메뉴 건너뛰기




Volumn 83, Issue 10, 2005, Pages 877-891

The association of caveolae, actin, and the dystrophin-glycoprotein complex: A role in smooth muscle phenotype and function?

Author keywords

Caveolin; Dystroglycan; Filamin; G protein coupled receptors; Mechanical plasticity

Indexed keywords

ACTIN; BETA DYSTROGLYCAN; BINDING PROTEIN; CAVEOLIN 1; CYTOSKELETON PROTEIN; DYSTROPHIN; FILAMIN; GLYCOPROTEIN; INTEGRIN; LAMININ; PROTEIN SUBUNIT; RECEPTOR; STRUCTURAL PROTEIN;

EID: 32544448060     PISSN: 00084212     EISSN: None     Source Type: Journal    
DOI: 10.1139/y05-107     Document Type: Review
Times cited : (40)

References (161)
  • 1
    • 4544242249 scopus 로고    scopus 로고
    • Stretch of the vascular wall induces smooth muscle differentiation by promoting actin polymerization
    • Albinsson, S., Nordstrom, I., and Hellstrand, P. 2004. Stretch of the vascular wall induces smooth muscle differentiation by promoting actin polymerization. J. Biol. Chem. 279: 34849-34855.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34849-34855
    • Albinsson, S.1    Nordstrom, I.2    Hellstrand, P.3
  • 3
    • 9244226528 scopus 로고    scopus 로고
    • On the terminology for describing the length-force relationship and its changes in airway smooth muscle
    • Bai, T.R., Bates, J.H., Brusasco, V., Camoretti-Mercado, B., Chitano, P., Deng, L.H., et al. 2004. On the terminology for describing the length-force relationship and its changes in airway smooth muscle. J. Appl. Physiol. 97: 2029-2034.
    • (2004) J. Appl. Physiol. , vol.97 , pp. 2029-2034
    • Bai, T.R.1    Bates, J.H.2    Brusasco, V.3    Camoretti-Mercado, B.4    Chitano, P.5    Deng, L.H.6
  • 4
    • 0034623959 scopus 로고    scopus 로고
    • Expression of γ-sarcoglycan in smooth muscle and its interaction with the smooth muscle sarcoglycan-sarcospan complex
    • Barresi, R., Moore, S.A., Stolle, C.A., Mendell, J.R., and Campbell, K.P. 2000. Expression of γ-sarcoglycan in smooth muscle and its interaction with the smooth muscle sarcoglycan-sarcospan complex. J. Biol. Chem. 275: 38554-38560.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38554-38560
    • Barresi, R.1    Moore, S.A.2    Stolle, C.A.3    Mendell, J.R.4    Campbell, K.P.5
  • 5
    • 0031891501 scopus 로고    scopus 로고
    • Myosin light chain phosphatase and kinase abnormalities in fetal sheep pulmonary hypertension
    • Belik, J., Majumdar, R., Fabris, V.E., Kerc, E., and Pato, M.D. 1998. Myosin light chain phosphatase and kinase abnormalities in fetal sheep pulmonary hypertension. Pediatr. Res. 43: 57-61.
    • (1998) Pediatr. Res. , vol.43 , pp. 57-61
    • Belik, J.1    Majumdar, R.2    Fabris, V.E.3    Kerc, E.4    Pato, M.D.5
  • 6
    • 0037018153 scopus 로고    scopus 로고
    • High rhoa activity maintains the undifferentiated mesenchymal cell phenotype, whereas rhoa down-regulation by laminin-2 induces smooth muscle myogenesis
    • Beqaj, S., Jakkaraju, S., Mattingly, R.R., Pan, D., and Schuger, L. 2002. High rhoa activity maintains the undifferentiated mesenchymal cell phenotype, whereas rhoa down-regulation by laminin-2 induces smooth muscle myogenesis. J. Cell. Biol. 156: 893-903.
    • (2002) J. Cell. Biol. , vol.156 , pp. 893-903
    • Beqaj, S.1    Jakkaraju, S.2    Mattingly, R.R.3    Pan, D.4    Schuger, L.5
  • 8
    • 4143086109 scopus 로고    scopus 로고
    • Caveolae-associated signalling in smooth muscle
    • Bergdahl, A., and Sward, K. 2004. Caveolae-associated signalling in smooth muscle. Can. J. Physiol. Pharmacol. 82: 289-299.
    • (2004) Can. J. Physiol. Pharmacol. , vol.82 , pp. 289-299
    • Bergdahl, A.1    Sward, K.2
  • 10
    • 0019442473 scopus 로고
    • Freeze-fracture studies of muscle caveolae in human muscular dystrophy
    • Bonilla, E., Fischbeck, K., and Schotland, D.L. 1981. Freeze-fracture studies of muscle caveolae in human muscular dystrophy. Am. J. Pathol. 104: 167-173.
    • (1981) Am. J. Pathol. , vol.104 , pp. 167-173
    • Bonilla, E.1    Fischbeck, K.2    Schotland, D.L.3
  • 14
    • 2342655667 scopus 로고    scopus 로고
    • Increased sensitivity of asthmatic airway smooth muscle cells to prostaglandin E2 might be mediated by increased numbers of E-prostanoid receptors
    • Burgess, J.K., Ge, Q., Boustany, S., Black, J.L., and Johnson, P.R. 2004. Increased sensitivity of asthmatic airway smooth muscle cells to prostaglandin E2 might be mediated by increased numbers of E-prostanoid receptors. J. Allergy Clin. Immunol. 113: 876-881.
    • (2004) J. Allergy Clin. Immunol. , vol.113 , pp. 876-881
    • Burgess, J.K.1    Ge, Q.2    Boustany, S.3    Black, J.L.4    Johnson, P.R.5
  • 16
    • 0033037910 scopus 로고    scopus 로고
    • Association of the dystroglycan complex isolated from bovine brain synaptosomes with proteins involved in signal transduction
    • Cavaldesi, M., Macchia, G., Barca, S., Defilippi, P., Tarone, G., and Petrucci, T.C. 1999. Association of the dystroglycan complex isolated from bovine brain synaptosomes with proteins involved in signal transduction. J. Neurochem. 72: 1648-1655.
    • (1999) J. Neurochem. , vol.72 , pp. 1648-1655
    • Cavaldesi, M.1    Macchia, G.2    Barca, S.3    Defilippi, P.4    Tarone, G.5    Petrucci, T.C.6
  • 18
    • 0031014645 scopus 로고    scopus 로고
    • Mechanical strain tightly controls fibroblast growth factor-2 release from cultured human vascular smooth muscle cells
    • Cheng, G.C., Briggs, W.H., Gerson, D.S., Libby, P., Grodzinsky, A.J., Gray, M.L., and Lee, R.T. 1997. Mechanical strain tightly controls fibroblast growth factor-2 release from cultured human vascular smooth muscle cells. Circ. Res. 80: 28-36.
    • (1997) Circ. Res. , vol.80 , pp. 28-36
    • Cheng, G.C.1    Briggs, W.H.2    Gerson, D.S.3    Libby, P.4    Grodzinsky, A.J.5    Gray, M.L.6    Lee, R.T.7
  • 19
    • 2342451911 scopus 로고    scopus 로고
    • G-protein coupled receptors in lipid rafts and caveolae: How, when and why do they go there?
    • Chini, B., and Parenti, M. 2004. G-protein coupled receptors in lipid rafts and caveolae: how, when and why do they go there? J. Mol. Endocrinol. 32: 325-338.
    • (2004) J. Mol. Endocrinol. , vol.32 , pp. 325-338
    • Chini, B.1    Parenti, M.2
  • 20
    • 0027452338 scopus 로고
    • Relevance of classification by size to topographical differences in bronchial smooth muscle response
    • Chitano, P., Sigurdsson, S.B., Halayko, A.J., and Stephens, N.L. 1993. Relevance of classification by size to topographical differences in bronchial smooth muscle response. J. Appl. Physiol. 75: 2013-2021.
    • (1993) J. Appl. Physiol. , vol.75 , pp. 2013-2021
    • Chitano, P.1    Sigurdsson, S.B.2    Halayko, A.J.3    Stephens, N.L.4
  • 21
    • 0028113411 scopus 로고
    • Signal transduction of a G protein-coupled receptor in caveolae: Colocalization of endothelin and its receptor with caveolin
    • Chun, M., Liyanage, U.K., Lisanti, M.P., and Lodish, H.F. 1994. Signal transduction of a G protein-coupled receptor in caveolae: colocalization of endothelin and its receptor with caveolin. Proc. Natl. Acad. Sci. U.S.A. 91: 11728-11732.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11728-11732
    • Chun, M.1    Liyanage, U.K.2    Lisanti, M.P.3    Lodish, H.F.4
  • 22
    • 0035139829 scopus 로고    scopus 로고
    • Prevention of cardiomyopathy in mouse models lacking the smooth muscle sarcoglycan-sarcospan complex
    • Cohn, R.D., Durbeej, M., Moore, S.A., Coral-Vazquez, R., Prouty, S., and Campbell, K.P. 2001. Prevention of cardiomyopathy in mouse models lacking the smooth muscle sarcoglycan-sarcospan complex. J. Clin. Invest. 107: R1-R7.
    • (2001) J. Clin. Invest. , vol.107
    • Cohn, R.D.1    Durbeej, M.2    Moore, S.A.3    Coral-Vazquez, R.4    Prouty, S.5    Campbell, K.P.6
  • 24
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins
    • Couet, J., Li, S., Okamoto, T., Ikezu, T., and Lisanti, M.P. 1997a. Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins. J. Biol. Chem. 272: 6525-6533.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6525-6533
    • Couet, J.1    Li, S.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 25
    • 0030731231 scopus 로고    scopus 로고
    • Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities
    • Couet, J., Sargiacomo, M., and Lisanti, M.P. 1997b. Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities. J. Biol. Chem. 272: 30429-30438.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30429-30438
    • Couet, J.1    Sargiacomo, M.2    Lisanti, M.P.3
  • 26
    • 0034537052 scopus 로고    scopus 로고
    • Caveolae from canine airway smooth muscle contain the necessary components for a role in Ca(2+) handling
    • Darby, P.J., Kwan, C.Y., and Daniel, E.E. 2000. Caveolae from canine airway smooth muscle contain the necessary components for a role in Ca(2+) handling. Am. J. Physiol. Lung Cell. Mol. Physiol. 279: L1226-L1235.
    • (2000) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.279
    • Darby, P.J.1    Kwan, C.Y.2    Daniel, E.E.3
  • 27
  • 29
    • 0032577647 scopus 로고    scopus 로고
    • Caveolin-mediated regulation of signaling along the p42/44 map kinase cascade in vivo. A role for the caveolin-scaffolding domain
    • Engelman, J.A., Chu, C., Lin, A., Jo, H., Ikezu, T., Okamoto, T., Kohtz, D.S., and Lisanti, M.P. 1998. Caveolin-mediated regulation of signaling along the p42/44 map kinase cascade in vivo. A role for the caveolin-scaffolding domain. FEBS Lett. 428: 205-211.
    • (1998) FEBS Lett. , vol.428 , pp. 205-211
    • Engelman, J.A.1    Chu, C.2    Lin, A.3    Jo, H.4    Ikezu, T.5    Okamoto, T.6    Kohtz, D.S.7    Lisanti, M.P.8
  • 30
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti, J.M., and Campbell, K.P. 1993. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell. Biol. 122: 809-823.
    • (1993) J. Cell. Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 34
    • 0029086362 scopus 로고
    • De novo formation of caveolae in lymphocytes by expression of vip21-caveolin
    • Fra, A.M., Williamson, E., Simons, K., and Parton, R.G. 1995. De novo formation of caveolae in lymphocytes by expression of vip21-caveolin. Proc. Natl. Acad. Sci. U.S.A. 92: 8655-8659.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8655-8659
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 35
    • 5044234356 scopus 로고    scopus 로고
    • Caveolin-1 and caveolae in atherosclerosis: Differential roles in fatty streak formation and neointimal hyperplasia
    • Frank, P.G., and Lisanti, M.P. 2004. Caveolin-1 and caveolae in atherosclerosis: differential roles in fatty streak formation and neointimal hyperplasia. Curr. Opin. Lipidol. 15: 523-529.
    • (2004) Curr. Opin. Lipidol. , vol.15 , pp. 523-529
    • Frank, P.G.1    Lisanti, M.P.2
  • 36
    • 0028025190 scopus 로고
    • Multiple phenotypically distinct smooth muscle cell populations exist in the adult and developing bovine pulmonary arterial media in vivo
    • Frid, M.G., Moiseeva, E.P., and Stenmark, K.R. 1994. Multiple phenotypically distinct smooth muscle cell populations exist in the adult and developing bovine pulmonary arterial media in vivo. Circ. Res. 75: 669-681.
    • (1994) Circ. Res. , vol.75 , pp. 669-681
    • Frid, M.G.1    Moiseeva, E.P.2    Stenmark, K.R.3
  • 37
    • 0030731797 scopus 로고    scopus 로고
    • Smooth muscle cells isolated from discrete compartments of the mature vascular media exhibit unique phenotypes and distinct growth capabilities
    • Frid, M.G., Aldashev, A.A., Dempsey, E.C., and Stenmark, K.R. 1997. Smooth muscle cells isolated from discrete compartments of the mature vascular media exhibit unique phenotypes and distinct growth capabilities. Circ. Res. 81: 940-952.
    • (1997) Circ. Res. , vol.81 , pp. 940-952
    • Frid, M.G.1    Aldashev, A.A.2    Dempsey, E.C.3    Stenmark, K.R.4
  • 38
    • 0027102133 scopus 로고
    • Localization of inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae
    • Fujimoto, T., Nakade, S., Miyawaki, A., Mikoshiba, K., and Ogawa, K. 1992. Localization of inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae. J. Cell. Biol. 119: 1507-1513.
    • (1992) J. Cell. Biol. , vol.119 , pp. 1507-1513
    • Fujimoto, T.1    Nakade, S.2    Miyawaki, A.3    Mikoshiba, K.4    Ogawa, K.5
  • 39
    • 0027452708 scopus 로고
    • Calcium pump of the plasma membrane is localized in caveolae
    • Fujimoto, T. 1993. Calcium pump of the plasma membrane is localized in caveolae. J. Cell. Biol. 120: 1147-1157.
    • (1993) J. Cell. Biol. , vol.120 , pp. 1147-1157
    • Fujimoto, T.1
  • 40
    • 0017077247 scopus 로고
    • Quantitative morphological study of smooth muscle cells of the guinea-pig taenia coli
    • Gabella, G. 1976. Quantitative morphological study of smooth muscle cells of the guinea-pig taenia coli. Cell Tissue Res. 170: 161-186.
    • (1976) Cell Tissue Res. , vol.170 , pp. 161-186
    • Gabella, G.1
  • 41
    • 0024337128 scopus 로고
    • Development of smooth muscle: Ultrastructural study of the chick embryo gizzard
    • Gabella, G. 1989. Development of smooth muscle: Ultrastructural study of the chick embryo gizzard. Anat. Embryol. (Berl.), 180: 213-226.
    • (1989) Anat. Embryol. (Berl.) , vol.180 , pp. 213-226
    • Gabella, G.1
  • 43
    • 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
    • Gerthoffer, W.T., and Gunst, S.J. 2001. Invited review: focal adhesion and small heat shock proteins in the regulation of actin remodeling and contractility in smooth muscle. J. Appl. Physiol. 91: 963-972.
    • (2001) J. Appl. Physiol. , vol.91 , pp. 963-972
    • Gerthoffer, W.T.1    Gunst, S.J.2
  • 44
    • 0033580697 scopus 로고    scopus 로고
    • Differential involvement of Gα12 and Gα13 in receptor-mediated stress fiber formation
    • Gohla, A., Offermanns, S., Wilkie, T.M., and Schultz, G. 1999. Differential involvement of Gα12 and Gα13 in receptor-mediated stress fiber formation. J. Biol. Chem. 274: 17901-17907.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17901-17907
    • Gohla, A.1    Offermanns, S.2    Wilkie, T.M.3    Schultz, G.4
  • 47
    • 2942685631 scopus 로고    scopus 로고
    • Caveolae and caveolins in the cardiovascular system
    • Gratton, J.P., Bernatchez, P., and Sessa, W.C. 2004. Caveolae and caveolins in the cardiovascular system. Circ. Res. 94: 1408-1417.
    • (2004) Circ. Res. , vol.94 , pp. 1408-1417
    • Gratton, J.P.1    Bernatchez, P.2    Sessa, W.C.3
  • 48
    • 0141680432 scopus 로고    scopus 로고
    • Cytoskeletal remodeling of the airway smooth muscle cell: A mechanism for adaptation to mechanical forces in the lung
    • Gunst, S.J., Tang, D.D., and Opazo Saez, A. 2003. Cytoskeletal remodeling of the airway smooth muscle cell: A mechanism for adaptation to mechanical forces in the lung. Respir. Physiol. Neurobiol. 137: 151-168.
    • (2003) Respir. Physiol. Neurobiol. , vol.137 , pp. 151-168
    • Gunst, S.J.1    Tang, D.D.2    Opazo Saez, A.3
  • 49
    • 0033885496 scopus 로고    scopus 로고
    • Differential requirement for individual sarcoglycans and dystrophin in the assembly and function of the dystrophin-glycoprotein complex
    • Hack, A.A., Lam, M.Y., Cordier, L., Shoturma, D.I., Ly, C.T., Hadhazy, M.A., Hadhazy, M.R., Sweeney, H.L., and McNally, E.M. 2000. Differential requirement for individual sarcoglycans and dystrophin in the assembly and function of the dystrophin-glycoprotein complex. J. Cell. Sci. 113(Pt 14): 2535-2544.
    • (2000) J. Cell. Sci. , vol.113 , Issue.PART 14 , pp. 2535-2544
    • Hack, A.A.1    Lam, M.Y.2    Cordier, L.3    Shoturma, D.I.4    Ly, C.T.5    Hadhazy, M.A.6    Hadhazy, M.R.7    Sweeney, H.L.8    McNally, E.M.9
  • 53
    • 0035164457 scopus 로고    scopus 로고
    • Molecular mechanisms of phenotypic plasticity in smooth muscle cells
    • Halayko, A.J., and Solway, J. 2001. Molecular mechanisms of phenotypic plasticity in smooth muscle cells. J. Appl. Physiol. 90: 358-368.
    • (2001) J. Appl. Physiol. , vol.90 , pp. 358-368
    • Halayko, A.J.1    Solway, J.2
  • 54
    • 0141792277 scopus 로고    scopus 로고
    • Mechanisms of inflammation-mediated airway smooth muscle plasticity and airways remodeling in asthma
    • Halayko, A.J., and Amrani, Y. 2003. Mechanisms of inflammation-mediated airway smooth muscle plasticity and airways remodeling in asthma. Respir. Physiol. Neurobiol. 137: 209-222.
    • (2003) Respir. Physiol. Neurobiol. , vol.137 , pp. 209-222
    • Halayko, A.J.1    Amrani, Y.2
  • 56
    • 0023713505 scopus 로고
    • Diverse effects of fibronectin and laminin on phenotypic properties of cultured arterial smooth muscle cells
    • Hedin, U., Bottger, B.A., Forsberg, E., Johansson, S., and Thyberg, J. 1988. Diverse effects of fibronectin and laminin on phenotypic properties of cultured arterial smooth muscle cells. J. Cell. Biol. 107: 307-319.
    • (1988) J. Cell. Biol. , vol.107 , pp. 307-319
    • Hedin, U.1    Bottger, B.A.2    Forsberg, E.3    Johansson, S.4    Thyberg, J.5
  • 58
    • 0033823661 scopus 로고    scopus 로고
    • Differential effects of extracellular matrix proteins on human airway smooth muscle cell proliferation and phenotype
    • Hirst, S.J., Twort, C.H., and Lee, T.H. 2000a. Differential effects of extracellular matrix proteins on human airway smooth muscle cell proliferation and phenotype. Am. J. Respir. Cell Mol. Biol. 23: 335-344.
    • (2000) Am. J. Respir. Cell Mol. Biol. , vol.23 , pp. 335-344
    • Hirst, S.J.1    Twort, C.H.2    Lee, T.H.3
  • 59
    • 0033911653 scopus 로고    scopus 로고
    • Phenotypic diversity and molecular mechanisms of airway smooth muscle proliferation in asthma
    • Hirst, S.J., Walker, T.R., and Chilvers, E.R. 2000b. Phenotypic diversity and molecular mechanisms of airway smooth muscle proliferation in asthma. Eur. Respir. J. 16: 159-177.
    • (2000) Eur. Respir. J. , vol.16 , pp. 159-177
    • Hirst, S.J.1    Walker, T.R.2    Chilvers, E.R.3
  • 60
    • 0037303578 scopus 로고    scopus 로고
    • Endothelin-1 activates mesangial cell ERK1/2 via EGF-receptor transactivation and caveolin-1 interaction
    • Hua, H., Munk, S., and Whiteside, C.I. 2003. Endothelin-1 activates mesangial cell ERK1/2 via EGF-receptor transactivation and caveolin-1 interaction. Am. J. Physiol. Renal Physiol. 284: F303-F312.
    • (2003) Am. J. Physiol. Renal Physiol. , vol.284
    • Hua, H.1    Munk, S.2    Whiteside, C.I.3
  • 61
    • 0034027602 scopus 로고    scopus 로고
    • Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin
    • James, M., Nuttall, A., Ilsley, J.L., Ottersbach, K., Tinsley, J.M., Sudol, M., and Winder, S.J. 2000. Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin. J. Cell. Sci. 113(Pt 10): 1717-1726.
    • (2000) J. Cell. Sci. , vol.113 , Issue.PART 10 , pp. 1717-1726
    • James, M.1    Nuttall, A.2    Ilsley, J.L.3    Ottersbach, K.4    Tinsley, J.M.5    Sudol, M.6    Winder, S.J.7
  • 62
    • 0036086743 scopus 로고    scopus 로고
    • 2+ regulation in airway smooth muscle contraction: Do the data contradict dogma?
    • 2+ regulation in airway smooth muscle contraction: Do the data contradict dogma? Am. J. Physiol. Lung Cell. Mol. Physiol. 282: L1161-1178.
    • (2002) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.282
    • Janssen, L.J.1
  • 64
    • 0027024915 scopus 로고
    • Ragweed sensitization-induced increase of myosin light chain kinase content in canine airway smooth muscle
    • Jiang, H., Rao, K., Halayko, A.J., Liu, X., and Stephens, N.L. 1992. Ragweed sensitization-induced increase of myosin light chain kinase content in canine airway smooth muscle. Am. J. Respir. Cell. Mol. Biol. 7: 567-573.
    • (1992) Am. J. Respir. Cell. Mol. Biol. , vol.7 , pp. 567-573
    • Jiang, H.1    Rao, K.2    Halayko, A.J.3    Liu, X.4    Stephens, N.L.5
  • 66
    • 0032853363 scopus 로고    scopus 로고
    • The mechanics of ex-aggerated airway narrowing in asthma: The role of smooth muscle
    • King, G.G., Pare, P.D., and Seow, C.Y. 1999. The mechanics of ex-aggerated airway narrowing in asthma: the role of smooth muscle. Respir. Physiol. 118: 1-13.
    • (1999) Respir. Physiol. , vol.118 , pp. 1-13
    • King, G.G.1    Pare, P.D.2    Seow, C.Y.3
  • 67
    • 0034616292 scopus 로고    scopus 로고
    • Agonists trigger g protein-mediated activation of the cpi-17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility
    • Kitazawa, T., Eto, M., Woodsome, T.P., and Brautigan, D.L. 2000. Agonists trigger g protein-mediated activation of the cpi-17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility. J. Biol. Chem. 275: 9897-9900.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9897-9900
    • Kitazawa, T.1    Eto, M.2    Woodsome, T.P.3    Brautigan, D.L.4
  • 69
    • 3142582011 scopus 로고    scopus 로고
    • Caveolins: Structure and function in signal transduction
    • Krajewska, W.M., and Maslowska, I. 2004. Caveolins: structure and function in signal transduction. Cell. Mol. Biol. Lett. 9: 195-220.
    • (2004) Cell. Mol. Biol. Lett. , vol.9 , pp. 195-220
    • Krajewska, W.M.1    Maslowska, I.2
  • 70
    • 0038819983 scopus 로고    scopus 로고
    • Ccaat/enhancer-binding protein and activator protein-1 transcription factors regulate the expression of interleukin-8 through the mitogen-activated protein kinase pathways in response to mechanical stretch of human airway smooth muscle cells
    • Kumar, A., Knox, A.J., and Boriek, A.M. 2003. Ccaat/enhancer-binding protein and activator protein-1 transcription factors regulate the expression of interleukin-8 through the mitogen-activated protein kinase pathways in response to mechanical stretch of human airway smooth muscle cells. J. Biol. Chem. 278: 18868-18876.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18868-18876
    • Kumar, A.1    Knox, A.J.2    Boriek, A.M.3
  • 71
    • 0035059170 scopus 로고    scopus 로고
    • Myosin thick filament lability induced by mechanical strain in airway smooth muscle
    • Kuo, K.H., Wang, L., Pare, P.D., Ford, L.E., and Seow, C.Y. 2001. Myosin thick filament lability induced by mechanical strain in airway smooth muscle. J. Appl. Physiol. 90: 1811-1816.
    • (2001) J. Appl. Physiol. , vol.90 , pp. 1811-1816
    • Kuo, K.H.1    Wang, L.2    Pare, P.D.3    Ford, L.E.4    Seow, C.Y.5
  • 73
    • 0020056168 scopus 로고
    • Developmental changes in the plasma membrane of gizzard smooth muscle of the chicken. A freeze-fracture study
    • La Mantia, J., and Shafiq, S.A. 1982. Developmental changes in the plasma membrane of gizzard smooth muscle of the chicken. A freeze-fracture study. J. Anat. 134 (Pt 2): 243-253.
    • (1982) J. Anat. , vol.134 , Issue.PART 2 , pp. 243-253
    • La Mantia, J.1    Shafiq, S.A.2
  • 74
    • 2342621479 scopus 로고    scopus 로고
    • The dystrophin glycoprotein complex: Signaling strength and integrity for the sarcolemma
    • Lapidos, K.A., Kakkar, R., and McNally, E.M. 2004. The dystrophin glycoprotein complex: signaling strength and integrity for the sarcolemma. Circ. Res. 94: 1023-1031.
    • (2004) Circ. Res. , vol.94 , pp. 1023-1031
    • Lapidos, K.A.1    Kakkar, R.2    McNally, E.M.3
  • 75
    • 0036917649 scopus 로고    scopus 로고
    • Effects of beta2-agonists on airway tone and bronchial responsiveness
    • Larj, M.J., and Bleecker, E.R. 2002. Effects of beta2-agonists on airway tone and bronchial responsiveness. J. Allergy Clin. Immunol. 110: S304-S312.
    • (2002) J. Allergy Clin. Immunol. , vol.110
    • Larj, M.J.1    Bleecker, E.R.2
  • 77
    • 0031667962 scopus 로고    scopus 로고
    • Mutational analysis of caveolin-induced vesicle formation. Expression of caveolin-1 recruits caveolin-2 to caveolae membranes
    • Li, S., Galbiati, F., Volonte, D., Sargiacomo, M., Engelman, J.A., Das, K., Scherer, P.E., and Lisanti, M.P. 1998. Mutational analysis of caveolin-induced vesicle formation. Expression of caveolin-1 recruits caveolin-2 to caveolae membranes. FEBS Lett. 434: 127-134.
    • (1998) FEBS Lett. , vol.434 , pp. 127-134
    • Li, S.1    Galbiati, F.2    Volonte, D.3    Sargiacomo, M.4    Engelman, J.A.5    Das, K.6    Scherer, P.E.7    Lisanti, M.P.8
  • 78
    • 9744229896 scopus 로고    scopus 로고
    • Effect of actin microfilament on potassium current in guinea pig gastric myocytes
    • Li, X.L., Zheng, H.F., Jin, Z.Y., Yang, M., Li, Z.L., and Xu, W.X. 2004. Effect of actin microfilament on potassium current in guinea pig gastric myocytes. World J. Gastroenterol. 10: 3303-3307.
    • (2004) World J. Gastroenterol. , vol.10 , pp. 3303-3307
    • Li, X.L.1    Zheng, H.F.2    Jin, Z.Y.3    Yang, M.4    Li, Z.L.5    Xu, W.X.6
  • 80
    • 4644346591 scopus 로고    scopus 로고
    • Gaq-receptor coupled signaling induces rho-dependent transcription of smooth muscle specific genes in cultured airway myocytes
    • Liu, H.W., Kassiri, K., Vörös, A., Hillier, C.T., Wang, L., Solway, J., and Halayko, A.J. 2002. Gaq-receptor coupled signaling induces rho-dependent transcription of smooth muscle specific genes in cultured airway myocytes. Am. J. Crit. Care Med. 165: A670.
    • (2002) Am. J. Crit. Care Med. , vol.165
    • Liu, H.W.1    Kassiri, K.2    Vörös, A.3    Hillier, C.T.4    Wang, L.5    Solway, J.6    Halayko, A.J.7
  • 83
    • 0033585061 scopus 로고    scopus 로고
    • Mechanical strain increases pdgf-b and pdgf beta receptor expression in vascular smooth muscle cells
    • Ma, Y.H., Ling, S., and Ives, H.E. 1999. Mechanical strain increases pdgf-b and pdgf beta receptor expression in vascular smooth muscle cells. Biochem. Biophys. Res. Commun. 265: 606-610.
    • (1999) Biochem. Biophys. Res. Commun. , vol.265 , pp. 606-610
    • Ma, Y.H.1    Ling, S.2    Ives, H.E.3
  • 84
    • 0035808389 scopus 로고    scopus 로고
    • Smooth muscle differentiation marker gene expression is regulated by rhoa-mediated actin polymerization
    • Mack, C.P., Somlyo, A.V., Hautmann, M., Somlyo, A.P., and Owens, G.K. 2001. Smooth muscle differentiation marker gene expression is regulated by rhoa-mediated actin polymerization. J. Biol. Chem. 276: 341-347.
    • (2001) J. Biol. Chem. , vol.276 , pp. 341-347
    • Mack, C.P.1    Somlyo, A.V.2    Hautmann, M.3    Somlyo, A.P.4    Owens, G.K.5
  • 85
    • 0036135735 scopus 로고    scopus 로고
    • Circumferential stretching of saphenous vein smooth muscle enhances vasoconstrictor responses by rho kinase-dependent pathways
    • McGregor, E., Gosling, M., Beattie, D.K., Ribbons, D.M., Davies, A.H., and Powell, J.T. 2002. Circumferential stretching of saphenous vein smooth muscle enhances vasoconstrictor responses by rho kinase-dependent pathways. Cardiovasc. Res. 53: 219-226.
    • (2002) Cardiovasc. Res. , vol.53 , pp. 219-226
    • McGregor, E.1    Gosling, M.2    Beattie, D.K.3    Ribbons, D.M.4    Davies, A.H.5    Powell, J.T.6
  • 88
    • 0026785988 scopus 로고
    • Dystrophin at the plasma membrane of human muscle fibers shows a costameric localization
    • Minetti, C., Beltrame, F., Marcenaro, G., and Bonilla, E. 1992. Dystrophin at the plasma membrane of human muscle fibers shows a costameric localization. Neuromuscul. Disord. 2: 99-109.
    • (1992) Neuromuscul. Disord. , vol.2 , pp. 99-109
    • Minetti, C.1    Beltrame, F.2    Marcenaro, G.3    Bonilla, E.4
  • 89
    • 0031889342 scopus 로고    scopus 로고
    • Disorganization of dystrophin costameric lattice in becker muscular dystrophy
    • Minetti, C., Cordone, G., Beltrame, F., Bado, M., and Bonilla, E. 1998. Disorganization of dystrophin costameric lattice in becker muscular dystrophy. Muscle Nerve, 21: 211-216.
    • (1998) Muscle Nerve , vol.21 , pp. 211-216
    • Minetti, C.1    Cordone, G.2    Beltrame, F.3    Bado, M.4    Bonilla, E.5
  • 90
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control srf activity by regulation of its coactivator mal
    • Miralles, F., Posern, G., Zaromytidou, A.I., and Treisman, R. 2003. Actin dynamics control srf activity by regulation of its coactivator mal. Cell, 113: 329-342.
    • (2003) Cell , vol.113 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaromytidou, A.I.3    Treisman, R.4
  • 92
    • 0018610892 scopus 로고
    • Inhomogeneous distribution of filipin-sterol complexes in smooth muscle cell plasma membrane
    • Montesano, R. 1979. Inhomogeneous distribution of filipin-sterol complexes in smooth muscle cell plasma membrane. Nature (London), 280: 328-329.
    • (1979) Nature (London) , vol.280 , pp. 328-329
    • Montesano, R.1
  • 95
    • 0027476106 scopus 로고
    • Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle
    • North, A.J., Galazkiewicz, B., Byers, T.J., Glenney, J.R., and Small, J.V. 1993. Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle. J. Cell. Biol. 120: 1159-1167.
    • (1993) J. Cell. Biol. , vol.120 , pp. 1159-1167
    • North, A.J.1    Galazkiewicz, B.2    Byers, T.J.3    Glenney, J.R.4    Small, J.V.5
  • 96
    • 0028196621 scopus 로고
    • Actin isoform compartments in chicken gizzard smooth muscle cells
    • North, A.J., Gimona, M., Lando, Z., and Small, J.V. 1994. Actin isoform compartments in chicken gizzard smooth muscle cells. J. Cell Sci. 107(Pt 3): 445-455.
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 3 , pp. 445-455
    • North, A.J.1    Gimona, M.2    Lando, Z.3    Small, J.V.4
  • 97
    • 0035878634 scopus 로고    scopus 로고
    • 2+ transients and distribution of BK channels and ryanodine receptors in smooth muscle cells of guinea-pig vas deferens and urinary bladder
    • 2+ transients and distribution of BK channels and ryanodine receptors in smooth muscle cells of guinea-pig vas deferens and urinary bladder. J. Physiol. 534: 313-326.
    • (2001) J. Physiol. , vol.534 , pp. 313-326
    • Ohi, Y.1    Yamamura, H.2    Nagano, N.3    Ohya, S.4    Muraki, K.5    Watanabe, M.6    Imaizumi, Y.7
  • 98
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing "pre-assembled signaling complexes" at the plasma membrane
    • Okamoto, T., Schlegel, A., Scherer, P.E., and Lisanti, M.P. 1998. Caveolins, a family of scaffolding proteins for organizing "pre-assembled signaling complexes" at the plasma membrane. J. Biol. Chem. 273: 5419-5422.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 99
    • 0036180964 scopus 로고    scopus 로고
    • New determinants of receptor-effector coupling: Trafficking and compartmentation in membrane microdomains
    • Ostrom, R.S. 2002. New determinants of receptor-effector coupling: trafficking and compartmentation in membrane microdomains. Mol. Pharmacol. 61: 473-476.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 473-476
    • Ostrom, R.S.1
  • 100
    • 13644263174 scopus 로고    scopus 로고
    • Caveolins muscle their way into the regulation of cell differentiation, development, and function. Focus on "muscle-specific interaction of caveolin isoforms: Differential complex formation between caveolins in fibroblastic vs. Muscle cells"
    • Ostrom, R.S. 2005. Caveolins muscle their way into the regulation of cell differentiation, development, and function. Focus on "muscle-specific interaction of caveolin isoforms: differential complex formation between caveolins in fibroblastic vs. Muscle cells". Am. J. Physiol. Cell Physiol. 288: C507-C509.
    • (2005) Am. J. Physiol. Cell Physiol. , vol.288
    • Ostrom, R.S.1
  • 101
    • 4744346615 scopus 로고    scopus 로고
    • The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: Implications for molecular pharmacology
    • Ostrom, R.S., and Insel, P.A. 2004. The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: implications for molecular pharmacology. Br. J. Pharmacol. 143: 235-245.
    • (2004) Br. J. Pharmacol. , vol.143 , pp. 235-245
    • Ostrom, R.S.1    Insel, P.A.2
  • 102
    • 0035834749 scopus 로고    scopus 로고
    • Receptor number and caveolar colocalization determine receptor coupling efficiency to adenylyl cyclase
    • Ostrom, R.S., Gregorian, C., Drenan, R.M., Xiang, Y., Regan, J.W., and Insel, P.A. 2001. Receptor number and caveolar colocalization determine receptor coupling efficiency to adenylyl cyclase. J. Biol. Chem. 276: 42063-42069.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42063-42069
    • Ostrom, R.S.1    Gregorian, C.2    Drenan, R.M.3    Xiang, Y.4    Regan, J.W.5    Insel, P.A.6
  • 103
    • 0029048550 scopus 로고
    • Regulation of differentiation of vascular smooth muscle cells
    • Owens, G.K. 1995. Regulation of differentiation of vascular smooth muscle cells. Physiol. Rev. 75: 487-517.
    • (1995) Physiol. Rev. , vol.75 , pp. 487-517
    • Owens, G.K.1
  • 104
    • 3042588831 scopus 로고    scopus 로고
    • Molecular regulation of vascular smooth muscle cell differentiation in development and disease
    • Owens, G.K., Kumar, M.S., and Wamhoff, B.R. 2004. Molecular regulation of vascular smooth muscle cell differentiation in development and disease. Physiol. Rev. 84: 767-801.
    • (2004) Physiol. Rev. , vol.84 , pp. 767-801
    • Owens, G.K.1    Kumar, M.S.2    Wamhoff, B.R.3
  • 105
    • 0032161343 scopus 로고    scopus 로고
    • Effects of LTD4 on human airway smooth muscle cell proliferation, matrix expression, and contraction in vitro: Differential sensitivity to cysteinyl leukotriene receptor antagonists
    • Panettieri, R.A., Tan, E.M., Ciocca, V., Luttmann, M.A., Leonard, T.B., and Hay, D.W. 1998. Effects of LTD4 on human airway smooth muscle cell proliferation, matrix expression, and contraction in vitro: differential sensitivity to cysteinyl leukotriene receptor antagonists. Am. J. Respir. Cell Mol. Biol. 19: 453-461.
    • (1998) Am. J. Respir. Cell Mol. Biol. , vol.19 , pp. 453-461
    • Panettieri, R.A.1    Tan, E.M.2    Ciocca, V.3    Luttmann, M.A.4    Leonard, T.B.5    Hay, D.W.6
  • 108
    • 1842527083 scopus 로고    scopus 로고
    • Regulation of smooth muscle contraction by calcium, monomeric GTPases of the Rho subfamily and their effector kinases
    • Pfitzer, G., Wirth, A., Lucius, C., Brkic-Koric, D., Manser, E., de Lanerolle, P., and Arner, A. 2003. Regulation of smooth muscle contraction by calcium, monomeric GTPases of the Rho subfamily and their effector kinases. Adv. Exp. Med. Biol. 538: 89-99.
    • (2003) Adv. Exp. Med. Biol. , vol.538 , pp. 89-99
    • Pfitzer, G.1    Wirth, A.2    Lucius, C.3    Brkic-Koric, D.4    Manser, E.5    De Lanerolle, P.6    Arner, A.7
  • 109
    • 0042329370 scopus 로고    scopus 로고
    • + channels in coronary artery smooth muscle cells
    • + channels in coronary artery smooth muscle cells. Pflugers Arch. 446: 523-528.
    • (2003) Pflugers Arch. , vol.446 , pp. 523-528
    • Piao, L.1    Ho, W.K.2    Earm, Y.E.3
  • 111
    • 0035213597 scopus 로고    scopus 로고
    • Caveolin-deficient mice: Insights into caveolar function human disease
    • Razani, B., and Lisanti, M.P. 2001a. Caveolin-deficient mice: Insights into caveolar function human disease. J. Clin. Invest. 108: 1553-1561.
    • (2001) J. Clin. Invest. , vol.108 , pp. 1553-1561
    • Razani, B.1    Lisanti, M.P.2
  • 112
    • 0035890289 scopus 로고    scopus 로고
    • Caveolins and caveolae: Molecular and functional relationships
    • Razani, B., and Lisanti, M.P. 2001b. Caveolins and caveolae: molecular and functional relationships. Exp. Cell. Res. 271: 36-44.
    • (2001) Exp. Cell. Res. , vol.271 , pp. 36-44
    • Razani, B.1    Lisanti, M.P.2
  • 114
    • 0036733284 scopus 로고    scopus 로고
    • Caveolae: From cell biology to animal physiology
    • Razani, B., Woodman, S.E., and Lisanti, M.P. 2002. Caveolae: from cell biology to animal physiology. Pharmacol. Rev. 54: 431-467.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 431-467
    • Razani, B.1    Woodman, S.E.2    Lisanti, M.P.3
  • 115
    • 0033552596 scopus 로고    scopus 로고
    • Cell elongation induces laminin alpha2 chain expression in mouse embryonic mesenchymal cells: Role in visceral myogenesis
    • Relan, N.K., Yang, Y., Beqaj, S., Miner, J.H., and Schuger, L. 1999. Cell elongation induces laminin alpha2 chain expression in mouse embryonic mesenchymal cells: role in visceral myogenesis. J. Cell. Biol. 147: 1341-1350.
    • (1999) J. Cell. Biol. , vol.147 , pp. 1341-1350
    • Relan, N.K.1    Yang, Y.2    Beqaj, S.3    Miner, J.H.4    Schuger, L.5
  • 117
    • 0030583157 scopus 로고    scopus 로고
    • Localization of the dystrophin binding site at the carboxyl terminus of beta-dystroglycan
    • Rosa, G., Ceccarini, M., Cavaldesi, M., Zini, M., and Petrucci, T.C. 1996. Localization of the dystrophin binding site at the carboxyl terminus of beta-dystroglycan. Biochem. Biophys. Res. Commun. 223: 272-277.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 272-277
    • Rosa, G.1    Ceccarini, M.2    Cavaldesi, M.3    Zini, M.4    Petrucci, T.C.5
  • 119
    • 0034605070 scopus 로고    scopus 로고
    • The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin
    • Rybakova, I.N., Patel, J.R., and Ervasti, J.M. 2000. The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J. Cell. Biol. 150: 1209-1214.
    • (2000) J. Cell. Biol. , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 120
    • 0036182481 scopus 로고    scopus 로고
    • Agonist-induced translocation of the kinin B(1) receptor to caveolae-related rafts
    • Sabourin, T., Bastien, L., Bachvarov, D.R., and Marceau, F. 2002. Agonist-induced translocation of the kinin B(1) receptor to caveolae-related rafts. Mol. Pharmacol. 61: 546-553.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 546-553
    • Sabourin, T.1    Bastien, L.2    Bachvarov, D.R.3    Marceau, F.4
  • 121
    • 0030612005 scopus 로고    scopus 로고
    • Laminin alpha 1 chain synthesis in the mouse developing lung: Requirement for epithelial-mesenchymal contact and possible role in bronchial smooth muscle development
    • Schuger, L., Skubitz, A.P., Zhang, J., Sorokin, L., and He, L. 1997. Laminin alpha 1 chain synthesis in the mouse developing lung: requirement for epithelial-mesenchymal contact and possible role in bronchial smooth muscle development. J. Cell. Biol. 139: 553-562.
    • (1997) J. Cell. Biol. , vol.139 , pp. 553-562
    • Schuger, L.1    Skubitz, A.P.2    Zhang, J.3    Sorokin, L.4    He, L.5
  • 122
    • 0033763133 scopus 로고    scopus 로고
    • Response of arterial smooth muscle to length perturbation
    • Seow, C.Y. 2000. Response of arterial smooth muscle to length perturbation. J. Appl. Physiol. 89: 2065-2072.
    • (2000) J. Appl. Physiol. , vol.89 , pp. 2065-2072
    • Seow, C.Y.1
  • 123
    • 0032446186 scopus 로고    scopus 로고
    • The cytoskeleton of the vertebrate smooth muscle cell
    • Small, J.V., and Gimona, M. 1998. The cytoskeleton of the vertebrate smooth muscle cell. Acta Physiol. Scand. 164: 341-348.
    • (1998) Acta Physiol. Scand. , vol.164 , pp. 341-348
    • Small, J.V.1    Gimona, M.2
  • 125
    • 0033764772 scopus 로고    scopus 로고
    • Selected contribution: Mechanical strain increases force production and calcium sensitivity in cultured airway smooth muscle cells
    • Smith, P.G., Roy, C., Fisher, S., Huang, Q.Q., and Brozovich, F. 2000. Selected contribution: mechanical strain increases force production and calcium sensitivity in cultured airway smooth muscle cells. J. Appl. Physiol. 89: 2092-2098.
    • (2000) J. Appl. Physiol. , vol.89 , pp. 2092-2098
    • Smith, P.G.1    Roy, C.2    Fisher, S.3    Huang, Q.Q.4    Brozovich, F.5
  • 126
    • 0037383931 scopus 로고    scopus 로고
    • Mechanical stress increases RhoA activation in airway smooth muscle cells
    • Smith, P.G., Roy, C., Zhang, Y.N., and Chauduri, S. 2003a. Mechanical stress increases RhoA activation in airway smooth muscle cells. Am. J. Respir. Cell. Mol. Biol. 28: 436-442.
    • (2003) Am. J. Respir. Cell. Mol. Biol. , vol.28 , pp. 436-442
    • Smith, P.G.1    Roy, C.2    Zhang, Y.N.3    Chauduri, S.4
  • 130
    • 15844401780 scopus 로고    scopus 로고
    • Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and cofractionates with dystrophin and dystrophin-associated glycoproteins
    • Song, K.S., Scherer, P.E., Tang, Z., Okamoto, T., Li, S., Chafel, M., Chu, C., Kohtz, D.S., and Lisanti, M.P 1996. Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and cofractionates with dystrophin and dystrophin-associated glycoproteins. J. Biol. Chem. 271: 15160-15165.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15160-15165
    • Song, K.S.1    Scherer, P.E.2    Tang, Z.3    Okamoto, T.4    Li, S.5    Chafel, M.6    Chu, C.7    Kohtz, D.S.8    Lisanti, M.P.9
  • 132
    • 0035807788 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins
    • Sotgia, F., Lee, H., Bedford, M.T., Petrucci, T., Sudol, M., and Lisanti, M.P. 2001. Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins. Biochemistry, 40: 14585-14592.
    • (2001) Biochemistry , vol.40 , pp. 14585-14592
    • Sotgia, F.1    Lee, H.2    Bedford, M.T.3    Petrucci, T.4    Sudol, M.5    Lisanti, M.P.6
  • 133
    • 2942604709 scopus 로고    scopus 로고
    • Dystroglycan, a scaffold for the ERK-map kinase cascade
    • Spence, H.J., Dhillon, A.S., James, M., and Winder, S.J. 2004. Dystroglycan, a scaffold for the ERK-map kinase cascade. EMBO Rep. 5: 484-489.
    • (2004) EMBO Rep. , vol.5 , pp. 484-489
    • Spence, H.J.1    Dhillon, A.S.2    James, M.3    Winder, S.J.4
  • 134
    • 1042291979 scopus 로고    scopus 로고
    • Comparative proteomics of human endothelial cell caveolae and rafts using two-dimensional gel electrophoresis and mass spectrometry
    • Sprenger, R.R., Speijer, D., Back, J.W., De Koster, C.G., Pannekoek, H., and Horrevoets, A.J. 2004. Comparative proteomics of human endothelial cell caveolae and rafts using two-dimensional gel electrophoresis and mass spectrometry. Electrophoresis, 25: 156-172.
    • (2004) Electrophoresis , vol.25 , pp. 156-172
    • Sprenger, R.R.1    Speijer, D.2    Back, J.W.3    De Koster, C.G.4    Pannekoek, H.5    Horrevoets, A.J.6
  • 135
    • 0033973279 scopus 로고    scopus 로고
    • Identification of filamin as a novel ligand for caveolin-1: Evidence for the organization of caveolin-1-associated membrane domains by the actin cytoskeleton
    • Stahlhut, M., and van Deurs, B. 2000. Identification of filamin as a novel ligand for caveolin-1: evidence for the organization of caveolin-1-associated membrane domains by the actin cytoskeleton. Mol. Biol. Cell. 11: 325-337.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 325-337
    • Stahlhut, M.1    Van Deurs, B.2
  • 136
    • 0033600605 scopus 로고    scopus 로고
    • Epsilon-sarcoglycan replaces alpha-sarcoglycan in smooth muscle to form a unique dystrophin-glycoprotein complex
    • Straub, V., Ettinger, A.J., Durbeej, M., Venzke, D.P., Cutshall, S., Sanes, J.R., and Campbell, K.P. 1999. Epsilon-sarcoglycan replaces alpha-sarcoglycan in smooth muscle to form a unique dystrophin-glycoprotein complex. J. Biol. Chem. 274: 27989-27996.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27989-27996
    • Straub, V.1    Ettinger, A.J.2    Durbeej, M.3    Venzke, D.P.4    Cutshall, S.5    Sanes, J.R.6    Campbell, K.P.7
  • 137
    • 0030881988 scopus 로고    scopus 로고
    • A 260-kDa filamin/ABP-related protein in chicken gizzard smooth muscle cells is a new component of the dense plaques and dense bodies of smooth muscle
    • Tachikawa, M., Nakagawa, H., Terasaki, A.G., Mori, H., and Ohashi, K. 1997. A 260-kDa filamin/ABP-related protein in chicken gizzard smooth muscle cells is a new component of the dense plaques and dense bodies of smooth muscle. J. Biochem. (Tokyo), 122: 314-321.
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 314-321
    • Tachikawa, M.1    Nakagawa, H.2    Terasaki, A.G.3    Mori, H.4    Ohashi, K.5
  • 138
    • 0035321725 scopus 로고    scopus 로고
    • Smooth muscle excitation-contraction coupling: A role for caveolae and caveolins?
    • Taggart, M.J. 2001. Smooth muscle excitation-contraction coupling: a role for caveolae and caveolins? News Physiol. Sci. 16: 61-65.
    • (2001) News Physiol. Sci. , vol.16 , pp. 61-65
    • Taggart, M.J.1
  • 139
    • 0034631516 scopus 로고    scopus 로고
    • Inhibition of PKCalpha and RhoA translocation in differentiated smooth muscle by a caveolin scaffolding domain peptide
    • Taggart, M.J., Leavis, P., Feron, O., and Morgan, K.G. 2000. Inhibition of PKCalpha and RhoA translocation in differentiated smooth muscle by a caveolin scaffolding domain peptide. Exp. Cell Res. 258: 72-81.
    • (2000) Exp. Cell Res. , vol.258 , pp. 72-81
    • Taggart, M.J.1    Leavis, P.2    Feron, O.3    Morgan, K.G.4
  • 140
    • 10644285520 scopus 로고    scopus 로고
    • The small GTPase Cdc42 regulates actin polymerization and tension development during contractile stimulation of smooth muscle
    • Tang, D.D., and Gunst, S.J. 2004. The small GTPase Cdc42 regulates actin polymerization and tension development during contractile stimulation of smooth muscle. J. Biol. Chem. 279: 51722-51728.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51722-51728
    • Tang, D.D.1    Gunst, S.J.2
  • 141
    • 0344896781 scopus 로고    scopus 로고
    • Expression of non-phosphorylatable paxillin mutants in canine tracheal smooth muscle inhibits tension development
    • Tang, D.D., Turner, C.E., and Gunst, S.J. 2003. Expression of non-phosphorylatable paxillin mutants in canine tracheal smooth muscle inhibits tension development. J. Physiol. 553: 21-35.
    • (2003) J. Physiol. , vol.553 , pp. 21-35
    • Tang, D.D.1    Turner, C.E.2    Gunst, S.J.3
  • 143
    • 0033945385 scopus 로고    scopus 로고
    • Differences in caveolae dynamics in vascular smooth muscle cells of different phenotypes
    • Thyberg, J. 2000. Differences in caveolae dynamics in vascular smooth muscle cells of different phenotypes. Lab. Invest. 80: 915-929.
    • (2000) Lab. Invest. , vol.80 , pp. 915-929
    • Thyberg, J.1
  • 144
    • 0030743282 scopus 로고    scopus 로고
    • Expression of caveolae on the surface of rat arterial smooth muscle cells is dependent on the phenotypic state of the cells
    • Thyberg, J., Roy, J., Tran, P.K., Blomgren, K., Dumitrescu, A., and Hedin, U. 1997a. Expression of caveolae on the surface of rat arterial smooth muscle cells is dependent on the phenotypic state of the cells. Lab. Invest. 77: 93-101.
    • (1997) Lab. Invest. , vol.77 , pp. 93-101
    • Thyberg, J.1    Roy, J.2    Tran, P.K.3    Blomgren, K.4    Dumitrescu, A.5    Hedin, U.6
  • 145
    • 0030977355 scopus 로고    scopus 로고
    • Phenotypic modulation of smooth muscle cells after arterial injury is associated with changes in the distribution of laminin and fibronectin
    • Thyberg, J., Blomgren, K., Roy, J., Tran, P.K., and Hedin, U. 1997b. Phenotypic modulation of smooth muscle cells after arterial injury is associated with changes in the distribution of laminin and fibronectin. J. Histochem. Cytochem. 45: 837-846.
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 837-846
    • Thyberg, J.1    Blomgren, K.2    Roy, J.3    Tran, P.K.4    Hedin, U.5
  • 146
    • 0031807422 scopus 로고    scopus 로고
    • Carbachol-induced actin reorganization involves gi activation of rho in human airway smooth muscle cells
    • Togashi, H., Emala, C.W., Hall, I.P., and Hirshman, C.A. 1998. Carbachol-induced actin reorganization involves gi activation of rho in human airway smooth muscle cells. Am. J. Physiol. 274: L803-L809.
    • (1998) Am. J. Physiol. , vol.274
    • Togashi, H.1    Emala, C.W.2    Hall, I.P.3    Hirshman, C.A.4
  • 148
    • 0035930570 scopus 로고    scopus 로고
    • Cholesterol depletion inhibits epidermal growth factor receptor transactivation by angiotensin II in vascular smooth muscle cells: Role of cholesterol-rich microdomains and focal adhesions in angiotensin II signaling
    • Ushio-Fukai, M., Hilenski, L., Santanam, N., Becker, P.L., Ma, Y., Griendling, K.K., and Alexander, R.W. 2001. Cholesterol depletion inhibits epidermal growth factor receptor transactivation by angiotensin II in vascular smooth muscle cells: role of cholesterol-rich microdomains and focal adhesions in angiotensin II signaling. J. Biol. Chem. 276: 48269-48275.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48269-48275
    • Ushio-Fukai, M.1    Hilenski, L.2    Santanam, N.3    Becker, P.L.4    Ma, Y.5    Griendling, K.K.6    Alexander, R.W.7
  • 150
    • 0036085102 scopus 로고    scopus 로고
    • Changes in force-velocity properties of trachealis due to oscillatory strains
    • Wang, L., Pare, P.D., and Seow, C.Y. 2002. Changes in force-velocity properties of trachealis due to oscillatory strains. J. Appl. Physiol. 92: 1865-1872.
    • (2002) J. Appl. Physiol. , vol.92 , pp. 1865-1872
    • Wang, L.1    Pare, P.D.2    Seow, C.Y.3
  • 152
    • 0036588248 scopus 로고    scopus 로고
    • Mechanical function of intermediate filaments in arteries of different size examined using desmin deficient mice
    • Wede, O.K., Lofgren, M., Li, Z., Paulin, D., and Arner, A. 2002. Mechanical function of intermediate filaments in arteries of different size examined using desmin deficient mice. J. Physiol. 540: 941-949.
    • (2002) J. Physiol. , vol.540 , pp. 941-949
    • Wede, O.K.1    Lofgren, M.2    Li, Z.3    Paulin, D.4    Arner, A.5
  • 153
    • 0041559837 scopus 로고    scopus 로고
    • Sarcoglycans in vascular smooth and striated muscle
    • Wheeler, M.T., and McNally, E.M. 2003. Sarcoglycans in vascular smooth and striated muscle. Trends Cardiovasc. Med. 13: 238-243.
    • (2003) Trends Cardiovasc. Med. , vol.13 , pp. 238-243
    • Wheeler, M.T.1    McNally, E.M.2
  • 154
    • 0036714792 scopus 로고    scopus 로고
    • Zeta-sarcoglycan, a novel component of the sarcoglycan complex, is reduced in muscular dystrophy
    • Wheeler, M.T., Zarnegar, S., and McNally, E.M. 2002. Zeta-sarcoglycan, a novel component of the sarcoglycan complex, is reduced in muscular dystrophy. Hum. Mol. Genet. 11: 2147-2154.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2147-2154
    • Wheeler, M.T.1    Zarnegar, S.2    McNally, E.M.3
  • 155
    • 0033594082 scopus 로고    scopus 로고
    • Extensive but coordinated reorganization of the membrane skeleton in myofibers of dystrophic (mdx) mice
    • Williams, M.W., and Bloch, R.J. 1999. Extensive but coordinated reorganization of the membrane skeleton in myofibers of dystrophic (mdx) mice. J. Cell. Biol. 144: 1259-1270.
    • (1999) J. Cell. Biol. , vol.144 , pp. 1259-1270
    • Williams, M.W.1    Bloch, R.J.2
  • 156
    • 0027358735 scopus 로고
    • Mechanical strain induces growth of vascular smooth muscle cells via autocrine action of PDGF
    • Wilson, E., Mai, Q., Sudhir, K., Weiss, R.H., and Ives, H.E. 1993. Mechanical strain induces growth of vascular smooth muscle cells via autocrine action of PDGF. J. Cell. Biol. 123: 741-747.
    • (1993) J. Cell. Biol. , vol.123 , pp. 741-747
    • Wilson, E.1    Mai, Q.2    Sudhir, K.3    Weiss, R.H.4    Ives, H.E.5
  • 158
    • 0035018464 scopus 로고    scopus 로고
    • Characterization of stretch-activated cation current in coronary smooth muscle cells
    • Wu, X., and Davis, M.J. 2001. Characterization of stretch-activated cation current in coronary smooth muscle cells. Am. J. Physiol. Heart Circ. Physiol. 280: H1751-H1761.
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.280
    • Wu, X.1    Davis, M.J.2
  • 161
    • 17644379396 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by N-WASp is required for actin polymerization and contraction in smooth muscle
    • Zhang, W., Wu, Y., Du, L., Tang, D.D., and Gunst, S.J. 2004. Activation of the Arp2/3 complex by N-WASp is required for actin polymerization and contraction in smooth muscle. Am. J. Physiol. Cell Physiol. 288: C1145-C1160.
    • (2004) Am. J. Physiol. Cell Physiol. , vol.288
    • Zhang, W.1    Wu, Y.2    Du, L.3    Tang, D.D.4    Gunst, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.