메뉴 건너뛰기




Volumn 135, Issue 2, 2008, Pages

Myosin Light Chain Kinase Is Central to Smooth Muscle Contraction and Required for Gastrointestinal Motility in Mice

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE; CALCIUM ION; MYOSIN LIGHT CHAIN KINASE; POTASSIUM ION; TAMOXIFEN;

EID: 48549089459     PISSN: 00165085     EISSN: None     Source Type: Journal    
DOI: 10.1053/j.gastro.2008.05.032     Document Type: Article
Times cited : (159)

References (37)
  • 1
    • 0035895901 scopus 로고    scopus 로고
    • Dedicated myosin light chain kinases with diverse cellular functions
    • Kamm K.E., and Stull J.T. Dedicated myosin light chain kinases with diverse cellular functions. J Biol Chem 276 (2001) 4527-4530
    • (2001) J Biol Chem , vol.276 , pp. 4527-4530
    • Kamm, K.E.1    Stull, J.T.2
  • 2
    • 0141751697 scopus 로고    scopus 로고
    • 2+-sensitivity of smooth and non-muscle myosin II: modulation by G Proteins, kinases and myosin phosphatase
    • 2+-sensitivity of smooth and non-muscle myosin II: modulation by G Proteins, kinases and myosin phosphatase. Physiological Rev 83 (2003) 1325-1358
    • (2003) Physiological Rev , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 3
    • 33645957353 scopus 로고    scopus 로고
    • Signaling for contraction and relaxation in smooth muscle of the gut
    • Murthy K.E. Signaling for contraction and relaxation in smooth muscle of the gut. Annu Rev Physiol 68 (2006) 11.1-11.30
    • (2006) Annu Rev Physiol , vol.68
    • Murthy, K.E.1
  • 4
    • 1942538405 scopus 로고    scopus 로고
    • Myosin phosphatase: structure, regulation and function
    • Ito M., Nakano T., Erdödi F., et al. Myosin phosphatase: structure, regulation and function. Mol Cell Biochem 259 (2004) 197-209
    • (2004) Mol Cell Biochem , vol.259 , pp. 197-209
    • Ito, M.1    Nakano, T.2    Erdödi, F.3
  • 5
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo A.P., and Somlyo A.V. Signal transduction and regulation in smooth muscle. Nature 372 (1994) 231-236
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 6
    • 0024211772 scopus 로고
    • Cytoplasmic free calcium, myosin light chain phosphorylation, and force in phasic and tonic smooth muscle
    • Himpens B., Matthijs G., Somlyo A.V., et al. Cytoplasmic free calcium, myosin light chain phosphorylation, and force in phasic and tonic smooth muscle. J Gen Physiol 92 (1988) 713-729
    • (1988) J Gen Physiol , vol.92 , pp. 713-729
    • Himpens, B.1    Matthijs, G.2    Somlyo, A.V.3
  • 7
    • 0034921574 scopus 로고    scopus 로고
    • Invited review: cross-bridge regulation by thin filament-associated proteins
    • Morgan K.G., and Gangopadhyay S.S. Invited review: cross-bridge regulation by thin filament-associated proteins. J Appl Physiol 91 (2001) 953-962
    • (2001) J Appl Physiol , vol.91 , pp. 953-962
    • Morgan, K.G.1    Gangopadhyay, S.S.2
  • 8
    • 0033485486 scopus 로고    scopus 로고
    • Analysis of the kinase-related protein gene found at human chromosome 3q21 in a multi-gene cluster: organization, expression, alternative splicing, and polymorphic marker
    • Watterson D.M., Schavocky J.P., Guo L., et al. Analysis of the kinase-related protein gene found at human chromosome 3q21 in a multi-gene cluster: organization, expression, alternative splicing, and polymorphic marker. J Cell Biochem 75 (1999) 481-491
    • (1999) J Cell Biochem , vol.75 , pp. 481-491
    • Watterson, D.M.1    Schavocky, J.P.2    Guo, L.3
  • 9
    • 0032883786 scopus 로고    scopus 로고
    • Identification of a novel actin binding motif in smooth muscle myosin light chain kinase
    • Smith L., Su X., Lin P., et al. Identification of a novel actin binding motif in smooth muscle myosin light chain kinase. J Biol Chem 274 (1999) 29433-29438
    • (1999) J Biol Chem , vol.274 , pp. 29433-29438
    • Smith, L.1    Su, X.2    Lin, P.3
  • 10
    • 0033697283 scopus 로고    scopus 로고
    • Smooth muscle myosin light chain kinase expression in cardiac and skeletal muscle
    • Herring B.P., Dixon S., and Gallagher P.J. Smooth muscle myosin light chain kinase expression in cardiac and skeletal muscle. Am J Physiol Cell Physiol 279 (2000) C1656-C1664
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Herring, B.P.1    Dixon, S.2    Gallagher, P.J.3
  • 11
    • 33646164671 scopus 로고    scopus 로고
    • Microfilament-binding properties of N-terminal extension of the isoform of smooth muscle long myosin light chain kinase
    • Yang C.X., Chen H.Q., Chen C., et al. Microfilament-binding properties of N-terminal extension of the isoform of smooth muscle long myosin light chain kinase. Cell Res 16 (2006) 367-376
    • (2006) Cell Res , vol.16 , pp. 367-376
    • Yang, C.X.1    Chen, H.Q.2    Chen, C.3
  • 13
    • 0035308590 scopus 로고    scopus 로고
    • A highly efficient Escherichia coli-based chromosome engineering system adapted for recombinogenic targeting and subcloning of BAC DNA
    • Lee E.C., Yu D., Marinez de Valasco J., et al. A highly efficient Escherichia coli-based chromosome engineering system adapted for recombinogenic targeting and subcloning of BAC DNA. Genomics 73 (2001) 56-65
    • (2001) Genomics , vol.73 , pp. 56-65
    • Lee, E.C.1    Yu, D.2    Marinez de Valasco, J.3
  • 14
    • 0037352031 scopus 로고    scopus 로고
    • A highly efficient recombineering-based method for generating conditional knockout mutations
    • Liu P., Jenkins N.A., and Copeland N.G. A highly efficient recombineering-based method for generating conditional knockout mutations. Genome Res 13 (2003) 476-484
    • (2003) Genome Res , vol.13 , pp. 476-484
    • Liu, P.1    Jenkins, N.A.2    Copeland, N.G.3
  • 15
    • 0033761423 scopus 로고    scopus 로고
    • Temporally controlled somatic mutagenesis in smooth muscle
    • Kuhbandner S., Brummer S., Metzger D., et al. Temporally controlled somatic mutagenesis in smooth muscle. Genesis 28 (2000) 15-22
    • (2000) Genesis , vol.28 , pp. 15-22
    • Kuhbandner, S.1    Brummer, S.2    Metzger, D.3
  • 16
    • 1942501600 scopus 로고    scopus 로고
    • Real-time evaluation of myosin light chain kinase activation in smooth muscle tissues from a transgenic calmodulin-biosensor mouse
    • Isotani E., Zhi G., Lau K.S., et al. Real-time evaluation of myosin light chain kinase activation in smooth muscle tissues from a transgenic calmodulin-biosensor mouse. Proc Natl Acad Sci U S A 101 (2004) 6279-6284
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6279-6284
    • Isotani, E.1    Zhi, G.2    Lau, K.S.3
  • 18
    • 0141723667 scopus 로고    scopus 로고
    • Alimentary tract innervation deficits and dysfunction in mice lacking GDNF family receptor α2
    • Rossi J., Herzig K.H., Voikar V., et al. Alimentary tract innervation deficits and dysfunction in mice lacking GDNF family receptor α2. J Clin Invest 112 (2003) 707-716
    • (2003) J Clin Invest , vol.112 , pp. 707-716
    • Rossi, J.1    Herzig, K.H.2    Voikar, V.3
  • 19
    • 0036728668 scopus 로고    scopus 로고
    • Altered urinary bladder function in mice lacking the vanilloid receptor TRPV
    • Birder L.A., Nakamura Y., Kiss S., et al. Altered urinary bladder function in mice lacking the vanilloid receptor TRPV. Nat Neurosci 5 (2002) 856-860
    • (2002) Nat Neurosci , vol.5 , pp. 856-860
    • Birder, L.A.1    Nakamura, Y.2    Kiss, S.3
  • 20
    • 3843146548 scopus 로고    scopus 로고
    • Genetic analysis of blood pressure in C3H/HeJ and SWR/J mice
    • DiPetrillo K., Tsaih S.W., Sheehan S., et al. Genetic analysis of blood pressure in C3H/HeJ and SWR/J mice. Physiol Genomics 17 (2004) 215-220
    • (2004) Physiol Genomics , vol.17 , pp. 215-220
    • DiPetrillo, K.1    Tsaih, S.W.2    Sheehan, S.3
  • 21
    • 0036080607 scopus 로고    scopus 로고
    • 220- and 130-kDa MLCKs have distinct tissue distributions and intracellular localization patterns
    • Blue E.K., Goeckeler Z.M., Jin Y.J., et al. 220- and 130-kDa MLCKs have distinct tissue distributions and intracellular localization patterns. Am J Physiol Cell Physiol 282 (2002) C451-C460
    • (2002) Am J Physiol Cell Physiol , vol.282
    • Blue, E.K.1    Goeckeler, Z.M.2    Jin, Y.J.3
  • 22
    • 27744543634 scopus 로고    scopus 로고
    • Smoothelin-a is essential for functional intestinal smooth muscle contractility in mice
    • Niessen P., Rensen S., van Deursen J., et al. Smoothelin-a is essential for functional intestinal smooth muscle contractility in mice. Gastroenterology 129 (2005) 1592-1601
    • (2005) Gastroenterology , vol.129 , pp. 1592-1601
    • Niessen, P.1    Rensen, S.2    van Deursen, J.3
  • 23
    • 33644953810 scopus 로고    scopus 로고
    • Motility disorder in experimentally obstructed intestine: relationship between muscularis inflammation and disruption of the ICC network
    • Won K.J., Suzuki T., Hori M., et al. Motility disorder in experimentally obstructed intestine: relationship between muscularis inflammation and disruption of the ICC network. Neurogastroenterol Motil 18 (2006) 53-61
    • (2006) Neurogastroenterol Motil , vol.18 , pp. 53-61
    • Won, K.J.1    Suzuki, T.2    Hori, M.3
  • 24
    • 33751172972 scopus 로고    scopus 로고
    • Spontaneously tonic smooth muscle has characteristically higher levels of RhoA/ROK compared with the phasic smooth muscle
    • Patel C.A., and Rattan S. Spontaneously tonic smooth muscle has characteristically higher levels of RhoA/ROK compared with the phasic smooth muscle. Am J Physiol Gastrointest Liver Physiol 291 (2006) G830-G837
    • (2006) Am J Physiol Gastrointest Liver Physiol , vol.291
    • Patel, C.A.1    Rattan, S.2
  • 26
    • 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 (2001) 29567-29674
    • (2001) J Biol Chem , vol.276 , pp. 29567-29674
    • Niiro, N.1    Ikebe, M.2
  • 27
    • 0035844257 scopus 로고    scopus 로고
    • 2+-independent smooth muscle contraction, a novel function for integrin-linked kinase
    • 2+-independent smooth muscle contraction, a novel function for integrin-linked kinase. J Biol Chem 276 (2001) 16365-16373
    • (2001) J Biol Chem , vol.276 , pp. 16365-16373
    • Deng, J.T.1    Van Lierop, J.E.2    Sutherland, C.3
  • 28
    • 33947537278 scopus 로고    scopus 로고
    • ROCK1 phosphorylates and activates zipper-interacting protein kinase
    • Hagerty L., Weitzel D.H., Chambers J., et al. ROCK1 phosphorylates and activates zipper-interacting protein kinase. J Biol Chem 282 (2007) 4884-4893
    • (2007) J Biol Chem , vol.282 , pp. 4884-4893
    • Hagerty, L.1    Weitzel, D.H.2    Chambers, J.3
  • 29
    • 8844261128 scopus 로고    scopus 로고
    • Rho-kinase inhibition and electromechanical coupling in rat and guinea-pig ureter smooth muscle: Ca2+-dependent and -independent mechanisms
    • Shabir S., Borisova L., Wray S., et al. Rho-kinase inhibition and electromechanical coupling in rat and guinea-pig ureter smooth muscle: Ca2+-dependent and -independent mechanisms. J Physiol 560 (2004) 839-855
    • (2004) J Physiol , vol.560 , pp. 839-855
    • Shabir, S.1    Borisova, L.2    Wray, S.3
  • 30
    • 33645286759 scopus 로고    scopus 로고
    • Attenuation of contractility in rat epididymal vas deferens by Rho kinase inhibitors
    • Amobi N.I., Chung I.P., and Smith I.C. Attenuation of contractility in rat epididymal vas deferens by Rho kinase inhibitors. Auton Autacoid Pharmacol 26 (2006) 169-181
    • (2006) Auton Autacoid Pharmacol , vol.26 , pp. 169-181
    • Amobi, N.I.1    Chung, I.P.2    Smith, I.C.3
  • 31
    • 0033037073 scopus 로고    scopus 로고
    • Cellular and molecular basis for electrical rhythmicity in gastrointestinal muscles
    • Horowitz B., Ward S.M., and Sanders K.M. Cellular and molecular basis for electrical rhythmicity in gastrointestinal muscles. Annu Rev Physiol 61 (1999) 19-43
    • (1999) Annu Rev Physiol , vol.61 , pp. 19-43
    • Horowitz, B.1    Ward, S.M.2    Sanders, K.M.3
  • 32
    • 0036902509 scopus 로고    scopus 로고
    • Pharmacology of transmission to gastrointestinal muscle
    • Lecci A., Santicioli P., and Maggi C.A. Pharmacology of transmission to gastrointestinal muscle. Curr Opin Pharmacol 2 (2002) 630-641
    • (2002) Curr Opin Pharmacol , vol.2 , pp. 630-641
    • Lecci, A.1    Santicioli, P.2    Maggi, C.A.3
  • 33
    • 0037233610 scopus 로고    scopus 로고
    • Neurohumoral control of gastrointestinal motility
    • Hansen M.B. Neurohumoral control of gastrointestinal motility. Physiol Res 52 (2003) 1-30
    • (2003) Physiol Res , vol.52 , pp. 1-30
    • Hansen, M.B.1
  • 34
    • 0037114189 scopus 로고    scopus 로고
    • Mice lacking M2 and M3 muscarinic acetylcholine receptors are devoid of cholinergic smooth muscle contractions but still viable
    • Matsui M., Motomura D., Fujikawa T., et al. Mice lacking M2 and M3 muscarinic acetylcholine receptors are devoid of cholinergic smooth muscle contractions but still viable. J Neurosci 22 (2002) 10627-10632
    • (2002) J Neurosci , vol.22 , pp. 10627-10632
    • Matsui, M.1    Motomura, D.2    Fujikawa, T.3
  • 36
    • 9144257346 scopus 로고    scopus 로고
    • v1.2 L-type calcium channel for urinary bladder function
    • v1.2 L-type calcium channel for urinary bladder function. FASEB J 18 (2004) 1159-1161
    • (2004) FASEB J , vol.18 , pp. 1159-1161
    • Wegener, J.W.1    Schulla, V.2    Lee, T.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.