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Volumn 287, Issue 2 56-2, 2004, Pages

Distinct kinases are involved in contraction of cat esophageal and lower esophageal sphincter smooth muscles

Author keywords

Integrin linked kinase; Myosin light chain kinase; Phosphatase; Protein kinase C

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; CALCIUM ION; CALMODULIN; CHELERYTHRINE; CYANOGINOSIN LR; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MYOSIN LIGHT CHAIN KINASE; MYOSIN LIGHT CHAIN KINASE INHIBITOR; MYOSIN LIGHT CHAIN PHOSPHATASE; OKADAIC ACID; PHOSPHOTRANSFERASE; PROTEIN KINASE C EPSILON; PROTEIN SERINE THREONINE KINASE;

EID: 3242689795     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.00390.2003     Document Type: Article
Times cited : (26)

References (69)
  • 1
    • 0028120416 scopus 로고
    • The biochemical basis of the regulation of smooth muscular contraction
    • Allen BG and Walsh MP. The biochemical basis of the regulation of smooth muscular contraction. Trends Biochem Sci 19: 362-368, 1994.
    • (1994) Trends Biochem Sci , vol.19 , pp. 362-368
    • Allen, B.G.1    Walsh, M.P.2
  • 5
    • 0020085954 scopus 로고
    • Lower esophageal sphincter mechanics: Anatomic and physiologic relationships of the esophagogastric junction of the cat
    • Biancani P, Zabinski M, Kerstein M, and Behar J. Lower esophageal sphincter mechanics: anatomic and physiologic relationships of the esophagogastric junction of the cat. Gastroenterology 82: 468-475, 1982.
    • (1982) Gastroenterology , vol.82 , pp. 468-475
    • Biancani, P.1    Zabinski, M.2    Kerstein, M.3    Behar, J.4
  • 6
    • 0022930591 scopus 로고
    • 2+ mobilization by inositol 1,4,5-trisphosphate in isolated gastric smooth muscle cells
    • 2+ mobilization by inositol 1,4,5-trisphosphate in isolated gastric smooth muscle cells. J Biol Chem 261: 16591-16596, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 16591-16596
    • Bitar, K.N.1    Bradford, P.2    Putney, J.W.3    Makhlouf, G.M.4
  • 7
    • 0026550875 scopus 로고
    • Specific G proteins mediate endothelin induced contraction
    • Bitar KN, Stein S, and Omann G. Specific G proteins mediate endothelin induced contraction. Life Sci 50: 2119-2124, 1992.
    • (1992) Life Sci , vol.50 , pp. 2119-2124
    • Bitar, K.N.1    Stein, S.2    Omann, G.3
  • 8
    • 0031021875 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C-α on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state
    • Bornancin F and Parker PJ. Phosphorylation of protein kinase C-α on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state. J Biol Chem 272: 3544-3549, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 3544-3549
    • Bornancin, F.1    Parker, P.J.2
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • a. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0037169533 scopus 로고    scopus 로고
    • Phosphorylation of the myosin-binding subunit of myosin phosphatase by Raf-1 and inhibition of phosphatase activity
    • Broustas CG, Grammatikakis N, Eto M, Dent P, Brautigan DL, and Kasid U. Phosphorylation of the myosin-binding subunit of myosin phosphatase by Raf-1 and inhibition of phosphatase activity. J Biol Chem 277: 3053-3059, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 3053-3059
    • Broustas, C.G.1    Grammatikakis, N.2    Eto, M.3    Dent, P.4    Brautigan, D.L.5    Kasid, U.6
  • 11
    • 0038339485 scopus 로고    scopus 로고
    • MAPK mediates PKC-dependent contraction of cat esophageal and lower esophageal sphincter circular smooth muscle
    • 10.1152/ajpgi.00156.2002
    • Cao W, Sohn UD, Bitar KN, Behar J, Biancani P, and Harnett KM. MAPK mediates PKC-dependent contraction of cat esophageal and lower esophageal sphincter circular smooth muscle. Am J Physiol Gastrointest Liver Physiol 285: G86-G95, 2003; 10.1152/ajpgi.00156.2002.
    • (2003) Am J Physiol Gastrointest Liver Physiol , vol.285
    • Cao, W.1    Sohn, U.D.2    Bitar, K.N.3    Behar, J.4    Biancani, P.5    Harnett, K.M.6
  • 12
    • 0027379143 scopus 로고
    • Okadaic acid-sensitive protein phosphatases dephosphorylate MARKS, a major protein kinase C substrate
    • Clarke P, Siddhanti S, Cohen P, and Blackshear P. Okadaic acid-sensitive protein phosphatases dephosphorylate MARKS, a major protein kinase C substrate. FEBS Lett 336: 37-42, 1993.
    • (1993) FEBS Lett , vol.336 , pp. 37-42
    • Clarke, P.1    Siddhanti, S.2    Cohen, P.3    Blackshear, P.4
  • 13
    • 0024361302 scopus 로고
    • An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues
    • Cohen P, Klumpp S, and Schelling DL. An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues. FEBS Lett 250: 596-600, 1989.
    • (1989) FEBS Lett , vol.250 , pp. 596-600
    • Cohen, P.1    Klumpp, S.2    Schelling, D.L.3
  • 14
    • 0037109063 scopus 로고    scopus 로고
    • Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase
    • Deng JT, Sutherland C, Brautigan DL, Eto M, and Walsh MP. Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase. Biochem J 367: 517-524, 2002.
    • (2002) Biochem J , vol.367 , pp. 517-524
    • Deng, J.T.1    Sutherland, C.2    Brautigan, D.L.3    Eto, M.4    Walsh, M.P.5
  • 16
    • 0032585532 scopus 로고    scopus 로고
    • Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1)
    • Dutil E, Toker A, and Newton AC. Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1). Curr Biol 8: 1366-1375, 1998.
    • (1998) Curr Biol , vol.8 , pp. 1366-1375
    • Dutil, E.1    Toker, A.2    Newton, A.C.3
  • 18
    • 0033525860 scopus 로고    scopus 로고
    • Carboxyl-terminal phosphorylation regulates the function and subcellular localization of protein kinase C βII
    • Edwards AS, Faux MC, Scott JD, and Newton AC. Carboxyl-terminal phosphorylation regulates the function and subcellular localization of protein kinase C βII. J Biol Chem 274: 6461-6468, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 6461-6468
    • Edwards, A.S.1    Faux, M.C.2    Scott, J.D.3    Newton, A.C.4
  • 19
    • 0029583638 scopus 로고
    • A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization
    • Eto M, Ohmori T, Suzuki M, Furuya K, and Morita F. A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization. J Biochem (Tokyo) 118: 1104-1107, 1995.
    • (1995) J Biochem (Tokyo) , vol.118 , pp. 1104-1107
    • Eto, M.1    Ohmori, T.2    Suzuki, M.3    Furuya, K.4    Morita, F.5
  • 20
    • 0028075375 scopus 로고
    • Protein phosphatase activity against protein kinase C-phosphorylated substrates in human placenta
    • Eyster K, Waller M, Miller T, and Olon D. Protein phosphatase activity against protein kinase C-phosphorylated substrates in human placenta. Placenta 7: 721-732, 1994.
    • (1994) Placenta , vol.7 , pp. 721-732
    • Eyster, K.1    Waller, M.2    Miller, T.3    Olon, D.4
  • 21
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • a. Fabiato A and Fabiato F. Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J Physiol (Paris) 75: 463-505, 1979.
    • (1979) J Physiol (Paris) , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 22
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase
    • Feng J, Ito M, Ichikawa K, Isaka N, Nishikawa M, Hartshorne DJ, and Nakano T. Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J Biol Chem 274: 37385-37390, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 37385-37390
    • Feng, J.1    Ito, M.2    Ichikawa, K.3    Isaka, N.4    Nishikawa, M.5    Hartshorne, D.J.6    Nakano, T.7
  • 23
    • 0025331576 scopus 로고
    • Potent peptide inhibitors of smooth muscle myosin light chain kinase: Mapping of the pseudosubstrate and calmodulin binding domains
    • Foster CJ, Johnston SA, Sunday B, and Gaeta FC. Potent peptide inhibitors of smooth muscle myosin light chain kinase: mapping of the pseudosubstrate and calmodulin binding domains. Arch Biochem Biophys 280: 397-404, 1990.
    • (1990) Arch Biochem Biophys , vol.280 , pp. 397-404
    • Foster, C.J.1    Johnston, S.A.2    Sunday, B.3    Gaeta, F.C.4
  • 24
    • 0025353128 scopus 로고
    • Hepatic protein kinase-C and protein phosphatase type-2A in the fetal rat
    • Gruppuso PA. Hepatic protein kinase-C and protein phosphatase type-2A in the fetal rat. Pediatr Res 27: 599-603, 1990.
    • (1990) Pediatr Res , vol.27 , pp. 599-603
    • Gruppuso, P.A.1
  • 27
    • 0030475207 scopus 로고    scopus 로고
    • 12-O-tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase Ca correlates with the presence of a membrane-associated protein phosphatase 2A heterotrimer
    • Hansra G, Bornancin F, Whelan R, Hemmings BA, and Parker PJ. 12-O-tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase Ca correlates with the presence of a membrane-associated protein phosphatase 2A heterotrimer. J Biol Chem 271: 32785-32788, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 32785-32788
    • Hansra, G.1    Bornancin, F.2    Whelan, R.3    Hemmings, B.A.4    Parker, P.J.5
  • 28
    • 0033198916 scopus 로고    scopus 로고
    • Multisite dephosphorylation and desensitization of conventional protein kinase C isotypes
    • Hansra G, Garcia-Paramio P, Prevostel C, Whelan R, Bornancin F, and Parker P. Multisite dephosphorylation and desensitization of conventional protein kinase C isotypes. Biochem J 342: 337-344, 1999.
    • (1999) Biochem J , vol.342 , pp. 337-344
    • Hansra, G.1    Garcia-Paramio, P.2    Prevostel, C.3    Whelan, R.4    Bornancin, F.5    Parker, P.6
  • 29
    • 0001068154 scopus 로고
    • Biochemistry of the contractile process in smooth muscle
    • edited by Johnson LR. New York: Raven
    • Hartshorne DJ. Biochemistry of the contractile process in smooth muscle. In: Physiology of the Gastrointestinal Tract (2nd ed.), edited by Johnson LR. New York: Raven, 1987, p. 423-482.
    • (1987) Physiology of the Gastrointestinal Tract (2nd Ed.) , pp. 423-482
    • Hartshorne, D.J.1
  • 30
    • 0031798554 scopus 로고    scopus 로고
    • Myosin light chain phosphatase: Subunit composition, interactions and regulation
    • Hartshorne DJ, Ito M, and Erdodi F. Myosin light chain phosphatase: subunit composition, interactions and regulation. J Muscle Res Cell Motil 19: 325-341, 1998.
    • (1998) J Muscle Res Cell Motil , vol.19 , pp. 325-341
    • Hartshorne, D.J.1    Ito, M.2    Erdodi, F.3
  • 32
    • 0025327745 scopus 로고
    • Mode of inhibition of smooth muscle myosin light chain kinase by synthetic peptide analogs of the regulatory site
    • Ikebe M. Mode of inhibition of smooth muscle myosin light chain kinase by synthetic peptide analogs of the regulatory site. Biochem Biophys Res Commun 168: 714-720, 1990.
    • (1990) Biochem Biophys Res Commun , vol.168 , pp. 714-720
    • Ikebe, M.1
  • 33
    • 0035998334 scopus 로고    scopus 로고
    • Comparison of protein phosphatase inhibitory activity and apparent toxicity of microcystins and related compounds
    • Ito E, Takai A, Kondo F, Masui H, Imanishi S, and Harada K. Comparison of protein phosphatase inhibitory activity and apparent toxicity of microcystins and related compounds. Toxicon 40: 1017-1025, 2002.
    • (2002) Toxicon , vol.40 , pp. 1017-1025
    • Ito, E.1    Takai, A.2    Kondo, F.3    Masui, H.4    Imanishi, S.5    Harada, K.6
  • 34
    • 0035895901 scopus 로고    scopus 로고
    • Dedicated myosin light chain kinases with diverse cellular functions
    • Kamm KE and Stull JT. Dedicated myosin light chain kinases with diverse cellular functions. J Biol Chem 276: 4527-4530, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 4527-4530
    • Kamm, K.E.1    Stull, J.T.2
  • 35
    • 0029021180 scopus 로고
    • Phosphotyrosine-dependent targeting of mitogen-activated protein kinase in differentiated contractile vascular cells
    • Khalil RA, Menice CB, Wang CLA, and Morgan KG. Phosphotyrosine-dependent targeting of mitogen-activated protein kinase in differentiated contractile vascular cells. Circ Res 76: 1101-1108, 1995.
    • (1995) Circ Res , vol.76 , pp. 1101-1108
    • Khalil, R.A.1    Menice, C.B.2    Wang, C.L.A.3    Morgan, K.G.4
  • 36
    • 0027203852 scopus 로고
    • PKC-mediated redistribution of mitogen-activated protein kinase during smooth muscle cell activation
    • Khalil RA and Morgan KG. PKC-mediated redistribution of mitogen-activated protein kinase during smooth muscle cell activation. Am J Physiol Cell Physiol 265: C406-C411, 1993.
    • (1993) Am J Physiol Cell Physiol , vol.265
    • Khalil, R.A.1    Morgan, K.G.2
  • 37
    • 0031595416 scopus 로고    scopus 로고
    • Leukotriene D4-induced contraction of cat esophageal and lower esophageal sphincter circular smooth muscle
    • Kim N, Cao W, Song IS, Kim CY, Sohn UD, Harnett KM, and Biancani P. Leukotriene D4-induced contraction of cat esophageal and lower esophageal sphincter circular smooth muscle. Gastroenterology 115: 919-928, 1998.
    • (1998) Gastroenterology , vol.115 , pp. 919-928
    • Kim, N.1    Cao, W.2    Song, I.S.3    Kim, C.Y.4    Sohn, U.D.5    Harnett, K.M.6    Biancani, P.7
  • 39
    • 0033214346 scopus 로고    scopus 로고
    • 2+ sensitization in Triton X-100-demembranated rabbit arterial smooth muscle
    • 2+ sensitization in Triton X-100-demembranated rabbit arterial smooth muscle. J Physiol 520: 139-152, 1999.
    • (1999) J Physiol , vol.520 , pp. 139-152
    • Kitazawa, T.1    Takizawa, N.2    Ikebe, M.3    Eto, M.4
  • 42
    • 0034705765 scopus 로고    scopus 로고
    • Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase
    • Koyama M, Ito M, Feng J, Seko T, Shiraki K, Takase K, Hartshorne DJ, and Nakano T. Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase. FEBS Lett 475: 197-200, 2000.
    • (2000) FEBS Lett , vol.475 , pp. 197-200
    • Koyama, M.1    Ito, M.2    Feng, J.3    Seko, T.4    Shiraki, K.5    Takase, K.6    Hartshorne, D.J.7    Nakano, T.8
  • 43
    • 0027231429 scopus 로고
    • An okadaic acid-sensitive protein phosphatase counteracts protein kinase C-induced phosphorylation in SH-SY5Y cells
    • Larsson C, Alling C, and Simmonsson P. An okadaic acid-sensitive protein phosphatase counteracts protein kinase C-induced phosphorylation in SH-SY5Y cells. Cell Signal 3: 305-313, 1993.
    • (1993) Cell Signal , vol.3 , pp. 305-313
    • Larsson, C.1    Alling, C.2    Simmonsson, P.3
  • 44
    • 0031920581 scopus 로고    scopus 로고
    • Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle
    • Li L, Eto M, Lee MR, Morita F, Yazawa M, and Kitazawa T. Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle. J Physiol 508: 871-881, 1998.
    • (1998) J Physiol , vol.508 , pp. 871-881
    • Li, L.1    Eto, M.2    Lee, M.R.3    Morita, F.4    Yazawa, M.5    Kitazawa, T.6
  • 46
    • 0035970713 scopus 로고    scopus 로고
    • Dual Ser and Thr phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by MYPT-associated kinase
    • MacDonald JA, Eto M, Borman MA, Brautigan DL, and Haystead TA. Dual Ser and Thr phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by MYPT-associated kinase. FEBS Lett 493: 91-94, 2001.
    • (2001) FEBS Lett , vol.493 , pp. 91-94
    • MacDonald, J.A.1    Eto, M.2    Borman, M.A.3    Brautigan, D.L.4    Haystead, T.A.5
  • 47
    • 0030868556 scopus 로고    scopus 로고
    • Calponin and mitogen-activated protein kinase signaling in differentiated vascular smooth muscle
    • Menice CB, Hulvershorn J, Adam LP, Wang CLA, and Morgan KG. Calponin and mitogen-activated protein kinase signaling in differentiated vascular smooth muscle. J Biol Chem 272: 25157-25161, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 25157-25161
    • Menice, C.B.1    Hulvershorn, J.2    Adam, L.P.3    Wang, C.L.A.4    Morgan, K.G.5
  • 50
    • 0028811653 scopus 로고
    • Protein kinase C: Structure function and regulation
    • Newton A. Protein kinase C: structure function and regulation. J Biol Chem 270: 28495-28498, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 28495-28498
    • Newton, A.1
  • 51
    • 0035800862 scopus 로고    scopus 로고
    • 2+-free smooth muscle contraction via myosin light chain phosphorylation
    • 2+-free smooth muscle contraction via myosin light chain phosphorylation. J Biol Chem 276: 29567-29574, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 29567-29574
    • Niiro, N.1    Ikebe, M.2
  • 52
    • 2642569478 scopus 로고    scopus 로고
    • Direct association and translocation of PKC-α with calponin
    • First published January 15, 2004; 10.1152/ajpgi.00477.2003
    • Patil SB, Pawar MD, and Bitar KN. Direct association and translocation of PKC-α with calponin. Am J Physiol Gastrointest Liver Physiol 286: G954-G963, 2004. First published January 15, 2004; 10.1152/ajpgi.00477.2003.
    • (2004) Am J Physiol Gastrointest Liver Physiol , vol.286
    • Patil, S.B.1    Pawar, M.D.2    Bitar, K.N.3
  • 53
    • 0032993518 scopus 로고    scopus 로고
    • Identification of trimeric myosin phosphatase (PP1M) as a target for a novel PKC-potentiated protein phosphatase-1 inhibitory protein (CPI17) in porcine aorta smooth muscle
    • Senba S, Eto M, and Yazawa M. Identification of trimeric myosin phosphatase (PP1M) as a target for a novel PKC-potentiated protein phosphatase-1 inhibitory protein (CPI17) in porcine aorta smooth muscle. J Biochem (Tokyo) 125: 354-362, 1999.
    • (1999) J Biochem (Tokyo) , vol.125 , pp. 354-362
    • Senba, S.1    Eto, M.2    Yazawa, M.3
  • 54
    • 0036721270 scopus 로고    scopus 로고
    • The signal transduction of endothelin-1-induced circular smooth muscle cell contraction in cat esophagus
    • Shin CY, Lee YP, Lee TS, Je HD, Kim DS, and Sohn UD. The signal transduction of endothelin-1-induced circular smooth muscle cell contraction in cat esophagus. J Pharmacol Exp Ther 302: 924-934, 2002.
    • (2002) J Pharmacol Exp Ther , vol.302 , pp. 924-934
    • Shin, C.Y.1    Lee, Y.P.2    Lee, T.S.3    Je, H.D.4    Kim, D.S.5    Sohn, U.D.6
  • 55
    • 0036830407 scopus 로고    scopus 로고
    • 2-ceramide-induced circular smooth muscle cell contraction involves PKC-ε and p44/p42 MAPK activation in cat oesophagus
    • 2-ceramide- induced circular smooth muscle cell contraction involves PKC-ε and p44/p42 MAPK activation in cat oesophagus. Cell Signal 14: 925-932, 2002.
    • (2002) Cell Signal , vol.14 , pp. 925-932
    • Shin, C.Y.1    Lee, Y.P.2    Lee, T.S.3    Song, H.J.4    Sohn, U.D.5
  • 57
    • 0027723664 scopus 로고
    • Distinct muscarinic receptors, G-proteins, and phospholipases in esophageal and lower esophageal sphincter circular muscle
    • Sohn UD, Harnett KM, De Petris G, Behar J, and Biancani P. Distinct muscarinic receptors, G-proteins, and phospholipases in esophageal and lower esophageal sphincter circular muscle. J Pharmacol Exp Ther 267: 1205-1214, 1993.
    • (1993) J Pharmacol Exp Ther , vol.267 , pp. 1205-1214
    • Sohn, U.D.1    Harnett, K.M.2    De Petris, G.3    Behar, J.4    Biancani, P.5
  • 58
    • 0000207414 scopus 로고    scopus 로고
    • Different PKC isozymes mediate lower esophageal sphincter (LES) tone and phasic contraction of esophageal (ESO) circular smooth muscle in the cat
    • Sohn UD, Zoukhri D, Dartt D, Sergheraert C, Harnett KM, Behar J, and Biancani P. Different PKC isozymes mediate lower esophageal sphincter (LES) tone and phasic contraction of esophageal (ESO) circular smooth muscle in the cat. Mol Pharmacol 51: 462-470, 1997.
    • (1997) Mol Pharmacol , vol.51 , pp. 462-470
    • Sohn, U.D.1    Zoukhri, D.2    Dartt, D.3    Sergheraert, C.4    Harnett, K.M.5    Behar, J.6    Biancani, P.7
  • 59
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo AP and Somlyo AV. Signal transduction and regulation in smooth muscle. Nature 372: 231-236, 1994.
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 60
    • 0034650714 scopus 로고    scopus 로고
    • Signal transduction by G-proteins, rhokinase and protein phosphatase to smooth muscle and non-muscle myosin II
    • Somlyo AP and Somlyo AV. Signal transduction by G-proteins, rhokinase and protein phosphatase to smooth muscle and non-muscle myosin II. J Physiol 522: 177-185, 2000.
    • (2000) J Physiol , vol.522 , pp. 177-185
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 61
    • 0023648079 scopus 로고
    • Smooth muscle myosin phosphatase inhibition and force enforcement by black sponge toxin
    • Takai A, Bialojan C, Troschla M, and Ruegg J. Smooth muscle myosin phosphatase inhibition and force enforcement by black sponge toxin. FEBS Lett 217: 81-84, 1987.
    • (1987) FEBS Lett , vol.217 , pp. 81-84
    • Takai, A.1    Bialojan, C.2    Troschla, M.3    Ruegg, J.4
  • 62
    • 0028950664 scopus 로고
    • Inhibition of specific binding of okadaic acid to protein phosphatase 2A by microcystin-LR, calyculin-A and tautomycin: Method of analysis of interactions of tight-binding ligands with target protein
    • Takai A, Saaki K, Nagai H, Mieskes G, Isobe K, Isono K, and Yasumoto T. Inhibition of specific binding of okadaic acid to protein phosphatase 2A by microcystin-LR, calyculin-A and tautomycin: method of analysis of interactions of tight-binding ligands with target protein. Biochem J 306: 657-665, 1995.
    • (1995) Biochem J , vol.306 , pp. 657-665
    • Takai, A.1    Saaki, K.2    Nagai, H.3    Mieskes, G.4    Isobe, K.5    Isono, K.6    Yasumoto, T.7
  • 63
    • 0028966935 scopus 로고
    • Regulation of sequence-specific DNA binding function of p53 by PKC and protein phosphatases
    • Takenaka I, Morin F, Seizinger B, and Kley N. Regulation of sequence-specific DNA binding function of p53 by PKC and protein phosphatases. J Biol Chem 270: 5405-5411, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 5405-5411
    • Takenaka, I.1    Morin, F.2    Seizinger, B.3    Kley, N.4
  • 64
    • 0025195356 scopus 로고
    • Phosphorylation of high-Mr caldesmon by protein kinase C modulates the regulatory function of this protein on the interaction between actin and myosin
    • Tanaka T, Ohta H, Kanda K, Tanaka T, Hidaka H, and Sobue K. Phosphorylation of high-Mr caldesmon by protein kinase C modulates the regulatory function of this protein on the interaction between actin and myosin. Eur J Biochem 188: 495-500, 1990.
    • (1990) Eur J Biochem , vol.188 , pp. 495-500
    • Tanaka, T.1    Ohta, H.2    Kanda, K.3    Tanaka, T.4    Hidaka, H.5    Sobue, K.6
  • 66
    • 0033134836 scopus 로고    scopus 로고
    • 2+-independent phosphorylation of myosin in rat caudal artery and chicken gizzard myofilaments
    • 2+-independent phosphorylation of myosin in rat caudal artery and chicken gizzard myofilaments. J Physiol 516: 805-824, 1999.
    • (1999) J Physiol , vol.516 , pp. 805-824
    • Weber, L.P.1    Van Lierop, J.E.2    Walsh, M.P.3
  • 67
    • 0031135506 scopus 로고    scopus 로고
    • Inhibition of ERK activation attenuates endothelin-stimulated airway smooth muscle cell proliferation
    • Whelchel A, Evans J, and Posada J. Inhibition of ERK activation attenuates endothelin-stimulated airway smooth muscle cell proliferation. Am J Respir Cell Mol Biol 16: 589-596, 1997.
    • (1997) Am J Respir Cell Mol Biol , vol.16 , pp. 589-596
    • Whelchel, A.1    Evans, J.2    Posada, J.3
  • 68
    • 0025348420 scopus 로고
    • Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation
    • Winder SJ and Walsh MP. Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation. J Biol Chem 265: 10148-10155, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 10148-10155
    • Winder, S.J.1    Walsh, M.P.2
  • 69
    • 0028863441 scopus 로고
    • Activation of MAP kinase and translocation with HSP27 in bombesin-induced contraction of rectosigmoid smooth muscle
    • Yamada H, Strahler J, Welsh MJ, and Bitar KN. Activation of MAP kinase and translocation with HSP27 in bombesin-induced contraction of rectosigmoid smooth muscle. Am J Physiol Gastrointest Liver Physiol 269: G683-G691, 1995.
    • (1995) Am J Physiol Gastrointest Liver Physiol , vol.269
    • Yamada, H.1    Strahler, J.2    Welsh, M.J.3    Bitar, K.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.