosine kinase inhibitor erbstatin
    • Bishop WR, Petrin J, Wang L, Ramesh U and Doll RJ, Inhibition of protein kinase C by the tyrosine kinase inhibitor erbstatin. Biochem Pharmacol 40: 2129-2135, 1990.
    • (1990) Biochem Pharmacol , vol.40 , pp. 2129-2135
    • Bishop, W.R.1    Petrin, J.2    Wang, L.3    Ramesh, U.4    Doll, R.J.5
  • 39
    • 0026458235 scopus 로고
    • Tyrphostins: Tyrosine kinase blockers as novel antiproliferative agents and dissectors of signal transduction
    • Levitzki A, Tyrphostins: Tyrosine kinase blockers as novel antiproliferative agents and dissectors of signal transduction. FASEB J 6: 3275-3281, 1992.
    • (1992) FASEB J , vol.6 , pp. 3275-3281
    • Levitzki, A.1
  • 40
    • 0024434810 scopus 로고
    • Tyrphostins I: Synthesis and biological activity of protein tyrosine kinase inhibitors
    • Gazit A, Yaish P, Gilon C and Levitzki A, Tyrphostins I: Synthesis and biological activity of protein tyrosine kinase inhibitors. J Med Chem 32: 2344-2352, 1989.
    • (1989) J Med Chem , vol.32 , pp. 2344-2352
    • Gazit, A.1    Yaish, P.2    Gilon, C.3    Levitzki, A.4
  • 41
    • 0025833550 scopus 로고
    • Tyrphostins: 2. Heterocyclic and alpha-substituted benzylidenemalononitrile tyrphostins as potent inhibitors of EGF receptor and ErbB2/neu tyrosine kinases
    • Gazit A, Osherov N, Posner I, Yaish P, Poradosu E, Gilon C and Levitzki A, Tyrphostins: 2. Heterocyclic and alpha-substituted benzylidenemalononitrile tyrphostins as potent inhibitors of EGF receptor and ErbB2/neu tyrosine kinases. J Med Chem 34: 1896-1907, 1991.
    • (1991) J Med Chem , vol.34 , pp. 1896-1907
    • Gazit, A.1    Osherov, N.2    Posner, I.3    Yaish, P.4    Poradosu, E.5    Gilon, C.6    Levitzki, A.7
  • 42
    • 0025158107 scopus 로고
    • Protein kinase recognition sequence motifs
    • Kemp BE and Pearson RB. Protein kinase recognition sequence motifs. Trends Biochem Sci 15: 342-346, 1990.
    • (1990) Trends Biochem Sci , vol.15 , pp. 342-346
    • Kemp, B.E.1    Pearson, R.B.2
  • 43
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton DR, Zheng J, Ten Eyck LF, Xuong N-H, Taylor SS and Sowadski JM, Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253: 414-420, 1991.
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Xuong, N.-H.4    Taylor, S.S.5    Sowadski, J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.