메뉴 건너뛰기




Volumn 116, Issue 1, 2011, Pages 116-127

Myosin light chain kinase / actin interaction in phorbol dibutyrate-stimulated smooth muscle cells

Author keywords

13 dibutyrate (PDBu); Actin remodeling; FRET analysis; Myosin light chain kinase (MLCK) deficient cell; Phorbol 12; Podosome

Indexed keywords

ALPHA ACTIN; BETA ACTIN; COMPLEMENTARY DNA; MYOSIN LIGHT CHAIN KINASE; PHORBOL DIBUTYRATE;

EID: 79956187556     PISSN: 13478613     EISSN: 13478648     Source Type: Journal    
DOI: 10.1254/jphs.10296FP     Document Type: Article
Times cited : (8)

References (44)
  • 3
    • 0027490560 scopus 로고
    • Spatial changes of [Ca2+]i and contraction caused by phorbol esters in vascular smooth muscle cells
    • Nakajima S, Fujimoto M, Ueda M. Spatial changes of [Ca2+]i and contraction caused by phorbol esters in vascular smooth muscle cells. Am J Physiol. 1993;265:C1138-C1145.
    • (1993) Am J Physiol , vol.265
    • Nakajima, S.1    Fujimoto, M.2    Ueda, M.3
  • 4
    • 0035895901 scopus 로고    scopus 로고
    • Dedicated myosin light chain kinase with diverse cellular functions
    • Kamm KE, Stull JT. Dedicated myosin light chain kinase with diverse cellular functions. J Biol Chem. 2001;276:4527-4530.
    • (2001) J Biol Chem , vol.276 , pp. 4527-4530
    • Kamm, K.E.1    Stull, J.T.2
  • 8
    • 0021894617 scopus 로고
    • The function of myosin and myosin light chain kinase phosphorylation in smooth muscle
    • Kamm KE, Stull JT. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Ann Rev Pharmacol Toxicol. 1985;25:593-620. (Pubitemid 15090995)
    • (1985) Annual Review of Pharmacology and Toxicology , vol.VOL. 25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 9
    • 0026778183 scopus 로고
    • A novel regulatory effect of myosin light chain kinase from smooth muscle on the ATP-dependent interaction between actin and myosin
    • Kohama K, Okagaki T, Hayakawa K, Lin Y, Ishikawa R, Shimmen T, et al. A novel regulatory effect of myosin light chain kinase from smooth muscle on the ATP-dependent interaction between actin and myosin. Biochem Biophys Res Commun. 1992;184:1204-1211.
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 1204-1211
    • Kohama, K.1    Okagaki, T.2    Hayakawa, K.3    Lin, Y.4    Ishikawa, R.5    Shimmen, T.6
  • 10
    • 0024330080 scopus 로고
    • Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase
    • Ito M, Dabrowska R, Guerriero UV, Hartshorne DJ. Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase. J Biol Chem. 1989;264:13971-13974. (Pubitemid 19214217)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.24 , pp. 13971-13974
    • Ito, M.1    Dabrowska, R.2    Guerriero Jr., V.3    Hartshorne, D.J.4
  • 11
    • 0035190054 scopus 로고    scopus 로고
    • Myosin light chain kinase as a multifunctional regulatory protein of smooth muscle contraction
    • DOI 10.1080/152165401753366087
    • Gao Y, Ye LH, Kishi H, Okagaki T, Samizo K, Nakamura A, et al. Myosin light chain kinase as a multifunctional regulatory protein of smooth muscle contraction. IUBMB Life. 2001;51: 337-344. (Pubitemid 33096653)
    • (2001) IUBMB Life , vol.51 , Issue.6 , pp. 337-344
    • Gao, Y.1    Ye, L.-H.2    Kishi, H.3    Okagaki, T.4    Samizo, K.5    Nakamura, A.6    Kohama, K.7
  • 12
    • 33644945032 scopus 로고    scopus 로고
    • Podosome as smart regulations of cellar adhesion
    • Spinardi L, Marchisio P. Podosome as smart regulations of cellar adhesion. Eur J Cell Biol. 2006;85:191-194.
    • (2006) Eur J Cell Biol , vol.85 , pp. 191-194
    • Spinardi, L.1    Marchisio, P.2
  • 13
    • 0036033308 scopus 로고    scopus 로고
    • Conventional protein kinase C mediates phorbol-dibutyrate-induced cytoskeletal remodeling in A7r5 smooth muscle cells
    • DOI 10.1006/excr.2002.5592
    • Hai CM, Hahne P, Harrington EO, Gimona M. Conventional PKC mediates phorbol dibutyrate-induced cytoskeletal remodeling in A7r5 smooth muscle cells. Exp Cell Res. 2002;280:64-74. (Pubitemid 35230368)
    • (2002) Experimental Cell Research , vol.280 , Issue.1 , pp. 64-74
    • Hai, C.-M.1    Hahne, P.2    Harrington, E.O.3    Gimona, M.4
  • 15
    • 0021687082 scopus 로고
    • Actin and tropomyosin variants in smooth muscles. Dependence on tissue type
    • Fatigati V, Murphy RA. Actin and tropomyosin variants in smooth muscles. Dependence on tissue types. J Biol Chem. 1984;259:14383-14388. (Pubitemid 15222253)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.23 , pp. 14383-14388
    • Fatigati, V.1    Murphy, R.A.2
  • 16
    • 0001068154 scopus 로고
    • Biochemistry of the contractile process in smooth muscle
    • Johnson L, editor. New York: Raven Press
    • Hartshorne DJ. Biochemistry of the contractile process in smooth muscle. In: Physiology of the gastrointestinal tract. Johnson L, editor. New York: Raven Press; 1987. p. 423-482.
    • (1987) Physiology of the Gastrointestinal Tract , pp. 423-482
    • Hartshorne, D.J.1
  • 18
    • 0016915065 scopus 로고
    • A simple method of preparing actin-free myosin from smooth muscle
    • Tokyo
    • Ebashi S. A simple method of preparing actin-free myosin from smooth muscle. J Biochem (Tokyo). 1976;79:229-231.
    • (1976) J Biochem , vol.79 , pp. 229-231
    • Ebashi, S.1
  • 19
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin- troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J, Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin- troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971;246:4866-4871.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.1    Watt, S.2
  • 20
    • 0018988232 scopus 로고
    • Heterogeneity of amino acid incorporation rate in adult skeletal muscle actin
    • Tokyo
    • Kohama K. Heterogeneity of amino acid incorporation rate in adult skeletal muscle actin. J Biochem (Tokyo). 1980;87:997-999.
    • (1980) J Biochem , vol.87 , pp. 997-999
    • Kohama, K.1
  • 21
    • 0019888289 scopus 로고
    • Purification and characterization of smooth muscle myosin light chain kinase
    • Adelstein RS, Klee CB. Purification and characterization of smooth muscle myosin light chain kinase. J Biol Chem. 1981;256:7501-7509.
    • (1981) J Biol Chem , vol.256 , pp. 7501-7509
    • Adelstein, R.S.1    Klee, C.B.2
  • 23
    • 0014829125 scopus 로고
    • An electrophoretic study of the low-molecular- weight components of myosin
    • Perrie WT, Perry SV. An electrophoretic study of the low-molecular- weight components of myosin. Biochem J. 1970;119:31-38.
    • (1970) Biochem J , vol.119 , pp. 31-38
    • Perrie, W.T.1    Perry, S.V.2
  • 24
    • 0025832505 scopus 로고
    • In vitro movement of actin filaments on gizzard smooth muscle myosin: Requirement of phosphorylation of myosin light chain and effects of tropomyosin and caldesmon
    • Tokyo
    • Okagaki T, Higashi-Fujime S, Ishikawa R, Takano-Ohmuro H, Kohama K. In vitro movement of actin filaments on gizzard smooth muscle myosin: requirement of phosphorylation of myosin light chain and effects of tropomyosin and caldesmon. J Biochem (Tokyo). 1991;109:858-866.
    • (1991) J Biochem , vol.109 , pp. 858-866
    • Okagaki, T.1    Higashi-Fujime, S.2    Ishikawa, R.3    Takano-Ohmuro, H.4    Kohama, K.5
  • 25
    • 0014949207 scopus 로고
    • Cleabage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleabage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0024565757 scopus 로고
    • Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon
    • Ishikawa R, Yamashiro S, Matusmura F. Different modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of rotective ability of troomyosins by 83-kDa nonmuscle caldesmon. J BiolChem. 1989;264:7490-7497. (Pubitemid 19119165)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.13 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 27
    • 0022497304 scopus 로고
    • The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate
    • Kodama T, Fukui K, Kometani K. The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate. J Biochem (Tokyo). 1986;99:1465-1472. (Pubitemid 16033517)
    • (1986) Journal of Biochemistry , vol.99 , Issue.5 , pp. 1465-1472
    • Kodama, T.1    Fukui, K.2    Kometani, K.3
  • 28
    • 0038352067 scopus 로고    scopus 로고
    • Troponin I inhibitory peptide suppresses the force generation in smooth muscle by directly interfering with cross-bridge formation
    • DOI 10.1016/S0006-291X(03)01170-7
    • Watanabe M, Yoshino Y, Morimoto S. Troponin I inhibitory peptide suppresses the force generation in smooth muscle by directly interfering with cross-bridge formation. Biochem Biophys Res Commun. 2003;307:236-240. (Pubitemid 36818859)
    • (2003) Biochemical and Biophysical Research Communications , vol.307 , Issue.2 , pp. 236-240
    • Watanabe, M.1    Yoshino, Y.2    Morimoto, S.3
  • 29
    • 0033695998 scopus 로고    scopus 로고
    • Agonist-induced isometric contraction of smooth muscle cell-populated collagen gel fiber
    • Oishi K, Itoh Y, Isshiki Y, Kai C, Takeda Y, Yamaura K, et al. Agonist-induced isometric contraction of smooth muscle cell-populated collagen gel fiber. Am J Physiol. 2000;279:C1432-C1442.
    • (2000) Am J Physiol , vol.279
    • Oishi, K.1    Itoh, Y.2    Isshiki, Y.3    Kai, C.4    Takeda, Y.5    Yamaura, K.6
  • 30
    • 0035542854 scopus 로고    scopus 로고
    • Molecular transporters for peptides: Delivery of a cardioprotective εPKC agonist peptide into cells and intact ischemic heart using a transport system, R7
    • Chen L, Wright LR, Che-Hong C, Oliver SF, Wender PA, Mochly-Rosen D. Molecular transporters for peptides: delivery of a cardioprotective εPKC agonist peptide into cells and intact ischemic heart using a transport system, R7. Chem Biol. 2001;8:1123-1129.
    • (2001) Chem Biol , vol.8 , pp. 1123-1129
    • Chen, L.1    Wright, L.R.2    Che-Hong, C.3    Oliver, S.F.4    Wender, P.A.5    Mochly-Rosen, D.6
  • 31
    • 44949206620 scopus 로고    scopus 로고
    • Blebbistatin inhibits the chemotaxis of vascular smooth muscle cells by disrupting the myosin II-actin interaction
    • Wang HH, Tanaka H, Qin X, Zhao T, Ye LH, Okagaki T, et al. Blebbistatin inhibits the chemotaxis of vascular smooth muscle cells by disrupting the myosin II-actin interaction. Am J Physiol Heart Circ Physiol. 2008;294:H2060-H2068.
    • (2008) Am J Physiol Heart Circ Physiol , vol.294
    • Wang, H.H.1    Tanaka, H.2    Qin, X.3    Zhao, T.4    Ye, L.H.5    Okagaki, T.6
  • 32
    • 77951482150 scopus 로고    scopus 로고
    • Blebbistatin, a myosin II inhibitor, suppresses contraction and disrupts contractile filaments organization of skinned taenia cecum from guinea pig
    • Watanabe M, Yumoto M, Tanaka H, Wang HH, Katayama T, Yoshiyama S, et al. Blebbistatin, a myosin II inhibitor, suppresses contraction and disrupts contractile filaments organization of skinned taenia cecum from guinea pig. Am J Physiol Cell Physiol. 2010;298:1118-1126.
    • (2010) Am J Physiol Cell Physiol , vol.298 , pp. 1118-1126
    • Watanabe, M.1    Yumoto, M.2    Tanaka, H.3    Wang, H.H.4    Katayama, T.5    Yoshiyama, S.6
  • 33
    • 66149105040 scopus 로고    scopus 로고
    • Nonkinase activity of MLCK in elongated filopodia formation and chemotaxis of vascular smooth muscle cells toward sphingosylphosphorylcholine
    • Wang HH, Nakamura A, Matsumoto A, Yoshiyama S, Qin X, Ye LH, et al. Nonkinase activity of MLCK in elongated filopodia formation and chemotaxis of vascular smooth muscle cells toward sphingosylphosphorylcholine. Am J Physiol Heart Circ Physiol. 2009;296:H1683-H1693.
    • (2009) Am J Physiol Heart Circ Physiol , vol.296
    • Wang, H.H.1    Nakamura, A.2    Matsumoto, A.3    Yoshiyama, S.4    Qin, X.5    Ye, L.H.6
  • 34
    • 0242678496 scopus 로고    scopus 로고
    • 2+ antagonist-insensitive coronary smooth muscle contraction involves activation of epsilon-protein kinase C-dependent pathway
    • 2+ antagonist-insensitive coronary smooth muscle contraction involves activation of epsilon-protein kinase C-dependent pathway. Am J Physiol. 2003;285:C1454-C1463.
    • (2003) Am J Physiol , vol.285
    • Dallas, A.1    Khalil, R.A.2
  • 35
    • 40849105174 scopus 로고    scopus 로고
    • Role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, a review dedicated to Dr. Setsuo Ebashi
    • Nakamura A, Xie C, Gao Y, Wang HH, Ye LH, Kishi H, et al. Role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, a review dedicated to Dr. Setsuo Ebashi. Biochem Biophys Res Commun. 2008;369:135-143.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 135-143
    • Nakamura, A.1    Xie, C.2    Gao, Y.3    Wang, H.H.4    Ye, L.H.5    Kishi, H.6
  • 37
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • DOI 10.1006/meth.2001.1189
    • Kenworthy A. Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods. 2001;24:289-296. (Pubitemid 32846434)
    • (2001) Methods , vol.24 , Issue.3 , pp. 289-296
    • Kenworthy, A.K.1
  • 38
    • 0023316741 scopus 로고
    • Fluorescence resonance energy transfer of distances in actin and myosin. A critical evaluation
    • Dos Remedios CG, Miki M, Barden J. Fluorescence resonance energy transfer of distances in actin and myosin. A critical evaluation. J Muscle Res Cell Motil. 1987;8:97-117.
    • (1987) J Muscle Res Cell Motil , vol.8 , pp. 97-117
    • Dos Remedios, C.G.1    Miki, M.2    Barden, J.3
  • 39
    • 0034441863 scopus 로고    scopus 로고
    • Remodeling of the actin cytoskeleton in the contracting A7r5 smooth muscle cell
    • DOI 10.1023/A:1010396429297
    • Fultz ME, Li C, Geng W, Wright GL. Remodeling of the actin cytoskeleton in the contracting A7r5 smooth muscle cell. J Muscle Res Cell Motil. 2000;21:775-787. (Pubitemid 32423412)
    • (2000) Journal of Muscle Research and Cell Motility , vol.21 , Issue.8 , pp. 775-787
    • Fultz, M.E.1    Li, C.2    Geng, W.3    Wright, G.L.4
  • 41
    • 0030866194 scopus 로고    scopus 로고
    • Mechanisms for the mechanical response of airway smooth muscle to length oscillation
    • Shen X, Wu M, Tepper R, Gunst S. Mechanisms for mechanical response of airway smooth muscle to length oscillation. J Appl Physiol. 1997;83:731-738. (Pubitemid 27392290)
    • (1997) Journal of Applied Physiology , vol.83 , Issue.3 , pp. 731-738
    • Shen, X.1    Wu, M.F.2    Tepper, R.S.3    Gunst, S.J.4
  • 42
    • 0031776844 scopus 로고    scopus 로고
    • Involvement of the cytoskeleton in calcium-dependent stress relaxation of rat aortic smooth muscle
    • DOI 10.1023/A:1005301821628
    • Wright GL, Battistella-Patterson AS. Involvement of the cytoskeleton in calcium-dependent stress relaxation of rat aortic smooth muscle. J Muscle Res Cell Motil. 1998;19:405-414. (Pubitemid 28253113)
    • (1998) Journal of Muscle Research and Cell Motility , vol.19 , Issue.4 , pp. 405-414
    • Wright, G.L.1    Battistella-Patterson, A.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.