메뉴 건너뛰기




Volumn 298, Issue 2, 2010, Pages

Stimulatory effects of arachidonic acid on myosin ATPase activity and contraction of smooth muscle via myosin motor domain

Author keywords

Skinned fiber

Indexed keywords

ACTIN; ARACHIDONIC ACID; ICOSANOID; MEROMYOSIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN; PHOSPHATE;

EID: 74949141354     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.00577.2009     Document Type: Article
Times cited : (12)

References (61)
  • 1
    • 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 256: 7501-7509, 1981.
    • (1981) J Biol Chem , vol.256 , pp. 7501-7509
    • Adelstein, R.S.1    Klee, C.B.2
  • 3
    • 0025344156 scopus 로고
    • A continuous fluorimetric assay for ATPase activity
    • Banik U, Roy S. A continuous fluorimetric assay for ATPase activity. Biochem J 266: 611-614, 1990.
    • (1990) Biochem J , vol.266 , pp. 611-614
    • Banik, U.1    Roy, S.2
  • 4
    • 0021329057 scopus 로고
    • Mediators of arachidonic acid-induced contractions of indomethacin-treated guinea-pig airways: Leukotrienes C4 and D4
    • Burka JF, Saad MH. Mediators of arachidonic acid-induced contractions of indomethacin-treated guinea-pig airways: leukotrienes C4 and D4. Br J Pharmacol 81: 465-473, 1984.
    • (1984) Br J Pharmacol , vol.81 , pp. 465-473
    • Burka, J.F.1    Saad, M.H.2
  • 5
    • 0020481210 scopus 로고
    • Superprecipitation of gizzard actomyosin, and tension in gizzard muscle skinned fibers in the presence of nucleotides other than ATP
    • Cassidy P, Kerrick WG. Superprecipitation of gizzard actomyosin, and tension in gizzard muscle skinned fibers in the presence of nucleotides other than ATP. Biochim Biophys Acta 705: 63-69, 1982.
    • (1982) Biochim Biophys Acta , vol.705 , pp. 63-69
    • Cassidy, P.1    Kerrick, W.G.2
  • 6
    • 0020678721 scopus 로고
    • Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules
    • Craig R, Smith R, Kendrick-Jones J. Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules. Nature 302: 436-49, 1983.
    • (1983) Nature , vol.302 , pp. 436-449
    • Craig, R.1    Smith, R.2    Kendrick-Jones, J.3
  • 7
    • 0016915065 scopus 로고
    • A simple method of preparing actin-free myosin from smooth muscle
    • Ebashi S. A simple method of preparing actin-free myosin from smooth muscle. J Biochem (Tokyo) 79: 229-231, 1976.
    • (1976) J Biochem (Tokyo) , vol.79 , pp. 229-231
    • Ebashi, S.1
  • 8
    • 33846461305 scopus 로고    scopus 로고
    • Potent inhibition of arterial smooth muscle tonic contractions by the selective myosin II inhibitor, blebbistatin
    • Eddinger TJ, Meer DP, Miner AS, Meehl J, Rovner AS, Ratz PH. Potent inhibition of arterial smooth muscle tonic contractions by the selective myosin II inhibitor, blebbistatin. J Pharmacol Exp Ther 320: 865-870, 2007.
    • (2007) J Pharmacol Exp Ther , vol.320 , pp. 865-870
    • Eddinger, T.J.1    Meer, D.P.2    Miner, A.S.3    Meehl, J.4    Rovner, A.S.5    Ratz, P.H.6
  • 11
    • 0035190054 scopus 로고    scopus 로고
    • Myosin light chain kinase as a multifunctional regulatory protein of smooth muscle contraction
    • Gao Y, Ye LH, Kishi H, Okagaki T, Samizo K, Nakamura A, Kohama K. Myosin light chain kinase as a multifunctional regulatory protein of smooth muscle contraction. IUBMB Life 51: 337-344, 2001.
    • (2001) IUBMB Life , vol.51 , 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
    • 0026806485 scopus 로고
    • Arachidonic acid inhibits myosin light chain phosphatase, and sensitizes smooth muscle to calcium
    • Gong MC, Fuglsang A, Alessi D, Kobayashi S, Cohen P, Somlyo AV, Somlyo AP. Arachidonic acid inhibits myosin light chain phosphatase, and sensitizes smooth muscle to calcium. J Biol Chem 267: 21492-21498, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 21492-21498
    • Gong, M.C.1    Fuglsang, A.2    Alessi, D.3    Kobayashi, S.4    Cohen, P.5    Somlyo, A.V.6    Somlyo, A.P.7
  • 13
    • 0029008006 scopus 로고
    • Arachidonic acid and diacylglycerol release associated with inhibition of myosin light chain dephosphorylation in rabbit smooth muscle
    • Gong MC, Kinter MT, Somlyo AV, Somlyo AP. Arachidonic acid and diacylglycerol release associated with inhibition of myosin light chain dephosphorylation in rabbit smooth muscle. J Physiol 486: 113-122, 1995.
    • (1995) J Physiol , vol.486 , pp. 113-122
    • Gong, M.C.1    Kinter, M.T.2    Somlyo, A.V.3    Somlyo, A.P.4
  • 14
    • 0001068154 scopus 로고
    • Biochemistry of the contractile proteins in smooth muscle
    • 2nd ed, edited by Johnson LR. New York: Raven
    • Hartshorne DJ. Biochemistry of the contractile proteins 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 , pp. 423-482
    • Hartshorne, D.J.1
  • 16
    • 0023851762 scopus 로고
    • Mechanism of contracture on cooling of caffeine-treated frog skeletal muscle fibres
    • Horiuti K. Mechanism of contracture on cooling of caffeine-treated frog skeletal muscle fibres. J Physiol 398: 131-148, 1988.
    • (1988) J Physiol , vol.398 , pp. 131-148
    • Horiuti, K.1
  • 17
    • 0021824642 scopus 로고
    • Proteolysis of smooth muscle myosin by Staphylococcus aureus protease: Preparation of heavy meromyosin and subfragment 1 with intact 20,000-dalton light chains
    • Ikebe M, Hartshorne DJ. Proteolysis of smooth muscle myosin by Staphylococcus aureus protease: preparation of heavy meromyosin and subfragment 1 with intact 20,000-dalton light chains. Biochemistry 24: 2380-2387, 1985.
    • (1985) Biochemistry , vol.24 , pp. 2380-2387
    • Ikebe, M.1    Hartshorne, D.J.2
  • 18
    • 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, Matsumura F. 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. J Biol Chem 264: 7490-7497, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 20
    • 33751238836 scopus 로고    scopus 로고
    • Blebbistatin inhibits sphingosylphosphorylcholine-induced contraction of collagen-gel fiber populated by vascular smooth-muscle cells
    • Katayama T, Yoshiyama S, Tanaka H, Wang HH, Nakamura A, Kohama K. Blebbistatin inhibits sphingosylphosphorylcholine-induced contraction of collagen-gel fiber populated by vascular smooth-muscle cells. J Pharmacol Sci 102: 339-342, 2006.
    • (2006) J Pharmacol Sci , vol.102 , pp. 339-342
    • Katayama, T.1    Yoshiyama, S.2    Tanaka, H.3    Wang, H.H.4    Nakamura, A.5    Kohama, K.6
  • 21
    • 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) 99: 1465-1472, 1986.
    • (1986) J Biochem (Tokyo) , vol.99 , pp. 1465-1472
    • Kodama, T.1    Fukui, K.2    Kometani, K.3
  • 22
    • 74949085496 scopus 로고    scopus 로고
    • Kohama K, Saida K. (Editors) Smooth Muscle Contraction, New Regulatory Modes. Tokyo: Japan Sci. Soc., 1995.
    • Kohama K, Saida K. (Editors) Smooth Muscle Contraction, New Regulatory Modes. Tokyo: Japan Sci. Soc., 1995.
  • 23
    • 0018988232 scopus 로고
    • Heterogeneity of amino acid incorporation rate in adult skeletal muscle actin
    • Kohama K. Heterogeneity of amino acid incorporation rate in adult skeletal muscle actin. J Biochem (Tokyo) 87: 997-999, 1980.
    • (1980) J Biochem (Tokyo) , vol.87 , pp. 997-999
    • Kohama, K.1
  • 24
    • 0034663463 scopus 로고    scopus 로고
    • Determination of plasma free fatty acids by high-performance liquid chromatography with electrochemical detection
    • Kotani A, Fuse T, Kusu F. Determination of plasma free fatty acids by high-performance liquid chromatography with electrochemical detection. Anal Biochem 284: 65-69, 2000.
    • (2000) Anal Biochem , vol.284 , pp. 65-69
    • Kotani, A.1    Fuse, T.2    Kusu, F.3
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0025990355 scopus 로고
    • Heavy-meromyosin-decorated actin filaments: A simple method to preserve actin filaments for rotary shadowing
    • Mabuchi K. Heavy-meromyosin-decorated actin filaments: a simple method to preserve actin filaments for rotary shadowing. J Struct Biol 107: 22-28, 1991.
    • (1991) J Struct Biol , vol.107 , pp. 22-28
    • Mabuchi, K.1
  • 29
    • 0019317330 scopus 로고
    • Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles
    • Marston SB, Taylor EW. Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles. J Mol Biol 139: 573-600, 1980.
    • (1980) J Mol Biol , vol.139 , pp. 573-600
    • Marston, S.B.1    Taylor, E.W.2
  • 32
    • 0025881329 scopus 로고
    • Characterization of magnesium-induced contractions in detergent-skinned swine carotid media
    • Moreland RS, Moreland S. Characterization of magnesium-induced contractions in detergent-skinned swine carotid media. Am J Physiol Cell Physiol 260: C1224-C1232, 1991.
    • (1991) Am J Physiol Cell Physiol , vol.260
    • Moreland, R.S.1    Moreland, S.2
  • 34
    • 17644419995 scopus 로고    scopus 로고
    • Brain arachidonic acid incorporation is decreased in heart fatty acid binding protein gene-ablated mice
    • Murphy EJ, Owada Y, Kitanaka N, Kondo H, Glatz JF. Brain arachidonic acid incorporation is decreased in heart fatty acid binding protein gene-ablated mice. Biochemistry 44: 6350-6360, 2005.
    • (2005) Biochemistry , vol.44 , pp. 6350-6360
    • Murphy, E.J.1    Owada, Y.2    Kitanaka, N.3    Kondo, H.4    Glatz, J.F.5
  • 36
    • 0021165725 scopus 로고
    • A simple and rapid method to remove light chain phosphatase from chicken gizzard myosin
    • Nakamura S, Nonomura Y. A simple and rapid method to remove light chain phosphatase from chicken gizzard myosin. J Biochem (Tokyo) 96: 575-578, 1984.
    • (1984) J Biochem (Tokyo) , vol.96 , pp. 575-578
    • Nakamura, S.1    Nonomura, Y.2
  • 39
    • 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
    • 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) 108: 856-866, 1991.
    • (1991) J Biochem (Tokyo) , vol.108 , pp. 856-866
    • Okagaki, T.1    Higashi-Fujime, S.2    Ishikawa, R.3    Takano-Ohmuro, H.4    Kohama, K.5
  • 40
    • 0034695927 scopus 로고    scopus 로고
    • Assembly of smooth muscle myosin by the 38k protein, a homologue of a subunit of pre-mRNA splicing factor-2
    • Okagaki T, Nakamura A, Suzuki T, Ohmi K, Kohama K. Assembly of smooth muscle myosin by the 38k protein, a homologue of a subunit of pre-mRNA splicing factor-2. J Cell Biol 148: 653-663, 2000.
    • (2000) J Cell Biol , vol.148 , pp. 653-663
    • Okagaki, T.1    Nakamura, A.2    Suzuki, T.3    Ohmi, K.4    Kohama, K.5
  • 41
    • 0020181786 scopus 로고
    • Electron microscopic studies of myosin molecules from chicken gizzard muscle I: The formation of the intramolecular loop in the myosin tail
    • Onishi H, Wakabayashi T. Electron microscopic studies of myosin molecules from chicken gizzard muscle I: the formation of the intramolecular loop in the myosin tail. J Biochem (Tokyo) 92: 871-879, 1982.
    • (1982) J Biochem (Tokyo) , vol.92 , pp. 871-879
    • Onishi, H.1    Wakabayashi, T.2
  • 42
    • 0018425157 scopus 로고
    • Chicken gizzard heavy meromyosin that retains the two light-chain components, including a phosphorylatable one
    • Onishi H, Watanabe S. Chicken gizzard heavy meromyosin that retains the two light-chain components, including a phosphorylatable one. J Biochem (Tokyo) 85: 457-472, 1979.
    • (1979) J Biochem (Tokyo) , vol.85 , pp. 457-472
    • Onishi, H.1    Watanabe, S.2
  • 43
    • 0014829125 scopus 로고
    • An electrophoretic study of the low-molecularweight components of myosin
    • Perrie WT, Perry SV. An electrophoretic study of the low-molecularweight components of myosin. Biochem J 119: 31-38, 1970.
    • (1970) Biochem J , vol.119 , pp. 31-38
    • Perrie, W.T.1    Perry, S.V.2
  • 44
    • 0021331534 scopus 로고
    • Smooth muscle contraction as a model to study the mediator role of endogenous lipoxygenase products of arachidonic acid
    • Ritchie DM, Hahn DW, McGuire JL. Smooth muscle contraction as a model to study the mediator role of endogenous lipoxygenase products of arachidonic acid. Life Sci 34: 509-513, 1984.
    • (1984) Life Sci , vol.34 , pp. 509-513
    • Ritchie, D.M.1    Hahn, D.W.2    McGuire, J.L.3
  • 45
    • 0017902791 scopus 로고
    • 2+-induced tension development in chemically skinned smooth muscle fibers
    • 2+-induced tension development in chemically skinned smooth muscle fibers. J Gen Physiol 72: 1-14, 1978.
    • (1978) J Gen Physiol , vol.72 , pp. 1-14
    • Saida, K.1    Nonomura, Y.2
  • 46
    • 0019308534 scopus 로고
    • Regulation of non-muscle myosin assembly by calmodulin-dependent light chain kinase
    • Scholey JM, Taylor KA, Kendrick-Jones J. Regulation of non-muscle myosin assembly by calmodulin-dependent light chain kinase. Nature 287: 233-235, 1980.
    • (1980) Nature , vol.287 , pp. 233-235
    • Scholey, J.M.1    Taylor, K.A.2    Kendrick-Jones, J.3
  • 47
    • 0019321058 scopus 로고
    • Fragmentation of gizzard myosin by alpha-chymotrypsin and papain, the effects on ATPase activity, and the interaction with actin
    • Seidel JC. Fragmentation of gizzard myosin by alpha-chymotrypsin and papain, the effects on ATPase activity, and the interaction with actin. J Biol Chem 255: 4355-4361, 1980.
    • (1980) J Biol Chem , vol.255 , pp. 4355-4361
    • Seidel, J.C.1
  • 49
    • 31044450637 scopus 로고    scopus 로고
    • Lipid-derived autacoids: Eicosanoids, and platelet-activating factor
    • 11th ed, edited by Laurence Brunton LL, Lazo JS, and Parker KP. New York: McGraw-Hill
    • Smyth EM, Burke A, FitzGerald GA. Lipid-derived autacoids: eicosanoids, and platelet-activating factor. In: Goodman & Gilman's The Pharmacological Basis of Therapeutics (11th ed.), edited by Laurence Brunton LL, Lazo JS, and Parker KP. New York: McGraw-Hill, 2006, p. 653-736.
    • (2006) Goodman & Gilman's The Pharmacological Basis of Therapeutics , pp. 653-736
    • Smyth, E.M.1    Burke, A.2    FitzGerald, G.A.3
  • 50
    • 0034650714 scopus 로고    scopus 로고
    • Signal transduction by G-proteins, Rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II
    • Somlyo AP, Somlyo AV. Signal transduction by G-proteins, Rho-kinase 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
  • 51
    • 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 JA, 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 246: 4866-4871, 1971.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 54
    • 0002209012 scopus 로고    scopus 로고
    • Myosin regulation and assembly
    • edited by Barany M. San Diego, CA: Academic
    • Trybus KM. Myosin regulation and assembly. In: Biochemistry of Smooth Muscle Contraction, edited by Barany M. San Diego, CA: Academic, 1996, p. 37-46.
    • (1996) Biochemistry of Smooth Muscle Contraction , pp. 37-46
    • Trybus, K.M.1
  • 55
    • 0028085210 scopus 로고
    • Enhanced force generation by smooth muscle myosin in vitro
    • VanBuren P, Work SS, Warshaw DM. Enhanced force generation by smooth muscle myosin in vitro. Proc Natl Acad Sci USA 91: 202-205, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 202-205
    • VanBuren, P.1    Work, S.S.2    Warshaw, D.M.3
  • 58
    • 0038352067 scopus 로고    scopus 로고
    • Troponin I inhibitory peptide suppresses the force generation in smooth muscle by directly interfering with cross-bridge formation
    • 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 307: 236-240, 2003.
    • (2003) Biochem Biophys Res Commun , vol.307 , pp. 236-240
    • Watanabe, M.1    Yoshino, Y.2    Morimoto, S.3
  • 59
    • 0015514873 scopus 로고
    • Fluorescence studies on heavy meromyosin-substrate interaction
    • Werber MM, Szent-Györgyi AG, Fasman GD. Fluorescence studies on heavy meromyosin-substrate interaction. Biochemistry 11: 2872-2883, 1972.
    • (1972) Biochemistry , vol.11 , pp. 2872-2883
    • Werber, M.M.1    Szent-Györgyi, A.G.2    Fasman, G.D.3
  • 60
    • 0023661175 scopus 로고
    • Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence. Implications on topography and function of myosin
    • Yanagisawa M, Hamada Y, Katsuragawa Y, Imamura M, Mikawa T, Masaki T. Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence. Implications on topography and function of myosin. J Mol Biol 198: 143-157, 1987.
    • (1987) J Mol Biol , vol.198 , pp. 143-157
    • Yanagisawa, M.1    Hamada, Y.2    Katsuragawa, Y.3    Imamura, M.4    Mikawa, T.5    Masaki, T.6
  • 61
    • 0033536060 scopus 로고    scopus 로고
    • Myosin light-chain kinase of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain
    • Ye LH, Kishi H, Nakamura A, Okagaki T, Tanaka T, Oiwa K, Kohama K. Myosin light-chain kinase of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain. Proc Natl Acad Sci USA 96: 6666-6671, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6666-6671
    • Ye, L.H.1    Kishi, H.2    Nakamura, A.3    Okagaki, T.4    Tanaka, T.5    Oiwa, K.6    Kohama, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.