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Volumn 17, Issue 1, 2010, Pages

Caldesmon regulates the motility of vascular smooth muscle cells by modulating the actin cytoskeleton stability

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALANINE; CALDESMON; MITOGEN ACTIVATED PROTEIN KINASE; MYOSIN ADENOSINE TRIPHOSPHATASE; SERINE; CALMODULIN BINDING PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; GREEN FLUORESCENT PROTEIN;

EID: 77950433106     PISSN: 10217770     EISSN: 14230127     Source Type: Journal    
DOI: 10.1186/1423-0127-17-6     Document Type: Article
Times cited : (25)

References (43)
  • 1
    • 0035749892 scopus 로고    scopus 로고
    • Caldesmon and smooth-muscle regulation
    • 10.1385/CBB:35:3:275. 11894847
    • Caldesmon and smooth-muscle regulation. C-LA Wang, Cell Biochem Biophys 2001 35 3 275 288 10.1385/CBB:35:3:275 11894847
    • (2001) Cell Biochem Biophys , vol.35 , Issue.3 , pp. 275-288
    • C-La, W.1
  • 2
    • 0026510219 scopus 로고
    • Cloning of cDNAs encoding human caldesmons
    • 10.1016/0378-1119(92)90376-Z. 1555769
    • Cloning of cDNAs encoding human caldesmons. MB Humphrey H Herrera-Sosa G Gonzalez R Lee J Bryan, Gene 1992 112 2 197 204 10.1016/0378-1119(92)90376-Z 1555769
    • (1992) Gene , vol.112 , Issue.2 , pp. 197-204
    • Humphrey, M.B.1    Herrera-Sosa, H.2    Gonzalez, G.3    Lee, R.4    Bryan, J.5
  • 4
    • 60849135151 scopus 로고    scopus 로고
    • Caldesmon and the regulation of cytoskeletal functions
    • full-text. 19209827
    • Caldesmon and the Regulation of Cytoskeletal Functions. CL Wang, Adv Exp Med Biol 2008 644 250 272 full-text 19209827
    • (2008) Adv Exp Med Biol , vol.644 , pp. 250-272
    • Wang, C.L.1
  • 5
    • 77950409860 scopus 로고
    • Loading of caldesmon peptide (GS17C) into intact vascular smooth muscle by reversible permeablization
    • Loading of caldesmon peptide (GS17C) into intact vascular smooth muscle by reversible permeablization. CA Lajoie CA Parker CL Wang KG Morgan, Biophys J 1994 66 408
    • (1994) Biophys J , vol.66 , pp. 1408
    • Lajoie, C.A.1    Parker, C.A.2    Wang, C.L.3    Morgan, K.G.4
  • 6
    • 0026695761 scopus 로고
    • Regulation of vascular smooth muscle tone by caldesmon
    • 1386078
    • Regulation of vascular smooth muscle tone by caldesmon. H Katsuyama CL Wang KG Morgan, J Biol Chem 1992 267 21 14555 14558 1386078
    • (1992) J Biol Chem , vol.267 , Issue.21 , pp. 14555-14558
    • Katsuyama, H.1    Wang, C.L.2    Morgan, K.G.3
  • 7
    • 0034602971 scopus 로고    scopus 로고
    • Regulation of vascular smooth muscle tone by N-terminal region of caldesmon. Possible role of tethering actin to myosin
    • DOI 10.1074/jbc.275.5.3213
    • Regulation of vascular smooth muscle tone by N-terminal region of caldesmon. Possible role of tethering actin to myosin. YH Lee C Gallant H Guo Y Li CL Wang KG Morgan, J Biol Chem 2000 275 5 3213 3220 10.1074/jbc.275.5.3213 10652307 (Pubitemid 30083021)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.5 , pp. 3213-3220
    • Lee, Y.-H.1    Gallant, C.2    Guo, H.3    Li, Y.4    Wang, C.-L.A.5    Morgan, K.G.6
  • 9
    • 0032555992 scopus 로고    scopus 로고
    • Caldesmon inhibits active crossbridges in unstimulated vascular smooth muscle: An antisense oligodeoxynucleotide approach
    • Caldesmon inhibits active crossbridges in unstimulated vascular smooth muscle: an antisense oligodeoxynucleotide approach. JJ Earley X Su RS Moreland, Circ Res 1998 83 6 661 667 9742062 (Pubitemid 28427750)
    • (1998) Circulation Research , vol.83 , Issue.6 , pp. 661-667
    • Earley, J.J.1    Su, X.2    Moreland, R.S.3
  • 10
    • 0026519840 scopus 로고
    • Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas
    • 10.1016/0014-5793(92)80446-N. 1601129
    • Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas. LP Adam CJ Gapinski DR Hathaway, FEBS Lett 1992 302 3 223 226 10.1016/0014-5793(92)80446-N 1601129
    • (1992) FEBS Lett , vol.302 , Issue.3 , pp. 223-226
    • Adam, L.P.1    Gapinski, C.J.2    Hathaway, D.R.3
  • 11
    • 0037432321 scopus 로고    scopus 로고
    • Caldesmon binding to actin is regulated by calmodulin and phosphorylation via different mechanisms
    • DOI 10.1021/bi0268605
    • Caldesmon binding to actin is regulated by calmodulin and phosphorylation via different mechanisms. R Huang L Li H Guo CL Wang, Biochemistry 2003 42 9 2513 2523 10.1021/bi0268605 12614145 (Pubitemid 36330604)
    • (2003) Biochemistry , vol.42 , Issue.9 , pp. 2513-2523
    • Huang, R.1    Li, L.2    Guo, H.3    Wang, C.-L.A.4
  • 12
    • 0034695554 scopus 로고    scopus 로고
    • 2+ sensitivity of smooth muscle contraction
    • DOI 10.1074/jbc.275.3.1959
    • Phosphorylation of caldesmon by p21-activated kinase. Implications for the Ca(2+) sensitivity of smooth muscle contraction. DB Foster LH Shen J Kelly P Thibault JE Van Eyk AS Mak, J Biol Chem 2000 275 3 1959 1965 10.1074/jbc.275.3.1959 10636898 (Pubitemid 30060822)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.3 , pp. 1959-1965
    • Foster, D.B.1    Shen, L.-H.2    Kelly, J.3    Thibault, P.4    Van Eyk, J.E.5    Mak, A.S.6
  • 13
    • 0026078926 scopus 로고
    • Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during mitosis
    • 10.1038/349169a0. 1986309
    • Phosphorylation of non-muscle caldesmon by p34cdc2 kinase during mitosis. S Yamashiro Y Yamakita H Hosoya F Matsumura, Nature 1991 349 6305 169 172 10.1038/349169a0 1986309
    • (1991) Nature , vol.349 , Issue.6305 , pp. 169-172
    • Yamashiro, S.1    Yamakita, Y.2    Hosoya, H.3    Matsumura, F.4
  • 14
    • 0034982994 scopus 로고    scopus 로고
    • Modulatory role of ERK MAPK-caldesmon pathway in PDGF-stimulated migration of cultured pulmonary artery SMCs
    • 11350764
    • Modulatory role of ERK MAPK-caldesmon pathway in PDGF-stimulated migration of cultured pulmonary artery SMCs. IA Yamboliev WT Gerthoffer, American Journal of Physiology - Cell Physiology 2001 280 6 1680 C1688 11350764
    • (2001) American Journal of Physiology - Cell Physiology , vol.280 , Issue.6
    • Yamboliev, I.A.1    Gerthoffer, W.T.2
  • 16
    • 28344440602 scopus 로고    scopus 로고
    • Phosphorylated l-caldesmon is involved in disassembly of actin stress fibers and postmitotic spreading
    • DOI 10.1016/j.yexcr.2005.09.021, PII S0014482705004520
    • Phosphorylated l-caldesmon is involved in disassembly of actin stress fibers and postmitotic spreading. J Kordowska T Hetrick LP Adam CL Wang, Exp Cell Res 2006 312 2 95 110 10.1016/j.yexcr.2005.09.021 16289153 (Pubitemid 41721173)
    • (2006) Experimental Cell Research , vol.312 , Issue.2 , pp. 95-110
    • Kordowska, J.1    Hetrick, T.2    Adam, L.P.3    Albert Wang, C.-L.4
  • 17
    • 0142152635 scopus 로고    scopus 로고
    • Caldesmon-dependent switching between capillary endothelial cell growth and apoptosis through modulation of cell shape and contractility
    • DOI 10.1023/A:1025821517679
    • Caldesmon-dependent switching between capillary endothelial cell growth and apoptosis through modulation of cell shape and contractility. Y Numaguchi S Huang TR Polte GS Eichler N Wang DE Ingber, Angiogenesis 2003 6 1 55 64 10.1023/A:1025821517679 14517405 (Pubitemid 37305340)
    • (2003) Angiogenesis , vol.6 , Issue.1 , pp. 55-64
    • Numaguchi, Y.1    Huang, S.2    Polte, T.R.3    Eichler, G.S.4    Wang, N.5    Ingber, D.E.6
  • 18
    • 0026063170 scopus 로고
    • Inhibition of intracellular granule movement by microinjection of monoclonal antibodies against caldesmon
    • 10.1002/cm.970200204. 1751965
    • Inhibition of intracellular granule movement by microinjection of monoclonal antibodies against caldesmon. TE Hegmann DL Schulte JL Lin JJ Lin, Cell Motil Cytoskeleton 1991 20 2 109 120 10.1002/cm.970200204 1751965
    • (1991) Cell Motil Cytoskeleton , vol.20 , Issue.2 , pp. 109-120
    • Hegmann, T.E.1    Schulte, D.L.2    Lin, J.L.3    Lin, J.J.4
  • 19
    • 33748645951 scopus 로고    scopus 로고
    • Requirement of reversible caldesmon phosphorylation at P21-activated kinase-responsive sites for lamellipodia extensions during cell migration
    • DOI 10.1002/cm.20144
    • Requirement of reversible caldesmon phosphorylation at P21-activated kinase-responsive sites for lamellipodia extensions during cell migration. RD Eppinga Y Li JL Lin AS Mak JJ Lin, Cell Motil Cytoskeleton 2006 63 9 543 562 10.1002/cm.20144 16800003 (Pubitemid 44384280)
    • (2006) Cell Motility and the Cytoskeleton , vol.63 , Issue.9 , pp. 543-562
    • Eppinga, R.D.1    Li, Y.2    Lin, J.L.-C.3    Mak, A.S.4    Lin, J.J.-C.5
  • 20
    • 33744507187 scopus 로고    scopus 로고
    • Caldesmon is an integral component of podosomes in smooth muscle cells
    • DOI 10.1242/jcs.02881
    • Caldesmon is an integral component of podosomes in smooth muscle cells. R Eves BA Webb S Zhou AS Mak, J Cell Sci 2006 119 Pt 9 1691 1702 10.1242/jcs.02881 16595550 (Pubitemid 43810996)
    • (2006) Journal of Cell Science , vol.119 , Issue.9 , pp. 1691-1702
    • Eves, R.1    Webb, B.A.2    Zhou, S.3    Mak, A.S.4
  • 21
    • 33847215489 scopus 로고    scopus 로고
    • Erk1/2 MAPK and caldesmon differentially regulate podosome dynamics in A7r5 vascular smooth muscle cells
    • DOI 10.1016/j.yexcr.2006.12.005, PII S0014482706004988
    • Erk1/2 MAPK and caldesmon differentially regulate podosome dynamics in A7r5 vascular smooth muscle cells. Z Gu J Kordowska GL Williams CL Wang CM Hai, Exp Cell Res 2007 313 5 849 866 10.1016/j.yexcr.2006.12.005 17239373 (Pubitemid 46298559)
    • (2007) Experimental Cell Research , vol.313 , Issue.5 , pp. 849-866
    • Gu, Z.1    Kordowska, J.2    Williams, G.L.3    Wang, C.-L.A.4    Hai, C.-M.5
  • 22
    • 34247209087 scopus 로고    scopus 로고
    • Changes in the balance between caldesmon regulated by p21-activated kinases and the Arp2/3 complex govern podosome formation
    • DOI 10.1074/jbc.M609983200
    • Changes in the balance between caldesmon regulated by p21-activated kinases and the Arp2/3 complex govern podosome formation. T Morita T Mayanagi T Yoshio K Sobue, J Biol Chem 2007 282 11 8454 8463 10.1074/jbc.M609983200 17224451 (Pubitemid 47093626)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.11 , pp. 8454-8463
    • Morita, T.1    Mayanagi, T.2    Yoshio, T.3    Sobue, K.4
  • 23
    • 0037879150 scopus 로고    scopus 로고
    • Dissecting DNA-protein and protein-protein interactions involved in bacterial transcriptional regulation by a sensitive protein array method combining a near-infrared fluorescence detection
    • DOI 10.1002/pmic.200300390
    • Dissecting DNA-protein and protein-protein interactions involved in bacterial transcriptional regulation by a sensitive protein array method combining a near-infrared fluorescence detection. M Snapyan M Lecocq L Guevel MC Arnaud A Ghochikyan V Sakanyan, Proteomics 2003 3 5 647 657 10.1002/pmic.200300390 12748944 (Pubitemid 36570255)
    • (2003) Proteomics , vol.3 , Issue.5 , pp. 647-657
    • Snapyan, M.1    Lecocq, M.2    Guevel, L.3    Arnaud, M.-C.4    Ghochikyan, A.5    Sakanyan, V.6
  • 24
    • 0038604334 scopus 로고    scopus 로고
    • Activation of c-Jun-N-terminal-kinase is crucial for the induction of a cell cycle arrest in human colon carcinoma cells caused by flurbiprofen enantiomers
    • 12759338
    • Activation of c-Jun-N-terminal-kinase is crucial for the induction of a cell cycle arrest in human colon carcinoma cells caused by flurbiprofen enantiomers. S Grosch I Tegeder K Schilling TJ Maier E Niederberger G Geisslinger, Faseb J 2003 17 10 1316 1318 12759338
    • (2003) Faseb J , vol.17 , Issue.10 , pp. 1316-1318
    • Grosch, S.1    Tegeder, I.2    Schilling, K.3    Maier, T.J.4    Niederberger, E.5    Geisslinger, G.6
  • 25
    • 0033066120 scopus 로고    scopus 로고
    • Stresses at the cell-to-substrate interface during locomotion of fibroblasts
    • Stresses at the cell-to-substrate interface during locomotion of fibroblasts. M Dembo YL Wang, Biophys J 1999 76 4 2307 2316 10.1016/S0006- 3495(99)77386-8 10096925 (Pubitemid 29266384)
    • (1999) Biophysical Journal , vol.76 , Issue.4 , pp. 2307-2316
    • Dembo, M.1    Wang, Y.-L.2
  • 27
    • 0036783757 scopus 로고    scopus 로고
    • Spatial and temporal traction response in human airway smooth muscle cells
    • 12225988
    • Spatial and temporal traction response in human airway smooth muscle cells. IM Tolic-Norrelykke JP Butler J Chen N Wang, American journal of physiology 2002 283 4 1254 1266 12225988
    • (2002) American Journal of Physiology , vol.283 , Issue.4 , pp. 31254-1266
    • Tolic-Norrelykke, I.M.1    Butler, J.P.2    Chen, J.3    Wang, N.4
  • 29
    • 0001957916 scopus 로고    scopus 로고
    • The biochemistry of animal cell crawling
    • New York: Wiley-Liss
    • The biochemistry of animal cell crawling. J Condeelis, Motion Analysis of Living Cell New York: Wiley-Liss 1998 85 100
    • (1998) Motion Analysis of Living Cell , pp. 85-100
    • Condeelis, J.1
  • 30
    • 63449091349 scopus 로고    scopus 로고
    • Chapter 1: Roles of caldesmon in cell motility and actin cytoskeleton remodeling
    • full-text. 19349035
    • Chapter 1: roles of caldesmon in cell motility and actin cytoskeleton remodeling. JJ Lin Y Li RD Eppinga Q Wang JP Jin, Int Rev Cell Mol Biol 2009 274 1 68 full-text 19349035
    • (2009) Int Rev Cell Mol Biol , vol.274 , pp. 1-68
    • Lin, J.J.1    Li, Y.2    Eppinga, R.D.3    Wang, Q.4    Jin, J.P.5
  • 31
    • 0024514394 scopus 로고
    • Phosphorylation of caldesmon in arterial smooth muscle
    • 2708386
    • Phosphorylation of caldesmon in arterial smooth muscle. LP Adam JR Haeberle DR Hathaway, J Biol Chem 1989 264 13 7698 7703 2708386
    • (1989) J Biol Chem , vol.264 , Issue.13 , pp. 7698-7703
    • Adam, L.P.1    Haeberle, J.R.2    Hathaway, D.R.3
  • 32
    • 0025272184 scopus 로고
    • Mitosis-specific phosphorylation causes 83K non-muscle caldesmon to dissociate from microfilaments
    • 10.1038/344675a0. 2157986
    • Mitosis-specific phosphorylation causes 83K non-muscle caldesmon to dissociate from microfilaments. S Yamashiro Y Yamakita R Ishikawa F Matsumura, Nature 1990 344 6267 675 678 10.1038/344675a0 2157986
    • (1990) Nature , vol.344 , Issue.6267 , pp. 675-678
    • Yamashiro, S.1    Yamakita, Y.2    Ishikawa, R.3    Matsumura, F.4
  • 33
    • 0029900896 scopus 로고    scopus 로고
    • Overexpression of microfilament-stabilizing human caldesmon fragment, CaD39, affects cell attachment, spreading, and cytokinesis
    • 10.1002/(SICI)1097-0169(1996)34:3<215::AID-CM5>3.0.CO;2-8. 8816288
    • Overexpression of microfilament-stabilizing human caldesmon fragment, CaD39, affects cell attachment, spreading, and cytokinesis. KS Warren DC Shutt JP McDermott JL Lin DR Soll JJ Lin, Cell Motil Cytoskeleton 1996 34 3 215 229 10.1002/(SICI)1097-0169(1996)34:3<215::AID-CM5>3.0.CO;2-8 8816288
    • (1996) Cell Motil Cytoskeleton , vol.34 , Issue.3 , pp. 215-229
    • Warren, K.S.1    Shutt, D.C.2    McDermott, J.P.3    Lin, J.L.4    Soll, D.R.5    Lin, J.J.6
  • 34
    • 0037275128 scopus 로고    scopus 로고
    • Regulation of caldesmon activity by Cdc2 kinase plays an important role in maintaining membrane cortex integrity during cell division
    • DOI 10.1007/s000180300014
    • Regulation of caldesmon activity by Cdc2 kinase plays an important role in maintaining membrane cortex integrity during cell division. Y Li D Wessels T Wang JL Lin DR Soll JJ Lin, Cell Mol Life Sci 2003 60 1 198 211 10.1007/s000180300014 12613668 (Pubitemid 36223127)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.1 , pp. 198-211
    • Li, Y.1    Wessels, D.2    Wang, T.3    Lin, J.L.-C.4    Soll, D.R.5    Lin, J.J.-C.6
  • 35
    • 0028881723 scopus 로고
    • Over-expression of smooth muscle caldesmon in mouse fibroblasts
    • 10.1002/cm.970320307. 8581978
    • Over-expression of smooth muscle caldesmon in mouse fibroblasts. I Surgucheva J Bryan, Cell Motil Cytoskeleton 1995 32 3 233 243 10.1002/cm.970320307 8581978
    • (1995) Cell Motil Cytoskeleton , vol.32 , Issue.3 , pp. 233-243
    • Surgucheva, I.1    Bryan, J.2
  • 36
    • 18244383029 scopus 로고    scopus 로고
    • The role of caldesmon in the regulation of endothelial cytoskeleton and migration
    • DOI 10.1002/jcp.20244
    • The role of caldesmon in the regulation of endothelial cytoskeleton and migration. T Mirzapoiazova IA Kolosova L Romer JG Garcia AD Verin, J Cell Physiol 2005 203 3 520 528 10.1002/jcp.20244 15521070 (Pubitemid 40629014)
    • (2005) Journal of Cellular Physiology , vol.203 , Issue.3 , pp. 520-528
    • Mirzapoiazova, T.1    Kolosova, I.A.2    Romer, L.3    Garcia, J.G.N.4    Verin, A.D.5
  • 39
    • 11144230917 scopus 로고    scopus 로고
    • Modes of caldesmon binding to actin: Sites of caldesmon contact and modulation of interactions by phosphorylation
    • DOI 10.1074/jbc.M410109200
    • Modes of caldesmon binding to actin: sites of caldesmon contact and modulation of interactions by phosphorylation. DB Foster R Huang V Hatch R Craig P Graceffa W Lehman C-LA Wang, J Biol Chem 2004 279 51 53387 53394 10.1074/jbc.M410109200 15456752 (Pubitemid 40051844)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53387-53394
    • Foster, D.B.1    Huang, R.2    Hatch, V.3    Craig, R.4    Graceffa, P.5    Lehman, W.6    Wang, C.-L.A.7
  • 40
    • 0035187389 scopus 로고    scopus 로고
    • Mutant caldesmon lacking cdc2 phosphorylation sites delays M-phase entry and inhibits cytokinesis
    • Mutant caldesmon lacking cdc2 phosphorylation sites delays M-phase entry and inhibits cytokinesis. S Yamashiro H Chern Y Yamakita F Matsumura, Molecular Biology of the Cell 2001 12 1 239 250 11160835 (Pubitemid 32060590)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.1 , pp. 239-250
    • Yamashiro, S.1    Chern, H.2    Yamakita, Y.3    Matsumura, F.4
  • 41
    • 4444257529 scopus 로고    scopus 로고
    • 2+-calmodulin binding interferes with assembly of stress fibers and affects cell morphology, growth and motility
    • DOI 10.1242/jcs.01216
    • Caldesmon mutant defective in Ca2+-calmodulin binding interferes with assembly of stress fibers and affects cell morphology, growth and motility. Y Li JL Lin RS Reiter K Daniels DR Soll JJ Lin, J Cell Sci 2004 117 Pt 16 3593 604 10.1242/jcs.01216 15226374 (Pubitemid 39206399)
    • (2004) Journal of Cell Science , vol.117 , Issue.16 , pp. 3593-3604
    • Li, Y.1    Lin, J.L.C.2    Reiter, R.S.3    Daniels, K.4    Soll, D.R.5    Lin, J.J.C.6
  • 43
    • 34547097279 scopus 로고    scopus 로고
    • Caldesmon suppresses cancer cell invasion by regulating podosome/invadopodium formation
    • 10.1016/j.febslet.2007.06.073. 17631293
    • Caldesmon suppresses cancer cell invasion by regulating podosome/invadopodium formation. T Yoshio T Morita Y Kimura M Tsujii N Hayashi K Sobue, FEBS Lett 2007 581 20 3777 3782 10.1016/j.febslet.2007.06.073 17631293
    • (2007) FEBS Lett , vol.581 , Issue.20 , pp. 3777-3782
    • Yoshio, T.1    Morita, T.2    Kimura, Y.3    Tsujii, M.4    Hayashi, N.5    Sobue, K.6


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