메뉴 건너뛰기




Volumn 97, Issue 3, 2015, Pages 281-291

α5-Integrin-mediated cellular signaling contributes to the myogenic response of cerebral resistance arteries

Author keywords

Cerebral arteries; Integrin adhesions; Myogenic response; Phosphoprotein content; Signaling

Indexed keywords

ALPHA5 INTEGRIN; ALPHAVBETA1 INTEGRIN; FOCAL ADHESION KINASE; G ACTIN; INTEGRIN; MYOSIN LIGHT CHAIN PHOSPHATASE; PHOSPHOLIPASE C GAMMA1; UNCLASSIFIED DRUG; PHOSPHOPROTEIN; PROTEIN KINASE;

EID: 84941808777     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2015.08.088     Document Type: Article
Times cited : (22)

References (96)
  • 1
    • 0025097985 scopus 로고
    • Regulation of large cerebral arteries and cerebral microvascular pressure
    • F.M. Faraci, and D.D. Heistad Regulation of large cerebral arteries and cerebral microvascular pressure Circ. Res. 66 1990 8 17
    • (1990) Circ. Res. , vol.66 , pp. 8-17
    • Faraci, F.M.1    Heistad, D.D.2
  • 2
    • 0032899216 scopus 로고    scopus 로고
    • Signaling mechanisms underlying the vascular myogenic response
    • M.J. Davis, and M.A. Hill Signaling mechanisms underlying the vascular myogenic response Physiol. Rev. 79 1999 387 423
    • (1999) Physiol. Rev. , vol.79 , pp. 387-423
    • Davis, M.J.1    Hill, M.A.2
  • 3
    • 0036889937 scopus 로고    scopus 로고
    • Myogenic tone, reactivity, and forced dilatation: A three-phase model of in vitro arterial myogenic behavior
    • G. Osol, J.F. Brekke, K. McElroy-Yaggy, and N.I. Gokina Myogenic tone, reactivity, and forced dilatation: a three-phase model of in vitro arterial myogenic behavior Am. J. Physiol. Heart Circ. Physiol. 283 2002 H2260 H2267
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.283 , pp. H2260-H2267
    • Osol, G.1    Brekke, J.F.2    McElroy-Yaggy, K.3    Gokina, N.I.4
  • 4
    • 79958704519 scopus 로고    scopus 로고
    • Role of myosin light chain kinase and myosin light chain phosphatase in the resistance arterial myogenic response to intravascular pressure
    • W.C. Cole, and D.G. Welsh Role of myosin light chain kinase and myosin light chain phosphatase in the resistance arterial myogenic response to intravascular pressure Arch. Biochem. Biophys. 510 2011 160 173
    • (2011) Arch. Biochem. Biophys. , vol.510 , pp. 160-173
    • Cole, W.C.1    Welsh, D.G.2
  • 5
    • 84871919065 scopus 로고    scopus 로고
    • The role of actin filament dynamics in the myogenic response of cerebral resistance arteries
    • M.P. Walsh, and W.C. Cole The role of actin filament dynamics in the myogenic response of cerebral resistance arteries J. Cereb. Blood Flow Metab. 33 1 2013 1 12
    • (2013) J. Cereb. Blood Flow Metab. , vol.33 , Issue.1 , pp. 1-12
    • Walsh, M.P.1    Cole, W.C.2
  • 6
    • 0032055663 scopus 로고    scopus 로고
    • 2+] in cerebral arteries of rat by membrane potential and intravascular pressure
    • 2+] in cerebral arteries of rat by membrane potential and intravascular pressure J.Physiol. 508 1998 199 209
    • (1998) J.Physiol. , vol.508 , pp. 199-209
    • Knot, H.J.1    Nelson, M.T.2
  • 7
    • 0028825658 scopus 로고
    • 2+]i in myogenic reactivity and arteriolar tone
    • 2+]i in myogenic reactivity and arteriolar tone Am. J. Physiol. 269 1995 H1590 H1596
    • (1995) Am. J. Physiol. , vol.269 , pp. H1590-H1596
    • Zou, H.1    Ratz, P.H.2    Hill, M.A.3
  • 8
    • 66649089243 scopus 로고    scopus 로고
    • 2+ sensitization via phosphorylation of myosin phosphatase targeting subunit at threonine-855 by Rho kinase contributes to the arterial myogenic response
    • 2+ sensitization via phosphorylation of myosin phosphatase targeting subunit at threonine-855 by Rho kinase contributes to the arterial myogenic response J. Physiol. 587 2009 2537 2553
    • (2009) J. Physiol. , vol.587 , pp. 2537-2553
    • Johnson, R.P.1    El-Yazbi, A.F.2    Takeya, K.3    Walsh, E.J.4    Walsh, M.P.5    Cole, W.C.6
  • 9
    • 84874423302 scopus 로고    scopus 로고
    • 2+ sensitization due to myosin light chain phosphatase inhibition and cytoskeletal reorganization in the myogenic response of skeletal muscle resistance arteries
    • 2+ sensitization due to myosin light chain phosphatase inhibition and cytoskeletal reorganization in the myogenic response of skeletal muscle resistance arteries J. Physiol. 591 2013 1235 1250
    • (2013) J. Physiol. , vol.591 , pp. 1235-1250
    • Moreno-Domínguez, A.1    Colinas, O.2    El-Yazbi, A.3    Walsh, E.J.4    Hill, M.A.5    Walsh, M.P.6
  • 10
    • 0036135875 scopus 로고    scopus 로고
    • Pressure-induced actin polymerization in vascular smooth muscle as a mechanism underlying myogenic behavior
    • M.J. Cipolla, N.I. Gokina, and G. Osol Pressure-induced actin polymerization in vascular smooth muscle as a mechanism underlying myogenic behavior FASEB J. 16 2002 72 76
    • (2002) FASEB J. , vol.16 , pp. 72-76
    • Cipolla, M.J.1    Gokina, N.I.2    Osol, G.3
  • 11
    • 84905406388 scopus 로고    scopus 로고
    • Cytoskeletal reorganization evoked by ROK- and PKC-catalyzed phosphorylation of cofilin and HSP27, respectively, contributes to myogenic constriction of rat cerebral arteries
    • A. Moreno-Domínguez, A. El-Yazbi, H. Zhu, O. Colinas, X.Z. Zhong, E.J. Walsh, and et al. Cytoskeletal reorganization evoked by ROK- and PKC-catalyzed phosphorylation of cofilin and HSP27, respectively, contributes to myogenic constriction of rat cerebral arteries J. Biol. Chem. 289 2014 20939 20952
    • (2014) J. Biol. Chem. , vol.289 , pp. 20939-20952
    • Moreno-Domínguez, A.1    El-Yazbi, A.2    Zhu, H.3    Colinas, O.4    Zhong, X.Z.5    Walsh, E.J.6
  • 12
    • 84863455163 scopus 로고    scopus 로고
    • Arteriolar vascular smooth muscle cells: Mechanotransducers in a complex environment
    • M.A. Hill, and G.A. Meininger Arteriolar vascular smooth muscle cells: mechanotransducers in a complex environment Int. J. Biochem. Cell Biol. 44 2012 1505 1510
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 1505-1510
    • Hill, M.A.1    Meininger, G.A.2
  • 15
    • 21644457637 scopus 로고    scopus 로고
    • Alphavbeta3- and alpha5beta1-integrin blockade inhibits myogenic constriction of skeletal muscle resistance arterioles
    • L.A. Martinez-Lemus, T. Crow, M.J. Davis, and G.A. Meininger Alphavbeta3- and alpha5beta1-integrin blockade inhibits myogenic constriction of skeletal muscle resistance arterioles Am. J. Physiol. Heart Circ. Physiol. 289 2005 H322 H329
    • (2005) Am. J. Physiol. Heart Circ. Physiol. , vol.289 , pp. H322-H329
    • Martinez-Lemus, L.A.1    Crow, T.2    Davis, M.J.3    Meininger, G.A.4
  • 16
    • 53449100875 scopus 로고    scopus 로고
    • Actin cytoskeletal dynamics in smooth muscle: A new paradigm for the regulation of smooth muscle contraction
    • S.J. Gunst, and W. Zhang Actin cytoskeletal dynamics in smooth muscle: a new paradigm for the regulation of smooth muscle contraction Am. J. Physiol. 295 2008 C576 C587
    • (2008) Am. J. Physiol. , vol.295 , pp. C576-C587
    • Gunst, S.J.1    Zhang, W.2
  • 17
    • 84865604742 scopus 로고    scopus 로고
    • Deciphering actin cytoskeletal function in the contractile vascular smooth muscle cell
    • R. Yamin, and K.G. Morgan Deciphering actin cytoskeletal function in the contractile vascular smooth muscle cell J. Physiol. 590 2012 4145 4154
    • (2012) J. Physiol. , vol.590 , pp. 4145-4154
    • Yamin, R.1    Morgan, K.G.2
  • 18
    • 0031037080 scopus 로고    scopus 로고
    • Myogenic contraction by modulation of voltage-dependent calcium currents in isolated rat cerebral arteries
    • J.G. McCarron, C.A. Crichton, P.D. Langton, A. MacKenzie, and G.L. Smith Myogenic contraction by modulation of voltage-dependent calcium currents in isolated rat cerebral arteries J. Physiol. 498 1997 371 379
    • (1997) J. Physiol. , vol.498 , pp. 371-379
    • McCarron, J.G.1    Crichton, C.A.2    Langton, P.D.3    MacKenzie, A.4    Smith, G.L.5
  • 19
    • 0030946915 scopus 로고    scopus 로고
    • KCa-channel blockade prevents sustained pressure-induced depolarization in rat mesenteric small arteries
    • J.P. Wesselman, R. Schubert, E.D. VanBavel, H. Nilsson, and M.J. Mulvany KCa-channel blockade prevents sustained pressure-induced depolarization in rat mesenteric small arteries Am. J. Physiol. 272 1997 H2241 H2249
    • (1997) Am. J. Physiol. , vol.272 , pp. H2241-H2249
    • Wesselman, J.P.1    Schubert, R.2    VanBavel, E.D.3    Nilsson, H.4    Mulvany, M.J.5
  • 20
    • 40349114611 scopus 로고    scopus 로고
    • A new trick for an old dogma: ENaC proteins as mechanotransducers in vascular smooth muscle
    • H.A. Drummond, S.C. Grifoni, and N.L. Jernigan A new trick for an old dogma: ENaC proteins as mechanotransducers in vascular smooth muscle Physiology (Bethesda) 23 2008 23 31
    • (2008) Physiology (Bethesda) , vol.23 , pp. 23-31
    • Drummond, H.A.1    Grifoni, S.C.2    Jernigan, N.L.3
  • 21
    • 79961072515 scopus 로고    scopus 로고
    • Mechanical control of cation channels in the myogenic response
    • B.E. Carlson, and D.A. Beard Mechanical control of cation channels in the myogenic response Am. J. Physiol. Heart Circ. Physiol. 301 2011 H331 H343
    • (2011) Am. J. Physiol. Heart Circ. Physiol. , vol.301 , pp. H331-H343
    • Carlson, B.E.1    Beard, D.A.2
  • 22
    • 84901944514 scopus 로고    scopus 로고
    • A PLCγ1-dependent, force-sensitive signaling network in the myogenic constriction of cerebral arteries
    • A.L. Gonzales, Y. Yang, M.N. Sullivan, L. Sanders, F. Dabertrand, D.C. Hill-Eubanks, and et al. A PLCγ1-dependent, force-sensitive signaling network in the myogenic constriction of cerebral arteries Sci. Signal. 7 2014 327
    • (2014) Sci. Signal. , vol.7 , pp. 327
    • Gonzales, A.L.1    Yang, Y.2    Sullivan, M.N.3    Sanders, L.4    Dabertrand, F.5    Hill-Eubanks, D.C.6
  • 23
    • 84874236229 scopus 로고    scopus 로고
    • Capitalizing on diversity: An integrative approach towards the multiplicity of cellular mechanisms underlying myogenic responsiveness
    • D. Lidington, R. Schubert, and S.S. Bolz Capitalizing on diversity: an integrative approach towards the multiplicity of cellular mechanisms underlying myogenic responsiveness Cardiovasc. Res. 97 2013 404 412
    • (2013) Cardiovasc. Res. , vol.97 , pp. 404-412
    • Lidington, D.1    Schubert, R.2    Bolz, S.S.3
  • 24
    • 10044256495 scopus 로고    scopus 로고
    • Involvement of metalloproteinases 2/9 in epidermal growth factor receptor transactivation in pressure-induced myogenic tone in mouse mesenteric resistance arteries
    • P.A. Lucchesi, A. Sabri, S. Belmadani, and K. Matrougui Involvement of metalloproteinases 2/9 in epidermal growth factor receptor transactivation in pressure-induced myogenic tone in mouse mesenteric resistance arteries Circulation 110 2004 3587 3593
    • (2004) Circulation , vol.110 , pp. 3587-3593
    • Lucchesi, P.A.1    Sabri, A.2    Belmadani, S.3    Matrougui, K.4
  • 26
    • 83555164095 scopus 로고    scopus 로고
    • N-cadherin and integrin blockade inhibit arteriolar myogenic reactivity but not pressure-induced increases in intracellular Ca
    • T.Y. Jackson, Z. Sun, L.A. Martinez-Lemus, M.A. Hill, and G.A. Meininger N-cadherin and integrin blockade inhibit arteriolar myogenic reactivity but not pressure-induced increases in intracellular Ca Front. Physiol. 1 2010 165
    • (2010) Front. Physiol. , vol.1 , pp. 165
    • Jackson, T.Y.1    Sun, Z.2    Martinez-Lemus, L.A.3    Hill, M.A.4    Meininger, G.A.5
  • 28
    • 0034925225 scopus 로고    scopus 로고
    • Invited review: Focal adhesion and small heat shock proteins in the regulation of actin remodeling and contractility in smooth muscle
    • W.T. Gerthoffer, and S.J. Gunst Invited review: focal adhesion and small heat shock proteins in the regulation of actin remodeling and contractility in smooth muscle J Appl Physiol. 91 2001 963 972
    • (2001) J Appl Physiol. , vol.91 , pp. 963-972
    • Gerthoffer, W.T.1    Gunst, S.J.2
  • 29
    • 61449220945 scopus 로고    scopus 로고
    • Genetic and cell biological analysis of integrin outside-in signaling
    • K.R. Legate, S.A. Wickström, and R. Fässler Genetic and cell biological analysis of integrin outside-in signaling Genes Dev. 23 2009 397 418
    • (2009) Genes Dev. , vol.23 , pp. 397-418
    • Legate, K.R.1    Wickström, S.A.2    Fässler, R.3
  • 30
    • 84889975549 scopus 로고    scopus 로고
    • Cell adhesion and intracellular calcium signaling in neurons
    • L. Sheng, I. Leshchyns'ka, and V. Sytnyk Cell adhesion and intracellular calcium signaling in neurons Cell Commun. Signal. 11 2013 94
    • (2013) Cell Commun. Signal. , vol.11 , pp. 94
    • Sheng, L.1    Leshchyns'ka, I.2    Sytnyk, V.3
  • 32
    • 34250026140 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of focal adhesion kinase
    • D. Lietha, X. Cai, D.F. Ceccarelli, Y. Li, M.D. Schaller, and M.J. Eck Structural basis for the autoinhibition of focal adhesion kinase Cell 129 2007 1177 1187
    • (2007) Cell , vol.129 , pp. 1177-1187
    • Lietha, D.1    Cai, X.2    Ceccarelli, D.F.3    Li, Y.4    Schaller, M.D.5    Eck, M.J.6
  • 33
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • S.M. Thomas, and J.S. Brugge Cellular functions regulated by Src family kinases Annu. Rev. Cell Dev. Biol. 13 1997 513 609
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 34
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • R.P. Johnson, and S.W. Craig F-actin binding site masked by the intramolecular association of vinculin head and tail domains Nature 373 1995 261 264
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 35
    • 21644478210 scopus 로고    scopus 로고
    • PLCgamma1 is essential for early events in integrin signalling required for cell motility
    • N.P. Jones, J. Peak, S. Brader, S.A. Eccles, and M. Katan PLCgamma1 is essential for early events in integrin signalling required for cell motility J. Cell Sci. 15 2005 2695 2706
    • (2005) J. Cell Sci. , vol.15 , pp. 2695-2706
    • Jones, N.P.1    Peak, J.2    Brader, S.3    Eccles, S.A.4    Katan, M.5
  • 36
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • S.G. Rhee Regulation of phosphoinositide-specific phospholipase C Annu. Rev. Biochem. 70 2001 281 312
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 37
    • 37249071435 scopus 로고    scopus 로고
    • A novel role for Lsc/p115 RhoGEF and LARG in regulating RhoA activity downstream of adhesion to fibronectin
    • A.D. Dubash, K. Wennerberg, R. García-Mata, M.M. Menold, W.T. Arthur, and K. Burridge A novel role for Lsc/p115 RhoGEF and LARG in regulating RhoA activity downstream of adhesion to fibronectin J. Cell Sci. 120 2007 3989 3998
    • (2007) J. Cell Sci. , vol.120 , pp. 3989-3998
    • Dubash, A.D.1    Wennerberg, K.2    García-Mata, R.3    Menold, M.M.4    Arthur, W.T.5    Burridge, K.6
  • 38
    • 42549105514 scopus 로고    scopus 로고
    • FAK, PDZ-RhoGEF and ROCKII cooperate to regulate adhesion movement and trailing-edge retraction in fibroblasts
    • M.P. Iwanicki, T. Vomastek, R.W. Tilghman, K.H. Martin, J. Banerjee, P.B. Wedegaertner, and et al. FAK, PDZ-RhoGEF and ROCKII cooperate to regulate adhesion movement and trailing-edge retraction in fibroblasts J. Cell Sci. 121 2008 895 905
    • (2008) J. Cell Sci. , vol.121 , pp. 895-905
    • Iwanicki, M.P.1    Vomastek, T.2    Tilghman, R.W.3    Martin, K.H.4    Banerjee, J.5    Wedegaertner, P.B.6
  • 40
    • 84920586016 scopus 로고    scopus 로고
    • Mechanosensors in integrin signaling: The emerging role of p130Cas
    • R. Janoštiak, A.C. Pataki, J. Brábek, and D. Rösel Mechanosensors in integrin signaling: the emerging role of p130Cas Eur. J. Cell Biol. 93 2014 445 454
    • (2014) Eur. J. Cell Biol. , vol.93 , pp. 445-454
    • Janoštiak, R.1    Pataki, A.C.2    Brábek, J.3    Rösel, D.4
  • 42
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin adapting to change
    • M.C. Brown, and C.E. Turner Paxillin adapting to change Physiol. Rev. 84 2004 1315 1339
    • (2004) Physiol. Rev. , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 43
    • 84906861543 scopus 로고    scopus 로고
    • Phosphorylation at Y1065 in vinculin mediates actin bundling, cell spreading, and mechanical responses to force
    • C.E. Tolbert, P.M. Thompson, R. Superfine, K. Burridge, and S.L. Campbell Phosphorylation at Y1065 in vinculin mediates actin bundling, cell spreading, and mechanical responses to force Biochemistry 53 2014 5526 5536
    • (2014) Biochemistry , vol.53 , pp. 5526-5536
    • Tolbert, C.E.1    Thompson, P.M.2    Superfine, R.3    Burridge, K.4    Campbell, S.L.5
  • 46
    • 0029797941 scopus 로고    scopus 로고
    • Vascular smooth muscle alpha v beta 3 integrin mediates arteriolar vasodilation in response to RGD peptides
    • J.E. Mogford, G.E. Davis, S.H. Platts, and G.A. Meininger Vascular smooth muscle alpha v beta 3 integrin mediates arteriolar vasodilation in response to RGD peptides Circ. Res. 79 1996 821 826
    • (1996) Circ. Res. , vol.79 , pp. 821-826
    • Mogford, J.E.1    Davis, G.E.2    Platts, S.H.3    Meininger, G.A.4
  • 47
    • 0030701893 scopus 로고    scopus 로고
    • An Arg-Gly-ASP peptide stimulates constriction in rat afferent arteriole
    • K.P. Yip, and D.J. Marsh An Arg-Gly-Asp peptide stimulates constriction in rat afferent arteriole Am. J. Physiol. 273 1997 F768 F776
    • (1997) Am. J. Physiol. , vol.273 , pp. F768-F776
    • Yip, K.P.1    Marsh, D.J.2
  • 49
    • 0037040825 scopus 로고    scopus 로고
    • Alpha(4) beta(1) integrin activation of L-type calcium channels in vascular smooth muscle causes arteriole vasoconstriction
    • K.R. Waitkus-Edwards, L.A. Martinez-Lemus, X. Wu, J.P. Trzeciakowski, M.J. Davis, G.E. Davis, and et al. Alpha(4) beta(1) integrin activation of L-type calcium channels in vascular smooth muscle causes arteriole vasoconstriction Circ. Res. 90 2002 473 480
    • (2002) Circ. Res. , vol.90 , pp. 473-480
    • Waitkus-Edwards, K.R.1    Martinez-Lemus, L.A.2    Wu, X.3    Trzeciakowski, J.P.4    Davis, M.J.5    Davis, G.E.6
  • 51
    • 52749086084 scopus 로고    scopus 로고
    • Extracellular matrix-specific focal adhesions in vascular smooth muscle produce mechanically active adhesion sites
    • Z. Sun, L.A. Martinez-Lemus, M.A. Hill, and G.A. Meininger Extracellular matrix-specific focal adhesions in vascular smooth muscle produce mechanically active adhesion sites Am. J. Physiol. Cell Physiol. 295 2008 C268 C278
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295 , pp. C268-C278
    • Sun, Z.1    Martinez-Lemus, L.A.2    Hill, M.A.3    Meininger, G.A.4
  • 52
    • 0030795570 scopus 로고    scopus 로고
    • Specific attenuation of the pressure-induced contraction of rat cerebral artery by herbimycin A
    • N. Masumoto, K. Nakayama, A. Oyabe, M. Uchino, K. Ishii, K. Obara, and et al. Specific attenuation of the pressure-induced contraction of rat cerebral artery by herbimycin A Eur. J. Pharmacol. 330 1997 55 63
    • (1997) Eur. J. Pharmacol. , vol.330 , pp. 55-63
    • Masumoto, N.1    Nakayama, K.2    Oyabe, A.3    Uchino, M.4    Ishii, K.5    Obara, K.6
  • 53
    • 0033383148 scopus 로고    scopus 로고
    • Integrin signaling, free radicals, and tyrosine kinase mediate flow constriction in isolated cerebral arteries
    • J.A. Madden, and N.J. Christman Integrin signaling, free radicals, and tyrosine kinase mediate flow constriction in isolated cerebral arteries Am. J. Physiol. 277 1999 H2264 H2271
    • (1999) Am. J. Physiol. , vol.277 , pp. H2264-H2271
    • Madden, J.A.1    Christman, N.J.2
  • 54
    • 0034837889 scopus 로고    scopus 로고
    • Tyrosine phosphorylation following alterations in arteriolar intraluminal pressure and wall tension
    • T.V. Murphy, B.E. Spurrell, and M.A. Hill Tyrosine phosphorylation following alterations in arteriolar intraluminal pressure and wall tension Am. J. Physiol. Heart Circ. Physiol. 281 2001 H1047 H1056
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281 , pp. H1047-H1056
    • Murphy, T.V.1    Spurrell, B.E.2    Hill, M.A.3
  • 55
    • 48249157879 scopus 로고    scopus 로고
    • A highly sensitive technique to measure myosin regulatory light chain phosphorylation: The first quantification in renal arterioles
    • K. Takeya, K. Loutzenhiser, M. Shiraishi, R. Loutzenhiser, and M.P. Walsh A highly sensitive technique to measure myosin regulatory light chain phosphorylation: the first quantification in renal arterioles Am. J. Physiol. Renal Physiol. 294 2008 F1487 F1492
    • (2008) Am. J. Physiol. Renal Physiol. , vol.294 , pp. F1487-F1492
    • Takeya, K.1    Loutzenhiser, K.2    Shiraishi, M.3    Loutzenhiser, R.4    Walsh, M.P.5
  • 56
    • 0025047567 scopus 로고
    • Endothelium-dependent, flow-induced dilation of isolated coronary arterioles
    • L. Kuo, M.J. Davis, and W.M. Chilian Endothelium-dependent, flow-induced dilation of isolated coronary arterioles Am. J. Physiol. 259 1990 H1063 H1070
    • (1990) Am. J. Physiol. , vol.259 , pp. H1063-H1070
    • Kuo, L.1    Davis, M.J.2    Chilian, W.M.3
  • 57
    • 84929705321 scopus 로고    scopus 로고
    • PKC-mediated cerebral vasoconstriction: Role of myosin light chain phosphorylation versus actin cytoskeleton reorganization
    • A.F. El-Yazbi, K.S. Abd-Elrahman, and A. Moreno-Dominguez PKC-mediated cerebral vasoconstriction: role of myosin light chain phosphorylation versus actin cytoskeleton reorganization Biochem. Pharmacol. 95 2015 263 278
    • (2015) Biochem. Pharmacol. , vol.95 , pp. 263-278
    • El-Yazbi, A.F.1    Abd-Elrahman, K.S.2    Moreno-Dominguez, A.3
  • 58
    • 78651324925 scopus 로고    scopus 로고
    • Rho-associated kinase plays a role in rabbit urethral smooth muscle contraction, but not via enhanced myosin light chain phosphorylation
    • M.P. Walsh, K. Thornbury, W.C. Cole, G. Sergeant, M. Hollywood, and N. McHale Rho-associated kinase plays a role in rabbit urethral smooth muscle contraction, but not via enhanced myosin light chain phosphorylation Am. J. Physiol. Renal Physiol. 300 2011 F73 F85
    • (2011) Am. J. Physiol. Renal Physiol. , vol.300 , pp. F73-F85
    • Walsh, M.P.1    Thornbury, K.2    Cole, W.C.3    Sergeant, G.4    Hollywood, M.5    McHale, N.6
  • 59
    • 80054996654 scopus 로고    scopus 로고
    • Evidence for activation of BK Ca channels by a known inhibitor of focal adhesion kinase, PF573228
    • E.C. So, K.C. Wu, C.H. Liang, J.Y. Chen, and S.N. Wu Evidence for activation of BK Ca channels by a known inhibitor of focal adhesion kinase, PF573228 Life Sci. 89 2011 691 701
    • (2011) Life Sci. , vol.89 , pp. 691-701
    • So, E.C.1    Wu, K.C.2    Liang, C.H.3    Chen, J.Y.4    Wu, S.N.5
  • 60
    • 57349153946 scopus 로고    scopus 로고
    • A small molecule inhibitor, 1,2,4,5-benzenetetraamine tetrahydrochloride, targeting the Y397 site of focal adhesion kinase decreases tumor growth
    • V.M. Golubovskaya, C. Nyberg, M. Zheng, F. Kweh, A. Magis, D. Ostrov, and et al. A small molecule inhibitor, 1,2,4,5-benzenetetraamine tetrahydrochloride, targeting the Y397 site of focal adhesion kinase decreases tumor growth J. Med. Chem. 51 2008 7405 7416
    • (2008) J. Med. Chem. , vol.51 , pp. 7405-7416
    • Golubovskaya, V.M.1    Nyberg, C.2    Zheng, M.3    Kweh, F.4    Magis, A.5    Ostrov, D.6
  • 61
    • 84926443367 scopus 로고    scopus 로고
    • A role for the tyrosine kinase Pyk2 in depolarization-induced contraction of vascular smooth muscle
    • R.D. Mills, M. Mita, J.I. Nakagawa, M. Shoji, C. Sutherland, and M.P. Walsh A role for the tyrosine kinase Pyk2 in depolarization-induced contraction of vascular smooth muscle J. Biol. Chem. 290 2015 8677 8692
    • (2015) J. Biol. Chem. , vol.290 , pp. 8677-8692
    • Mills, R.D.1    Mita, M.2    Nakagawa, J.I.3    Shoji, M.4    Sutherland, C.5    Walsh, M.P.6
  • 62
    • 0034458943 scopus 로고    scopus 로고
    • SU6656, a selective src family kinase inhibitor, used to probe growth factor signaling
    • R.A. Blake, M.A. Broome, X. Liu, J. Wu, M. Gishizky, L. Sun, and et al. SU6656, a selective src family kinase inhibitor, used to probe growth factor signaling Mol. Cell Biol. 20 2000 9018 9027
    • (2000) Mol. Cell Biol. , vol.20 , pp. 9018-9027
    • Blake, R.A.1    Broome, M.A.2    Liu, X.3    Wu, J.4    Gishizky, M.5    Sun, L.6
  • 64
    • 0033002997 scopus 로고    scopus 로고
    • Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2
    • J.D. Owen, P.J. Ruest, D.W. Fry, and S.K. Hanks Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2 Mol. Cell Biol. 19 1999 4806 4818
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4806-4818
    • Owen, J.D.1    Ruest, P.J.2    Fry, D.W.3    Hanks, S.K.4
  • 65
    • 0343340035 scopus 로고    scopus 로고
    • Phosphospecific antibodies reveal focal adhesion kinase activation loop phosphorylation in nascent and mature focal adhesions and requirement for the autophosphorylation site
    • P.J. Ruest, S. Roy, E. Shi, R.L. Mernaugh, and S.K. Hanks Phosphospecific antibodies reveal focal adhesion kinase activation loop phosphorylation in nascent and mature focal adhesions and requirement for the autophosphorylation site Cell Growth Differ. 11 2000 41 48
    • (2000) Cell Growth Differ. , vol.11 , pp. 41-48
    • Ruest, P.J.1    Roy, S.2    Shi, E.3    Mernaugh, R.L.4    Hanks, S.K.5
  • 66
    • 0035947577 scopus 로고    scopus 로고
    • Src family kinases are required for integrin-mediated but not for G protein-coupled receptor stimulation of focal adhesion kinase autophosphorylation at Tyr-397
    • P. Salazar, and Rozengurt Src family kinases are required for integrin-mediated but not for G protein-coupled receptor stimulation of focal adhesion kinase autophosphorylation at Tyr-397 J. Biol. Chem. 276 2001 17788 17795
    • (2001) J. Biol. Chem. , vol.276 , pp. 17788-17795
    • Salazar, P.1    Rozengurt2
  • 67
  • 68
    • 0034998560 scopus 로고    scopus 로고
    • Depletion of focal adhesion kinase by antisense depresses contractile activation of smooth muscle
    • D.D. Tang, and S.J. Gunst Depletion of focal adhesion kinase by antisense depresses contractile activation of smooth muscle Am. J. Physiol. Cell Physiol. 280 2001 C874 C883
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280 , pp. C874-C883
    • Tang, D.D.1    Gunst, S.J.2
  • 69
    • 84864096689 scopus 로고    scopus 로고
    • Src modulates contractile vascular smooth muscle function via regulation of focal adhesions
    • J. Min, M. Reznichenko, R.H. Poythress, C.M. Gallant, S. Vetterkind, Y. Li, and et al. Src modulates contractile vascular smooth muscle function via regulation of focal adhesions J. Cell Physiol. 227 2012 3585 3592
    • (2012) J. Cell Physiol. , vol.227 , pp. 3585-3592
    • Min, J.1    Reznichenko, M.2    Poythress, R.H.3    Gallant, C.M.4    Vetterkind, S.5    Li, Y.6
  • 70
    • 70449428295 scopus 로고    scopus 로고
    • Stretch activates human myometrium via ERK, caldesmon and focal adhesion signaling
    • Y. Li, M. Reznichenko, R.M. Tribe, P.E. Hess, M. Taggart, H. Kim, and et al. Stretch activates human myometrium via ERK, caldesmon and focal adhesion signaling PLoS One 4 2009 e7489
    • (2009) PLoS One , vol.4 , pp. e7489
    • Li, Y.1    Reznichenko, M.2    Tribe, R.M.3    Hess, P.E.4    Taggart, M.5    Kim, H.6
  • 71
    • 13444268938 scopus 로고    scopus 로고
    • Differential regulation of vascular focal adhesion kinase by steady stretch and pulsatility
    • S. Lehoux, B. Esposito, R. Merval, and A. Tedgui Differential regulation of vascular focal adhesion kinase by steady stretch and pulsatility Circulation 111 2005 643 649
    • (2005) Circulation , vol.111 , pp. 643-649
    • Lehoux, S.1    Esposito, B.2    Merval, R.3    Tedgui, A.4
  • 72
    • 0035948579 scopus 로고    scopus 로고
    • Biochemical signals and biological responses elicited by the focal adhesion kinase
    • M.D. Schaller Biochemical signals and biological responses elicited by the focal adhesion kinase Biochim. Biophys. Acta 1540 2001 1 21
    • (2001) Biochim. Biophys. Acta , vol.1540 , pp. 1-21
    • Schaller, M.D.1
  • 74
    • 0037049555 scopus 로고    scopus 로고
    • Recruitment of the Arp2/3 complex to vinculin: Coupling membrane protrusion to matrix adhesion
    • K.A. DeMali, C.A. Barlow, and K. Burridge Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion J. Cell Biol. 159 2002 881 891
    • (2002) J. Cell Biol. , vol.159 , pp. 881-891
    • DeMali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 75
    • 77956268219 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of vinculin at position 1065 modifies focal adhesion dynamics and cell tractions
    • K. Küpper, N. Lang, C. Möhl, N. Kirchgessner, S. Born, W.H. Goldmann, and et al. Tyrosine phosphorylation of vinculin at position 1065 modifies focal adhesion dynamics and cell tractions Biochem. Biophys. Res. Commun. 399 2010 560 564
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , pp. 560-564
    • Küpper, K.1    Lang, N.2    Möhl, C.3    Kirchgessner, N.4    Born, S.5    Goldmann, W.H.6
  • 76
    • 84896710291 scopus 로고    scopus 로고
    • 1065 regulates vinculin conformation and tension development in arway smooth muscle tissues
    • 1065 regulates vinculin conformation and tension development in arway smooth muscle tissues J. Biol. Chem. 289 2014 3677 3688
    • (2014) J. Biol. Chem. , vol.289 , pp. 3677-3688
    • Huang, Y.1    Day, R.N.2    Gunst, S.J.3
  • 77
    • 21744450576 scopus 로고    scopus 로고
    • Role of the actin cytoskeleton in G-protein-coupled receptor activation of PYK2 and paxillin in vascular smooth muscle
    • V. Ohanian, K. Gatfield, and J. Ohanian Role of the actin cytoskeleton in G-protein-coupled receptor activation of PYK2 and paxillin in vascular smooth muscle Hypertension 46 2005 93 99
    • (2005) Hypertension , vol.46 , pp. 93-99
    • Ohanian, V.1    Gatfield, K.2    Ohanian, J.3
  • 78
    • 34548789929 scopus 로고    scopus 로고
    • Paxillin phosphorylation, actin polymerization, noise temperature, and the sustained phase of swine carotid artery contraction
    • C.M. Rembold, A.D. Tejani, M.L. Ripley, and S. Han Paxillin phosphorylation, actin polymerization, noise temperature, and the sustained phase of swine carotid artery contraction Am. J. Physiol. Cell Physiol. 293 2007 C993 C1002
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293 , pp. C993-C1002
    • Rembold, C.M.1    Tejani, A.D.2    Ripley, M.L.3    Han, S.4
  • 79
    • 0037101563 scopus 로고    scopus 로고
    • The focal adhesion protein paxillin regulates contraction in canine tracheal smooth muscle
    • D.D. Tang, M.F. Wu, A.M. Opazo Saez, and S.J. Gunst The focal adhesion protein paxillin regulates contraction in canine tracheal smooth muscle J. Physiol. 542 2002 501 513
    • (2002) J. Physiol. , vol.542 , pp. 501-513
    • Tang, D.D.1    Wu, M.F.2    Opazo Saez, A.M.3    Gunst, S.J.4
  • 80
    • 0027177730 scopus 로고
    • Myogenic tone is coupled to phospholipase C and G protein activation in small cerebral arteries
    • G. Osol, I. Laher, and M. Kelley Myogenic tone is coupled to phospholipase C and G protein activation in small cerebral arteries Am. J. Physiol. 265 1993 H415 H420
    • (1993) Am. J. Physiol. , vol.265 , pp. H415-H420
    • Osol, G.1    Laher, I.2    Kelley, M.3
  • 81
    • 84866680424 scopus 로고    scopus 로고
    • From mechanical force to RhoA activation
    • E.C. Lessey, C. Guilluy, and K. Burridge From mechanical force to RhoA activation Biochemistry 51 2012 7420 7432
    • (2012) Biochemistry , vol.51 , pp. 7420-7432
    • Lessey, E.C.1    Guilluy, C.2    Burridge, K.3
  • 84
    • 0033962672 scopus 로고    scopus 로고
    • Focal adhesions - The cytoskeletal connection
    • D.R. Critchley Focal adhesions - the cytoskeletal connection Curr. Opin. Cell Biol. 12 2000 133 139
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 133-139
    • Critchley, D.R.1
  • 85
    • 84922159978 scopus 로고    scopus 로고
    • A novel role for RhoA GTPase in the regulation of airway smooth muscle contraction
    • W. Zhang, Y. Huang, Y. Wu, and S.J. Gunst A novel role for RhoA GTPase in the regulation of airway smooth muscle contraction Can. J. Physiol. Pharmacol. 93 2015 129 136
    • (2015) Can. J. Physiol. Pharmacol. , vol.93 , pp. 129-136
    • Zhang, W.1    Huang, Y.2    Wu, Y.3    Gunst, S.J.4
  • 86
    • 17644379396 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by N-WASp is required for actin polymerization and contraction in smooth muscle
    • W. Zhang, Y. Wu, L. Du, D.D. Tang, and S.J. Gunst Activation of the Arp2/3 complex by N-WASp is required for actin polymerization and contraction in smooth muscle Am. J. Physiol. 288 2005 C1145 C1160
    • (2005) Am. J. Physiol. , vol.288 , pp. C1145-C1160
    • Zhang, W.1    Wu, Y.2    Du, L.3    Tang, D.D.4    Gunst, S.J.5
  • 87
    • 20744455807 scopus 로고    scopus 로고
    • The adapter protein CrkII regulates neuronal Wiskott-Aldrich syndrome protein, actin polymerization, and tension development during contractile stimulation of smooth muscle
    • D.D. Tang, W. Zhang, and S.J. Gunst The adapter protein CrkII regulates neuronal Wiskott-Aldrich syndrome protein, actin polymerization, and tension development during contractile stimulation of smooth muscle J. Biol. Chem. 280 2005 23380 23389
    • (2005) J. Biol. Chem. , vol.280 , pp. 23380-23389
    • Tang, D.D.1    Zhang, W.2    Gunst, S.J.3
  • 90
    • 0036606183 scopus 로고    scopus 로고
    • Membrane depolarization-induced contraction of rat caudal arterial smooth muscle involves Rho-associated kinase
    • M. Mita, H. Yanagihara, S. Hishinuma, M. Saito, and M.P. Walsh Membrane depolarization-induced contraction of rat caudal arterial smooth muscle involves Rho-associated kinase Biochem. J. 364 2002 431 440
    • (2002) Biochem. J. , vol.364 , pp. 431-440
    • Mita, M.1    Yanagihara, H.2    Hishinuma, S.3    Saito, M.4    Walsh, M.P.5
  • 91
    • 0034851713 scopus 로고    scopus 로고
    • Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK
    • Q.S. Du, X.R. Ren, Y. Xie, Q. Wang, L. Mei, and W.C. Xiong Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK J. Cell Sci. 114 2001 2977 2987
    • (2001) J. Cell Sci. , vol.114 , pp. 2977-2987
    • Du, Q.S.1    Ren, X.R.2    Xie, Y.3    Wang, Q.4    Mei, L.5    Xiong, W.C.6
  • 92
    • 34250639027 scopus 로고    scopus 로고
    • Phospholipase C-gamma1 potentiates integrin-dependent cell spreading and migration through Pyk2/paxillin activation
    • J.H. Choi, Y.R. Yang, S.K. Lee, I.S. Kim, S.H. Ha, E.K. Kim, and et al. Phospholipase C-gamma1 potentiates integrin-dependent cell spreading and migration through Pyk2/paxillin activation Cell Signal. 19 2007 1784 1796
    • (2007) Cell Signal. , vol.19 , pp. 1784-1796
    • Choi, J.H.1    Yang, Y.R.2    Lee, S.K.3    Kim, I.S.4    Ha, S.H.5    Kim, E.K.6
  • 93
    • 38349058006 scopus 로고    scopus 로고
    • PyK2 and FAK connections to p190Rho guanine nucleotide exchange factor regulate RhoA activity, focal adhesion formation, and cell motility
    • Y. Lim, S.T. Lim, A. Tomar, M. Gardel, J.A. Bernard-Trifilo, X.L. Chen, and et al. PyK2 and FAK connections to p190Rho guanine nucleotide exchange factor regulate RhoA activity, focal adhesion formation, and cell motility J.Cell Biol. 180 2008 187 203
    • (2008) J.Cell Biol. , vol.180 , pp. 187-203
    • Lim, Y.1    Lim, S.T.2    Tomar, A.3    Gardel, M.4    Bernard-Trifilo, J.A.5    Chen, X.L.6
  • 94
    • 85018144750 scopus 로고    scopus 로고
    • Abnormal phosphorylation of MYPT1 and actin polymerization are associated with the dysfunctional myogenic response in cerebral arteries of Goto-Kakizaki rats
    • K.S. Abd-Elrahman, E.J. Walsh, M.P. Walsh, and W.C. Cole Abnormal phosphorylation of MYPT1 and actin polymerization are associated with the dysfunctional myogenic response in cerebral arteries of Goto-Kakizaki rats J.Vasc. Res. 51 2014 67
    • (2014) J.Vasc. Res. , vol.51 , pp. 67
    • Abd-Elrahman, K.S.1    Walsh, E.J.2    Walsh, M.P.3    Cole, W.C.4
  • 96
    • 84908886269 scopus 로고    scopus 로고
    • β Integrins mediate FAK Y397 autophosphorylation of resistance arteries during eutrophic inward remodeling in hypertension
    • E.H. Heerkens, L. Quinn, S.B. Withers, and A.M. Heagerty β Integrins mediate FAK Y397 autophosphorylation of resistance arteries during eutrophic inward remodeling in hypertension J. Vasc. Res. 51 2014 305 314
    • (2014) J. Vasc. Res. , vol.51 , pp. 305-314
    • Heerkens, E.H.1    Quinn, L.2    Withers, S.B.3    Heagerty, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.