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Volumn 7, Issue 1, 2013, Pages 101-110

Laminin isoforms in endothelial and perivascular basement membranes

Author keywords

Basement membrane; Blood vessels; Endothelium; Laminin; Vascular smooth muscle

Indexed keywords

ALPHA DYSTROGLYCAN; BETA1 INTEGRIN; BETA3 INTEGRIN; LAMININ; LAMININ ALPHA2; LAMININ ALPHA4; LAMININ ALPHA5; LAMININ RECEPTOR; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 84872178048     PISSN: 19336918     EISSN: 19336926     Source Type: Journal    
DOI: 10.4161/cam.22680     Document Type: Review
Times cited : (193)

References (102)
  • 1
    • 25444463573 scopus 로고    scopus 로고
    • Endothelial/pericyte interactions
    • PMID:16166562
    • Armulik A, Abramsson A, Betsholtz C. Endothelial/pericyte interactions. Circ Res 2005; 97:512-23; PMID:16166562; http://dx.doi.org/10.1161/01.RES. 0000182903.16652.d7
    • (2005) Circ Res , vol.97 , pp. 512-523
    • Armulik, A.1    Abramsson, A.2    Betsholtz, C.3
  • 2
    • 0028967989 scopus 로고
    • Novel mouse endothelial cell surface marker is suppressed during differentiation of the blood brain barrier
    • PMID: 7626790
    • Hallmann R, Mayer DN, Berg EL, Broermann R, Butcher EC. Novel mouse endothelial cell surface marker is suppressed during differentiation of the blood brain barrier. Dev Dyn 1995; 202:325-32; PMID: 7626790; http://dx.doi.org/10.1002/aja.1002020402
    • (1995) Dev Dyn , vol.202 , pp. 325-332
    • Hallmann, R.1    Mayer, D.N.2    Berg, E.L.3    Broermann, R.4    Butcher, E.C.5
  • 3
    • 79961230399 scopus 로고    scopus 로고
    • Pericytes: Developmental, physiological, and pathological perspectives, problems, and promises
    • PMID:21839917
    • Armulik A, Genové G, Betsholtz C. Pericytes: developmental, physiological, and pathological perspectives, problems, and promises. Dev Cell 2011; 21: 193-215; PMID:21839917; http://dx.doi.org/10.1016/j.devcel.2011.07.001
    • (2011) Dev Cell , vol.21 , pp. 193-215
    • Armulik, A.1    Genové, G.2    Betsholtz, C.3
  • 4
    • 1842482987 scopus 로고    scopus 로고
    • Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development
    • PMID:14998921
    • Pöschl E, Schlötzer-Schrehardt U, Brachvogel B, Saito K, Ninomiya Y, Mayer U. Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development 2004; 131:1619-28; PMID:14998921; http://dx.doi.org/10.1242/dev. 01037
    • (2004) Development , vol.131 , pp. 1619-1628
    • Pöschl, E.1    Schlötzer-Schrehardt, U.2    Brachvogel, B.3    Saito, K.4    Ninomiya, Y.5    Mayer, U.6
  • 5
    • 42949086409 scopus 로고    scopus 로고
    • Laminins and their roles in mammals
    • PMID: 18219670
    • Miner JH. Laminins and their roles in mammals. Microsc Res Tech 2008; 71:349-56; PMID: 18219670; http://dx.doi.org/10.1002/jemt.20563
    • (2008) Microsc Res Tech , vol.71 , pp. 349-356
    • Miner, J.H.1
  • 6
    • 84872176052 scopus 로고
    • Basement membrane heparan sulphate proteoglycan binds to laminin by its heparan sulfate side chains and to nidogen by sites in the protein core
    • Battaglia C, Mayer U, Aumailley M, Timpl R. Basement membrane heparan sulphate proteoglycan binds to laminin by its heparan sulfate side chains and to nidogen by sites in the protein core. Biochem J 1992; 289:313-30.
    • (1992) Biochem J , vol.289 , pp. 313-330
    • Battaglia, C.1    Mayer, U.2    Aumailley, M.3    Timpl, R.4
  • 7
    • 0033082328 scopus 로고    scopus 로고
    • Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin
    • PMID:10092882
    • Hopf M, Göhring W, Kohfeldt E, Yamada Y, Timpl R. Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin. Eur J Biochem 1999; 259:917-25; PMID:10092882; http://dx.doi.org/10.1046/j.1432-1327.1999.00127.x
    • (1999) Eur J Biochem , vol.259 , pp. 917-925
    • Hopf, M.1    Göhring, W.2    Kohfeldt, E.3    Yamada, Y.4    Timpl, R.5
  • 8
    • 0026006388 scopus 로고
    • Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV
    • PMID:1717261
    • Fox JW, Mayer U, Nischt R, Aumailley M, Reinhardt D, Wiedemann H, et al. Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV. EMBO J 1991; 10:3137-46; PMID:1717261
    • (1991) EMBO J , vol.10 , pp. 3137-3146
    • Fox, J.W.1    Mayer, U.2    Nischt, R.3    Aumailley, M.4    Reinhardt, D.5    Wiedemann, H.6
  • 9
    • 0025950577 scopus 로고
    • Localization of a major nidogen-binding site to domain III of laminin B2 chain
    • PMID:1935973
    • Gerl M, Mann K, Aumailley M, Timpl R. Localization of a major nidogen-binding site to domain III of laminin B2 chain. Eur J Biochem 1991; 202:167-74; PMID:1935973; http://dx.doi.org/10.1111/j.1432-1033.1991.tb16358.x
    • (1991) Eur J Biochem , vol.202 , pp. 167-174
    • Gerl, M.1    Mann, K.2    Aumailley, M.3    Timpl, R.4
  • 10
    • 84861537861 scopus 로고    scopus 로고
    • The epidermal basement membrane is a composite of separate laminin- Or collagen IV-containing networks connected by aggregated perlecan, but not by nidogens
    • PMID:22493504
    • Behrens DT, Villone D, Koch M, Brunner G, Sorokin L, Robenek H, et al. The epidermal basement membrane is a composite of separate laminin- or collagen IV-containing networks connected by aggregated perlecan, but not by nidogens. J Biol Chem 2012; 287:18700-9; PMID:22493504; http://dx.doi.org/10.1074/jbc.M111. 336073
    • (2012) J Biol Chem , vol.287 , pp. 18700-18709
    • Behrens, D.T.1    Villone, D.2    Koch, M.3    Brunner, G.4    Sorokin, L.5    Robenek, H.6
  • 11
    • 0034676061 scopus 로고    scopus 로고
    • A novel member of the netrin family, beta-netrin, shares homology with the beta chain of laminin: Identification, expression, and functional characterization
    • PMID: 11038171
    • Koch M, Murrell JR, Hunter DD, Olson PF, Jin W, Keene DR, et al. A novel member of the netrin family, beta-netrin, shares homology with the beta chain of laminin: identification, expression, and functional characterization. J Cell Biol 2000; 151:221-34; PMID: 11038171; http://dx.doi.org/10.1083/jcb.151.2.221
    • (2000) J Cell Biol , vol.151 , pp. 221-234
    • Koch, M.1    Murrell, J.R.2    Hunter, D.D.3    Olson, P.F.4    Jin, W.5    Keene, D.R.6
  • 12
    • 0037686257 scopus 로고    scopus 로고
    • Fibulins: A versatile family of extracellular matrix proteins
    • PMID:12778127
    • Timpl R, Sasaki T, Kostka G, Chu ML. Fibulins: a versatile family of extracellular matrix proteins. Nat Rev Mol Cell Biol 2003; 4:479-89; PMID:12778127; http://dx.doi.org/10.1038/nrm1130
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 479-489
    • Timpl, R.1    Sasaki, T.2    Kostka, G.3    Chu, M.L.4
  • 13
    • 0033741904 scopus 로고    scopus 로고
    • SPARC, a matricellular protein: At the crossroads of cell-matrix
    • PMID:11102747
    • Brekken RA, Sage EH. SPARC, a matricellular protein: at the crossroads of cell-matrix. Matrix Biol 2000; 19:569-80; PMID:11102747; http://dx.doi.org/10. 1016/S0945-053X(00)00105-0
    • (2000) Matrix Biol , vol.19 , pp. 569-580
    • Brekken, R.A.1    Sage, E.H.2
  • 14
    • 0034283571 scopus 로고    scopus 로고
    • Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity
    • PMID: 10966814
    • Sasaki T, Larsson H, Tisi D, Claesson-Welsh L, Hohenester E, Timpl R. Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity. J Mol Biol 2000; 301:1179-90; PMID: 10966814; http://dx.doi.org/10.1006/jmbi.2000.3996
    • (2000) J Mol Biol , vol.301 , pp. 1179-1190
    • Sasaki, T.1    Larsson, H.2    Tisi, D.3    Claesson-Welsh, L.4    Hohenester, E.5    Timpl, R.6
  • 15
    • 42949124873 scopus 로고    scopus 로고
    • Mammalian collagen IV
    • PMID:18219669
    • Khoshnoodi J, Pedchenko V, Hudson BG. Mammalian collagen IV. Microsc Res Tech 2008; 71:357-70; PMID:18219669; http://dx.doi.org/10.1002/jemt.20564
    • (2008) Microsc Res Tech , vol.71 , pp. 357-370
    • Khoshnoodi, J.1    Pedchenko, V.2    Hudson, B.G.3
  • 16
    • 0028171098 scopus 로고
    • Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae: Sequence, distribution, association with laminins, and developmental switches
    • PMID:7962065
    • Miner JH, Sanes JR. Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae: sequence, distribution, association with laminins, and developmental switches. J Cell Biol 1994; 127:879-91; PMID:7962065; http://dx.doi.org/10.1083/jcb.127.3.879
    • (1994) J Cell Biol , vol.127 , pp. 879-891
    • Miner, J.H.1    Sanes, J.R.2
  • 17
    • 0027997184 scopus 로고
    • The laminins
    • PMID:7827749
    • Timpl R, Brown JC. The laminins. Matrix Biol 1994; 14:275-81; PMID:7827749; http://dx.doi.org/10.1016/0945-053X(94)90192-9
    • (1994) Matrix Biol , vol.14 , pp. 275-281
    • Timpl, R.1    Brown, J.C.2
  • 18
    • 21244438355 scopus 로고    scopus 로고
    • Expression and function of laminins in the embryonic and mature vasculature
    • PMID:15987800
    • Hallmann R, Horn N, Selg M, Wendler O, Pausch F, Sorokin LM. Expression and function of laminins in the embryonic and mature vasculature. Physiol Rev 2005; 85:979-1000; PMID:15987800; http://dx.doi.org/10.1152/physrev.00014.2004
    • (2005) Physiol Rev , vol.85 , pp. 979-1000
    • Hallmann, R.1    Horn, N.2    Selg, M.3    Wendler, O.4    Pausch, F.5    Sorokin, L.M.6
  • 19
    • 34447550067 scopus 로고    scopus 로고
    • Laminin isoforms in development and disease
    • Berl PMID:17426950
    • Schéele S, Nyström A, Durbeej M, Talts JF, Ekblom M, Ekblom P. Laminin isoforms in development and disease. J Mol Med (Berl) 2007; 85:825-36; PMID:17426950; http://dx.doi.org/10.1007/s00109-007-0182-5
    • (2007) J Mol Med , vol.85 , pp. 825-836
    • Schéele, S.1    Nyström, A.2    Durbeej, M.3    Talts, J.F.4    Ekblom, M.5    Ekblom, P.6
  • 20
    • 72449128021 scopus 로고    scopus 로고
    • Laminins
    • PMID:19693542
    • Durbeej M. Laminins. Cell Tissue Res 2010; 339:259-68; PMID:19693542; http://dx.doi.org/10.1007/s00441-009-0838-2
    • (2010) Cell Tissue Res , vol.339 , pp. 259-268
    • Durbeej, M.1
  • 22
    • 0030955536 scopus 로고    scopus 로고
    • Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of endothelium
    • PMID:9219532
    • Frieser M, Nöckel H, Pausch F, Röder C, Hahn A, Deutzmann R, et al. Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of endothelium. Eur J Biochem 1997; 246:727-35; PMID:9219532; http://dx.doi.org/10. 1111/j.1432-1033.1997.t01-1-00727.x
    • (1997) Eur J Biochem , vol.246 , pp. 727-735
    • Frieser, M.1    Nöckel, H.2    Pausch, F.3    Röder, C.4    Hahn, A.5    Deutzmann, R.6
  • 23
    • 0028048718 scopus 로고
    • Expression of novel 400-kDa laminin chains by mouse and bovine endothelial cells
    • PMID:8055931
    • Sorokin LM, Girg W, Göpfert T, Hallmann R, Deutzmann R. Expression of novel 400-kDa laminin chains by mouse and bovine endothelial cells. Eur J Biochem 1994; 223:603-10; PMID:8055931; http://dx.doi.org/10.1111/j.1432-1033. 1994.tb19031.x
    • (1994) Eur J Biochem , vol.223 , pp. 603-610
    • Sorokin, L.M.1    Girg, W.2    Göpfert, T.3    Hallmann, R.4    Deutzmann, R.5
  • 24
    • 0031572281 scopus 로고    scopus 로고
    • Developmental regulation of the laminin alpha5 chain suggests a role in epithelial and endothelial cell maturation
    • PMID:9299121
    • Sorokin LM, Pausch F, Frieser M, Kröger S, Ohage E, Deutzmann R. Developmental regulation of the laminin alpha5 chain suggests a role in epithelial and endothelial cell maturation. Dev Biol 1997; 189:285-300; PMID:9299121; http://dx.doi.org/10.1006/dbio.1997.8668
    • (1997) Dev Biol , vol.189 , pp. 285-300
    • Sorokin, L.M.1    Pausch, F.2    Frieser, M.3    Kröger, S.4    Ohage, E.5    Deutzmann, R.6
  • 26
    • 0025242395 scopus 로고
    • Regulation of differentiated properties and proliferation of arterial smooth muscle cells
    • PMID:2244864
    • Thyberg J, Hedin U, Sjölund M, Palmberg L, Bottger BA. Regulation of differentiated properties and proliferation of arterial smooth muscle cells. Arteriosclerosis 1990; 10:966-90; PMID:2244864; http://dx.doi.org/10.1161/01. ATV.10.6.966
    • (1990) Arteriosclerosis , vol.10 , pp. 966-990
    • Thyberg, J.1    Hedin, U.2    Sjölund, M.3    Palmberg, L.4    Bottger, B.A.5
  • 27
    • 0036194786 scopus 로고    scopus 로고
    • Vitronectin is up-regulated after vascular injury and vitronectin blockade prevents neointima formation
    • PMID:11922905
    • Dufourcq P, Couffinhal T, Alzieu P, Daret D, Moreau C, Duplàa C, et al. Vitronectin is up-regulated after vascular injury and vitronectin blockade prevents neointima formation. Cardiovasc Res 2002; 53:952-62; PMID:11922905; http://dx.doi.org/10.1016/S0008-6363(01)00547-8
    • (2002) Cardiovasc Res , vol.53 , pp. 952-962
    • Dufourcq, P.1    Couffinhal, T.2    Alzieu, P.3    Daret, D.4    Moreau, C.5    Duplàa, C.6
  • 28
    • 0025965905 scopus 로고
    • Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis
    • PMID:1703162
    • Weller A, Beck S, Ekblom P. Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis. J Cell Biol 1991; 112:355-62; PMID:1703162; http://dx.doi.org/10.1083/jcb.112.2.355
    • (1991) J Cell Biol , vol.112 , pp. 355-362
    • Weller, A.1    Beck, S.2    Ekblom, P.3
  • 29
    • 0024205512 scopus 로고
    • Tenascin during gut development: Appearance in the mesenchyme, shift in molecular forms, and dependence on epithelial-mesenchymal interactions
    • PMID:2461951
    • Aufderheide E, Ekblom P. Tenascin during gut development: appearance in the mesenchyme, shift in molecular forms, and dependence on epithelial- mesenchymal interactions. J Cell Biol 1988; 107:2341-9; PMID:2461951; http://dx.doi.org/10.1083/jcb.107.6.2341
    • (1988) J Cell Biol , vol.107 , pp. 2341-2349
    • Aufderheide, E.1    Ekblom, P.2
  • 30
    • 0031838213 scopus 로고    scopus 로고
    • Vitronectin expression and interaction with receptors in smooth muscle cells from human atheromatous plaque
    • PMID:9484980
    • Dufourcq P, Louis H, Moreau C, Daret D, Boisseau MR, Lamazière JMD, et al. Vitronectin expression and interaction with receptors in smooth muscle cells from human atheromatous plaque. Arterioscler Thromb Vasc Biol 1998; 18:168-76; PMID:9484980; http://dx.doi.org/10.1161/01.ATV.18.2.168
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 168-176
    • Dufourcq, P.1    Louis, H.2    Moreau, C.3    Daret, D.4    Boisseau, M.R.5    Lamazière, J.M.D.6
  • 31
    • 0028048718 scopus 로고
    • Expression of novel 400-kDa laminin chains by mouse and bovine endothelial cells
    • PMID:8055931
    • Sorokin L, Girg W, Göpfert T, Hallmann R, Deutzmann R. Expression of novel 400-kDa laminin chains by mouse and bovine endothelial cells. Eur J Biochem 1994; 223:603-10; PMID:8055931; http://dx.doi.org/10.1111/j.1432-1033. 1994.tb19031.x
    • (1994) Eur J Biochem , vol.223 , pp. 603-610
    • Sorokin, L.1    Girg, W.2    Göpfert, T.3    Hallmann, R.4    Deutzmann, R.5
  • 32
    • 0030667063 scopus 로고    scopus 로고
    • Differential expression of five laminin alpha (1-5) chains in developing and adult mouse kidney
    • PMID:9415429
    • Sorokin LM, Pausch F, Durbeej M, Ekblom P. Differential expression of five laminin alpha (1-5) chains in developing and adult mouse kidney. Dev Dyn 1997; 210:446-62; PMID:9415429; http://dx.doi.org/10.1002/(SICI)1097- 0177(199712)210:4〈446::AID-AJA8〉3.0.CO;2-G
    • (1997) Dev Dyn , vol.210 , pp. 446-462
    • Sorokin, L.M.1    Pausch, F.2    Durbeej, M.3    Ekblom, P.4
  • 33
    • 0029008416 scopus 로고
    • Primary structure and expression of a novel human laminin alpha 4 chain
    • PMID:7781776
    • Iivanainen A, Sainio K, Sariola H, Tryggvason K. Primary structure and expression of a novel human laminin alpha 4 chain. FEBS Lett 1995; 365:183-8; PMID:7781776; http://dx.doi.org/10.1016/0014-5793(95)00462-I
    • (1995) FEBS Lett , vol.365 , pp. 183-188
    • Iivanainen, A.1    Sainio, K.2    Sariola, H.3    Tryggvason, K.4
  • 34
    • 33745029732 scopus 로고    scopus 로고
    • Venular basement membranes contain specific matrix protein low expression regions that act as exit points for emigrating neutrophils
    • PMID: 16754715
    • Wang S, Voisin MB, Larbi KY, Dangerfield J, Scheiermann C, Tran M, et al. Venular basement membranes contain specific matrix protein low expression regions that act as exit points for emigrating neutrophils. J Exp Med 2006; 203:1519-32; PMID: 16754715; http://dx.doi.org/10.1084/jem.20051210
    • (2006) J Exp Med , vol.203 , pp. 1519-1532
    • Wang, S.1    Voisin, M.B.2    Larbi, K.Y.3    Dangerfield, J.4    Scheiermann, C.5    Tran, M.6
  • 35
    • 67349162632 scopus 로고    scopus 로고
    • Endothelial basement membrane laminin alpha5 selectively inhibits T lymphocyte extravasation into the brain
    • PMID:19396173
    • Wu C, Ivars F, Anderson P, Hallmann R, Vestweber D, Nilsson P, et al. Endothelial basement membrane laminin alpha5 selectively inhibits T lymphocyte extravasation into the brain. Nat Med 2009; 15:519-27; PMID:19396173; http://dx.doi.org/10.1038/nm.1957
    • (2009) Nat Med , vol.15 , pp. 519-527
    • Wu, C.1    Ivars, F.2    Anderson, P.3    Hallmann, R.4    Vestweber, D.5    Nilsson, P.6
  • 36
    • 0035947768 scopus 로고    scopus 로고
    • Endothelial cell laminin isoforms, laminins 8 and 10, play decisive roles in T cell recruitment across the blood-brain barrier in experimental autoimmune encephalomyelitis
    • PMID:11381080
    • Sixt M, Engelhardt B, Pausch F, Hallmann R, Wendler O, Sorokin LM. Endothelial cell laminin isoforms, laminins 8 and 10, play decisive roles in T cell recruitment across the blood-brain barrier in experimental autoimmune encephalomyelitis. J Cell Biol 2001; 153:933-46; PMID:11381080; http://dx.doi.org/10.1083/jcb.153.5.933
    • (2001) J Cell Biol , vol.153 , pp. 933-946
    • Sixt, M.1    Engelhardt, B.2    Pausch, F.3    Hallmann, R.4    Wendler, O.5    Sorokin, L.M.6
  • 37
    • 34250848283 scopus 로고    scopus 로고
    • Isolated Anxa5+/Sca-1+ perivascular cells from mouse meningeal vasculature retain their perivascular phenotype in vitro and in vivo
    • PMID:17543301
    • Brachvogel B, Pausch F, Farlie P, Gaipl U, Etich J, Zhou Z, et al. Isolated Anxa5+/Sca-1+ perivascular cells from mouse meningeal vasculature retain their perivascular phenotype in vitro and in vivo. Exp Cell Res 2007; 313:2730-43; PMID:17543301; http://dx.doi.org/10.1016/j.yexcr.2007.04.031
    • (2007) Exp Cell Res , vol.313 , pp. 2730-2743
    • Brachvogel, B.1    Pausch, F.2    Farlie, P.3    Gaipl, U.4    Etich, J.5    Zhou, Z.6
  • 38
    • 73949086144 scopus 로고    scopus 로고
    • Pericyte recruitment during vasculogenic tube assembly stimulates endothelial basement membrane matrix formation
    • PMID:19822899
    • Stratman AN, Malotte KM, Mahan RD, Davis MJ, Davis GE. Pericyte recruitment during vasculogenic tube assembly stimulates endothelial basement membrane matrix formation. Blood 2009; 114:5091-101; PMID:19822899; http://dx.doi.org/10.1182/blood-2009-05-222364
    • (2009) Blood , vol.114 , pp. 5091-5101
    • Stratman, A.N.1    Malotte, K.M.2    Mahan, R.D.3    Davis, M.J.4    Davis, G.E.5
  • 39
    • 78649467527 scopus 로고    scopus 로고
    • Pericytes regulate the blood-brain barrier
    • PMID: 20944627
    • Armulik A, Genové G, Mäe M, Nisancioglu MH, Wallgard E, Niaudet C, et al. Pericytes regulate the blood-brain barrier. Nature 2010; 468:557-61; PMID: 20944627; http://dx.doi.org/10.1038/nature09522
    • (2010) Nature , vol.468 , pp. 557-561
    • Armulik, A.1    Genové, G.2    Mäe, M.3    Nisancioglu, M.H.4    Wallgard, E.5    Niaudet, C.6
  • 41
    • 0036007196 scopus 로고    scopus 로고
    • Deletion of the laminin alpha4 chain leads to impaired microvessel maturation
    • PMID:11809810
    • Thyboll J, Kortesmaa J, Cao R, Soininen R, Wang L, Iivanainen A, et al. Deletion of the laminin alpha4 chain leads to impaired microvessel maturation. Mol Cell Biol 2002; 22:1194-202; PMID:11809810; http://dx.doi.org/10.1128/MCB. 22.4.1194-1202.2002
    • (2002) Mol Cell Biol , vol.22 , pp. 1194-1202
    • Thyboll, J.1    Kortesmaa, J.2    Cao, R.3    Soininen, R.4    Wang, L.5    Iivanainen, A.6
  • 42
    • 0030736717 scopus 로고    scopus 로고
    • Primary structure, developmental expression, and immunolocalization of the murine laminin alpha4 chain
    • PMID:9346933
    • Iivanainen A, Kortesmaa J, Sahlberg C, Morita T, Bergmann U, Thesleff I, et al. Primary structure, developmental expression, and immunolocalization of the murine laminin alpha4 chain. J Biol Chem 1997; 272:27862-8; PMID:9346933; http://dx.doi.org/10.1074/jbc.272.44.27862
    • (1997) J Biol Chem , vol.272 , pp. 27862-27868
    • Iivanainen, A.1    Kortesmaa, J.2    Sahlberg, C.3    Morita, T.4    Bergmann, U.5    Thesleff, I.6
  • 43
    • 0028860732 scopus 로고
    • Molecular cloning of a novel laminin chain, alpha 5, and widespread expression in adult mouse tissues
    • PMID:7499364
    • Miner JH, Lewis RM, Sanes JR. Molecular cloning of a novel laminin chain, alpha 5, and widespread expression in adult mouse tissues. J Biol Chem 1995; 270:28523-6; PMID:7499364; http://dx.doi.org/10.1074/jbc.270.48.28523
    • (1995) J Biol Chem , vol.270 , pp. 28523-28526
    • Miner, J.H.1    Lewis, R.M.2    Sanes, J.R.3
  • 44
    • 33750918517 scopus 로고    scopus 로고
    • Extracellular matrix gene expression in the developing mouse aorta
    • McLean SE, Mecham BH, Kelleher CM, Mariani TJ, Mecham RP. Extracellular matrix gene expression in the developing mouse aorta. Adv Dev Biol 2005; 15: 81-128; http://dx.doi.org/10.1016/S1574-3349(05)15003-0
    • (2005) Adv Dev Biol , vol.15 , pp. 81-128
    • McLean, S.E.1    Mecham, B.H.2    Kelleher, C.M.3    Mariani, T.J.4    Mecham, R.P.5
  • 45
    • 0023970247 scopus 로고
    • Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development
    • PMID:3278318
    • Leivo I, Engvall E. Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development. Proc Natl Acad Sci U S A 1988; 85:1544-8; PMID:3278318; http://dx.doi.org/10.1073/pnas.85.5.1544
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 1544-1548
    • Leivo, I.1    Engvall, E.2
  • 46
    • 0025373178 scopus 로고
    • Merosin, a tissue-specific basement membrane protein, is a laminin-like protein
    • PMID:2185464
    • Ehrig K, Leivo I, Argraves WS, Ruoslahti E, Engvall E. Merosin, a tissue-specific basement membrane protein, is a laminin-like protein. Proc Natl Acad Sci U S A 1990; 87:3264-8; PMID:2185464; http://dx.doi.org/10.1073/pnas.87. 9.3264
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 3264-3268
    • Ehrig, K.1    Leivo, I.2    Argraves, W.S.3    Ruoslahti, E.4    Engvall, E.5
  • 47
    • 0029582766 scopus 로고
    • Expression of laminin isoforms in mouse myogenic cells in vitro and in vivo
    • PMID:8719886
    • Schuler F, Sorokin LM. Expression of laminin isoforms in mouse myogenic cells in vitro and in vivo. J Cell Sci 1995; 108:3795-805; PMID:8719886
    • (1995) J Cell Sci , vol.108 , pp. 3795-3805
    • Schuler, F.1    Sorokin, L.M.2
  • 48
    • 0027197249 scopus 로고
    • Laminin variants and integrin laminin receptors in developing and adult human smooth muscle
    • PMID:8500653
    • Glukhova M, Koteliansky V, Fondacci C, Marotte F, Rappaport L. Laminin variants and integrin laminin receptors in developing and adult human smooth muscle. Dev Biol 1993; 157:437-47; PMID:8500653; http://dx.doi.org/10.1006/dbio. 1993.1147
    • (1993) Dev Biol , vol.157 , pp. 437-447
    • Glukhova, M.1    Koteliansky, V.2    Fondacci, C.3    Marotte, F.4    Rappaport, L.5
  • 49
    • 84155162670 scopus 로고    scopus 로고
    • The adventitia: A progenitor cell niche for the vessel wall
    • PMID:22005572
    • Majesky MW, Dong XR, Hoglund V, Daum G, Mahoney WM, Jr. The adventitia: a progenitor cell niche for the vessel wall. Cells Tissues Organs 2012; 195:73-81; PMID:22005572; http://dx.doi.org/10.1159/000331413
    • (2012) Cells Tissues Organs , vol.195 , pp. 73-81
    • Majesky, M.W.1    Dong, X.R.2    Hoglund, V.3    Daum, G.4    Mahoney Jr., W.M.5
  • 50
    • 79959763975 scopus 로고    scopus 로고
    • The adventitia: A dynamic interface containing resident progenitor cells
    • PMID: 21677296
    • Majesky MW, Dong XR, Hoglund V, Mahoney WM, Jr., Daum G. The adventitia: a dynamic interface containing resident progenitor cells. Arterioscler Thromb Vasc Biol 2011; 31:1530-9; PMID: 21677296; http://dx.doi.org/10.1161/ATVBAHA. 110.221549
    • (2011) Arterioscler Thromb Vasc Biol , vol.31 , pp. 1530-1539
    • Majesky, M.W.1    Dong, X.R.2    Hoglund, V.3    Mahoney Jr., W.M.4    Daum, G.5
  • 51
    • 0037155254 scopus 로고    scopus 로고
    • Alternative splice variants of alpha 7 beta 1 integrin selectively recognize different laminin isoforms
    • PMID:11744715
    • von der Mark H, Williams I, Wendler O, Sorokin L, von der Mark K, Pöschl E. Alternative splice variants of alpha 7 beta 1 integrin selectively recognize different laminin isoforms. J Biol Chem 2002; 277:6012-6; PMID:11744715; http://dx.doi.org/10.1074/jbc.M102188200
    • (2002) J Biol Chem , vol.277 , pp. 6012-6016
    • Von Der Mark, H.1    Williams, I.2    Wendler, O.3    Sorokin, L.4    Von Der Mark, K.5    Pöschl, E.6
  • 52
    • 0034025635 scopus 로고    scopus 로고
    • Integrin binding specificity of laminin-10/11: Laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins
    • PMID:10671376
    • Kikkawa Y, Sanzen N, Fujiwara H, Sonnenberg A, Sekiguchi K. Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins. J Cell Sci 2000; 113:869-76; PMID:10671376
    • (2000) J Cell Sci , vol.113 , pp. 869-876
    • Kikkawa, Y.1    Sanzen, N.2    Fujiwara, H.3    Sonnenberg, A.4    Sekiguchi, K.5
  • 53
    • 33645380797 scopus 로고    scopus 로고
    • Ligand-binding specificities of laminin-binding integrins: A comprehensive survey of laminin-integrin interactions using recombinant alpha3beta1, alpha6beta1, alpha7beta1 and alpha6-beta4 integrins
    • PMID: 16413178
    • Nishiuchi R, Takagi J, Hayashi M, Ido H, Yagi Y, Sanzen N, et al. Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant alpha3beta1, alpha6beta1, alpha7beta1 and alpha6-beta4 integrins. Matrix Biol 2006; 25:189-97; PMID: 16413178; http://dx.doi.org/10.1016/j.matbio.2005.12.001
    • (2006) Matrix Biol , vol.25 , pp. 189-197
    • Nishiuchi, R.1    Takagi, J.2    Hayashi, M.3    Ido, H.4    Yagi, Y.5    Sanzen, N.6
  • 54
    • 0035824835 scopus 로고    scopus 로고
    • Domain IVa of laminin alpha5 chain is cell-adhesive and binds beta1 and alphaVbeta3 integrins through Arg-Gly-Asp
    • PMID:11741585
    • Sasaki T, Timpl R. Domain IVa of laminin alpha5 chain is cell-adhesive and binds beta1 and alphaVbeta3 integrins through Arg-Gly-Asp. FEBS Lett 2001; 509: 181-5; PMID:11741585; http://dx.doi.org/10.1016/S0014-5793(01)03167-2
    • (2001) FEBS Lett , vol.509 , pp. 181-185
    • Sasaki, T.1    Timpl, R.2
  • 55
    • 0035161468 scopus 로고    scopus 로고
    • Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity
    • PMID: 11133776
    • Parsons SF, Lee G, Spring FA, Willig TN, Peters LL, Gimm JA, et al. Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. Blood 2001; 97:312-20; PMID: 11133776; http://dx.doi.org/10.1182/blood.V97.1.312
    • (2001) Blood , vol.97 , pp. 312-320
    • Parsons, S.F.1    Lee, G.2    Spring, F.A.3    Willig, T.N.4    Peters, L.L.5    Gimm, J.A.6
  • 57
    • 0033597343 scopus 로고    scopus 로고
    • Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan
    • PMID: 10207021
    • Shimizu H, Hosokawa H, Ninomiya H, Miner JH, Masaki T. Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan. J Biol Chem 1999; 274:11995-2000; PMID: 10207021; http://dx.doi.org/10.1074/jbc. 274.17.11995
    • (1999) J Biol Chem , vol.274 , pp. 11995-12000
    • Shimizu, H.1    Hosokawa, H.2    Ninomiya, H.3    Miner, J.H.4    Masaki, T.5
  • 58
    • 0036538408 scopus 로고    scopus 로고
    • Vascular endothelial cells that express dystroglycan are involved in angiogenesis
    • PMID:11896196
    • Hosokawa H, Ninomiya H, Kitamura Y, Fujiwara K, Masaki T. Vascular endothelial cells that express dystroglycan are involved in angiogenesis. J Cell Sci 2002; 115:1487-96; PMID:11896196
    • (2002) J Cell Sci , vol.115 , pp. 1487-1496
    • Hosokawa, H.1    Ninomiya, H.2    Kitamura, Y.3    Fujiwara, K.4    Masaki, T.5
  • 59
    • 0030942450 scopus 로고    scopus 로고
    • Dystroglycan and laminins: Glycoconjugates involved in branching epithelial morphogenesis
    • PMID: 9088921
    • Durbeej M, Ekblom P. Dystroglycan and laminins: glycoconjugates involved in branching epithelial morphogenesis. Exp Lung Res 1997; 23:109-18; PMID: 9088921; http://dx.doi.org/10.3109/01902149709074024
    • (1997) Exp Lung Res , vol.23 , pp. 109-118
    • Durbeej, M.1    Ekblom, P.2
  • 60
    • 0028205487 scopus 로고
    • Alpha 6 integrin distribution in human embryonic and adult tissues
    • PMID: 8026982
    • Terpe HJ, Stark H, Ruiz P, Imhof BA. Alpha 6 integrin distribution in human embryonic and adult tissues. Histochemistry 1994; 101:41-9; PMID: 8026982; http://dx.doi.org/10.1007/BF00315830
    • (1994) Histochemistry , vol.101 , pp. 41-49
    • Terpe, H.J.1    Stark, H.2    Ruiz, P.3    Imhof, B.A.4
  • 61
    • 0032514841 scopus 로고    scopus 로고
    • Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all α v integrins
    • PMID:9827803
    • Bader BL, Rayburn H, Crowley D, Hynes RO. Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all α v integrins. Cell 1998; 95:507-19; PMID:9827803; http://dx.doi.org/10.1016/S0092- 8674(00)81618-9
    • (1998) Cell , vol.95 , pp. 507-519
    • Bader, B.L.1    Rayburn, H.2    Crowley, D.3    Hynes, R.O.4
  • 62
    • 84860453903 scopus 로고    scopus 로고
    • Screening of integrin-binding peptides from the laminin α4 and α5 chain G domain peptide library
    • PMID:22391228
    • Katagiri F, Ishikawa M, Yamada Y, Hozumi K, Kikkawa Y, Nomizu M. Screening of integrin-binding peptides from the laminin α4 and α5 chain G domain peptide library. Arch Biochem Biophys 2012; 521:32-42; PMID:22391228; http://dx.doi.org/10.1016/j.abb.2012.02.017
    • (2012) Arch Biochem Biophys , vol.521 , pp. 32-42
    • Katagiri, F.1    Ishikawa, M.2    Yamada, Y.3    Hozumi, K.4    Kikkawa, Y.5    Nomizu, M.6
  • 63
    • 0035907327 scopus 로고    scopus 로고
    • Purification and characterization of human laminin-8. Laminin-8 stimulates cell adhesion and migration through alpha3beta1 and alpha6beta1 integrins
    • PMID:11278628
    • Fujiwara H, Kikkawa Y, Sanzen N, Sekiguchi K. Purification and characterization of human laminin-8. Laminin-8 stimulates cell adhesion and migration through alpha3beta1 and alpha6beta1 integrins. J Biol Chem 2001; 276:17550-8; PMID:11278628; http://dx.doi.org/10.1074/jbc.M010155200
    • (2001) J Biol Chem , vol.276 , pp. 17550-17558
    • Fujiwara, H.1    Kikkawa, Y.2    Sanzen, N.3    Sekiguchi, K.4
  • 64
    • 0034686077 scopus 로고    scopus 로고
    • Recombinant laminin-8 (alpha(4)beta(1)gamma(1)). Production, purification,and interactions with integrins
    • PMID: 10809728
    • Kortesmaa J, Yurchenco P, Tryggvason K. Recombinant laminin-8 (alpha(4)beta(1)gamma(1)). Production, purification,and interactions with integrins. J Biol Chem 2000; 275:14853-9; PMID: 10809728; http://dx.doi.org/10. 1074/jbc.275.20.14853
    • (2000) J Biol Chem , vol.275 , pp. 14853-14859
    • Kortesmaa, J.1    Yurchenco, P.2    Tryggvason, K.3
  • 65
    • 17144464384 scopus 로고    scopus 로고
    • Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells
    • PMID: 11821406
    • Doi M, Thyboll J, Kortesmaa J, Jansson K, Iivanainen A, Parvardeh M, et al. Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells. J Biol Chem 2002; 277:12741-8; PMID: 11821406; http://dx.doi.org/10.1074/jbc.M111228200
    • (2002) J Biol Chem , vol.277 , pp. 12741-12748
    • Doi, M.1    Thyboll, J.2    Kortesmaa, J.3    Jansson, K.4    Iivanainen, A.5    Parvardeh, M.6
  • 66
    • 77954634090 scopus 로고    scopus 로고
    • Endothelial alpha5 and alphav integrins cooperate in remodeling of the vasculature during development
    • PMID:20570943
    • van der Flier A, Badu-Nkansah K, Whittaker CA, Crowley D, Bronson RT, Lacy-Hulbert A, et al. Endothelial alpha5 and alphav integrins cooperate in remodeling of the vasculature during development. Development 2010; 137:2439-49; PMID:20570943; http://dx.doi.org/10.1242/dev.049551
    • (2010) Development , vol.137 , pp. 2439-2449
    • Van Der Flier, A.1    Badu-Nkansah, K.2    Whittaker, C.A.3    Crowley, D.4    Bronson, R.T.5    Lacy-Hulbert, A.6
  • 67
    • 0030613628 scopus 로고    scopus 로고
    • The laminin alpha2-chain short arm mediates cell adhesion through both the alpha1beta1 and alpha2-beta1 integrins
    • PMID:9361014
    • Colognato H, MacCarrick M, O'Rear JJ, Yurchenco PD. The laminin alpha2-chain short arm mediates cell adhesion through both the alpha1beta1 and alpha2-beta1 integrins. J Biol Chem 1997; 272:29330-6; PMID:9361014; http://dx.doi.org/10.1074/jbc.272.46.29330
    • (1997) J Biol Chem , vol.272 , pp. 29330-29336
    • Colognato, H.1    MacCarrick, M.2    O'Rear, J.J.3    Yurchenco, P.D.4
  • 68
    • 0028316670 scopus 로고
    • Distinct and overlapping ligand specificities of the alpha 3A beta 1 and alpha 6A beta 1 integrins: Recognition of laminin isoforms
    • PMID:8019006
    • Delwel GO, de Melker AA, Hogervorst F, Jaspars LH, Fles DL, Kuikman I, et al. Distinct and overlapping ligand specificities of the alpha 3A beta 1 and alpha 6A beta 1 integrins: recognition of laminin isoforms. Mol Biol Cell 1994; 5:203-15; PMID:8019006
    • (1994) Mol Biol Cell , vol.5 , pp. 203-215
    • Delwel, G.O.1    De Melker, A.A.2    Hogervorst, F.3    Jaspars, L.H.4    Fles, D.L.5    Kuikman, I.6
  • 69
    • 0026354979 scopus 로고
    • Skeletal myoblasts utilize a novel β 1-series integrin and not alpha 6 β 1 for binding to the E8 and T8 fragments of laminin
    • PMID:1748636
    • von der Mark H, Dürr J, Sonnenberg A, von der Mark K, Deutzmann R, Goodman SL. Skeletal myoblasts utilize a novel β 1-series integrin and not alpha 6 β 1 for binding to the E8 and T8 fragments of laminin. J Biol Chem 1991; 266:23593-601; PMID:1748636
    • (1991) J Biol Chem , vol.266 , pp. 23593-23601
    • Von Der Mark, H.1    Dürr, J.2    Sonnenberg, A.3    Von Der Mark, K.4    Deutzmann, R.5    Goodman, S.L.6
  • 70
    • 23944462348 scopus 로고    scopus 로고
    • Role for the alpha7beta1 integrin in vascular development and integrity
    • PMID: 16003770
    • Flintoff-Dye NL, Welser J, Rooney J, Scowen P, Tamowski S, Hatton W, et al. Role for the alpha7beta1 integrin in vascular development and integrity. Dev Dyn 2005; 234:11-21; PMID: 16003770; http://dx.doi.org/10.1002/dvdy.20462
    • (2005) Dev Dyn , vol.234 , pp. 11-21
    • Flintoff-Dye, N.L.1    Welser, J.2    Rooney, J.3    Scowen, P.4    Tamowski, S.5    Hatton, W.6
  • 71
    • 34648837952 scopus 로고    scopus 로고
    • Role of the extracellular matrix and its receptors in smooth muscle cell function: Implications in vascular development and disease
    • PMID: 17885425
    • Hultgårdh-Nilsson A, Durbeej M. Role of the extracellular matrix and its receptors in smooth muscle cell function: implications in vascular development and disease. Curr Opin Lipidol 2007; 18:540-5; PMID: 17885425; http://dx.doi.org/10.1097/MOL.0b013e3282ef77e9
    • (2007) Curr Opin Lipidol , vol.18 , pp. 540-545
    • Hultgårdh-Nilsson, A.1    Durbeej, M.2
  • 72
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins
    • PMID: 10022829
    • Talts JF, Andac Z, Göhring W, Brancaccio A, Timpl R. Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins. EMBO J 1999; 18:863-70; PMID: 10022829; http://dx.doi.org/10.1093/emboj/18.4.863
    • (1999) EMBO J , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Göhring, W.3    Brancaccio, A.4    Timpl, R.5
  • 73
    • 0038414615 scopus 로고    scopus 로고
    • Beta1 integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain
    • PMID:12519075
    • Yu H, Talts JF. Beta1 integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain. Biochem J 2003; 371:289-99; PMID:12519075; http://dx.doi.org/10.1042/BJ20021500
    • (2003) Biochem J , vol.371 , pp. 289-299
    • Yu, H.1    Talts, J.F.2
  • 74
    • 12144286984 scopus 로고    scopus 로고
    • Molecular dissection of the alpha-dystroglycan- And integrin-binding sites within the globular domain of human laminin-10
    • PMID:14701821
    • Ido H, Harada K, Futaki S, Hayashi Y, Nishiuchi R, Natsuka Y, et al. Molecular dissection of the alpha-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10. J Biol Chem 2004; 279:10946-54; PMID:14701821; http://dx.doi.org/10.1074/jbc.M313626200
    • (2004) J Biol Chem , vol.279 , pp. 10946-10954
    • Ido, H.1    Harada, K.2    Futaki, S.3    Hayashi, Y.4    Nishiuchi, R.5    Natsuka, Y.6
  • 75
    • 0037160080 scopus 로고    scopus 로고
    • Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo
    • PMID:12244066
    • Kikkawa Y, Moulson CL, Virtanen I, Miner JH. Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo. J Biol Chem 2002; 277:44864-9; PMID:12244066; http://dx.doi.org/10.1074/jbc.M208731200
    • (2002) J Biol Chem , vol.277 , pp. 44864-44869
    • Kikkawa, Y.1    Moulson, C.L.2    Virtanen, I.3    Miner, J.H.4
  • 76
    • 0034858369 scopus 로고    scopus 로고
    • Localization of Lutheran, a novel laminin receptor, in normal, knockout, and transgenic mice suggests an interaction with laminin alpha5 in vivo
    • PMID:11507772
    • Moulson CL, Li C, Miner JH. Localization of Lutheran, a novel laminin receptor, in normal, knockout, and transgenic mice suggests an interaction with laminin alpha5 in vivo. Dev Dyn 2001; 222:101-14; PMID:11507772; http://dx.doi.org/10.1002/dvdy.1169
    • (2001) Dev Dyn , vol.222 , pp. 101-114
    • Moulson, C.L.1    Li, C.2    Miner, J.H.3
  • 77
    • 38849198549 scopus 로고    scopus 로고
    • Genetic inactivation of the laminin alpha5 chain receptor Lu/BCAM leads to kidney and intestinal abnormalities in the mouse
    • PMID: 18032551
    • Rahuel C, Filipe A, Ritie L, El Nemer W, Patey-Mariaud N, Eladari D, et al. Genetic inactivation of the laminin alpha5 chain receptor Lu/BCAM leads to kidney and intestinal abnormalities in the mouse. Am J Physiol Renal Physiol 2008; 294:F393-406; PMID: 18032551; http://dx.doi.org/10.1152/ajprenal.00315. 2007
    • (2008) Am J Physiol Renal Physiol , vol.294
    • Rahuel, C.1    Filipe, A.2    Ritie, L.3    El Nemer, W.4    Patey-Mariaud, N.5    Eladari, D.6
  • 78
    • 0032517785 scopus 로고    scopus 로고
    • Roles for laminin in embryogenesis: Exencephaly, syndactyly, and placentopathy in mice lacking the laminin alpha5 chain
    • PMID:9852162
    • Miner JH, Cunningham J, Sanes JR. Roles for laminin in embryogenesis: exencephaly, syndactyly, and placentopathy in mice lacking the laminin alpha5 chain. J Cell Biol 1998; 143:1713-23; PMID:9852162; http://dx.doi.org/10.1083/ jcb.143.6.1713
    • (1998) J Cell Biol , vol.143 , pp. 1713-1723
    • Miner, J.H.1    Cunningham, J.2    Sanes, J.R.3
  • 79
    • 77956534675 scopus 로고    scopus 로고
    • Endothelial alpha3beta1-integrin represses pathological angiogenesis and sustains endothelial-VEGF
    • PMID:20639457
    • da Silva RG, Tavora B, Robinson SD, Reynolds LE, Szekeres C, Lamar J, et al. Endothelial alpha3beta1-integrin represses pathological angiogenesis and sustains endothelial-VEGF. Am J Pathol 2010; 177:1534-48; PMID:20639457; http://dx.doi.org/10.2353/ajpath.2010.100043
    • (2010) Am J Pathol , vol.177 , pp. 1534-1548
    • Da Silva, R.G.1    Tavora, B.2    Robinson, S.D.3    Reynolds, L.E.4    Szekeres, C.5    Lamar, J.6
  • 80
    • 80255135606 scopus 로고    scopus 로고
    • Endothelial basement membrane limits tip cell formation by inducing Dll4/Notch signalling in vivo
    • PMID:21979816
    • Stenzel D, Franco CA, Estrach S, Mettouchi A, Sauvaget D, Rosewell I, et al. Endothelial basement membrane limits tip cell formation by inducing Dll4/Notch signalling in vivo. EMBO Rep 2011; 12:1135-43; PMID:21979816; http://dx.doi.org/10.1038/embor.2011.194
    • (2011) EMBO Rep , vol.12 , pp. 1135-1143
    • Stenzel, D.1    Franco, C.A.2    Estrach, S.3    Mettouchi, A.4    Sauvaget, D.5    Rosewell, I.6
  • 81
    • 79960357259 scopus 로고    scopus 로고
    • Laminin-binding integrins induce Dll4 expression and Notch signaling in endothelial cells
    • PMID:21474814
    • Estrach S, Cailleteau L, Franco CA, Gerhardt H, Stefani C, Lemichez E, et al. Laminin-binding integrins induce Dll4 expression and Notch signaling in endothelial cells. Circ Res 2011; 109:172-82; PMID:21474814; http://dx.doi.org/10.1161/CIRCRESAHA.111.240622
    • (2011) Circ Res , vol.109 , pp. 172-182
    • Estrach, S.1    Cailleteau, L.2    Franco, C.A.3    Gerhardt, H.4    Stefani, C.5    Lemichez, E.6
  • 82
    • 77957148462 scopus 로고    scopus 로고
    • Immune cell recruitment to inflammatory loci is impaired in mice deficient in basement membrane protein laminin alpha4
    • PMID:20483922
    • Kenne E, Soehnlein O, Genové G, Rotzius P, Eriksson EE, Lindbom L. Immune cell recruitment to inflammatory loci is impaired in mice deficient in basement membrane protein laminin alpha4. J Leukoc Biol 2010; 88:523-8; PMID:20483922
    • (2010) J Leukoc Biol , vol.88 , pp. 523-528
    • Kenne, E.1    Soehnlein, O.2    Genové, G.3    Rotzius, P.4    Eriksson, E.E.5    Lindbom, L.6
  • 83
    • 84864306054 scopus 로고    scopus 로고
    • Pericytes support neutrophil subendothelial cell crawling and breaching of venular walls in vivo
    • PMID:22615129
    • Proebstl D, Voisin M-B, Woodfin A, Whiteford J, D'Acquisto F, Jones GE, et al. Pericytes support neutrophil subendothelial cell crawling and breaching of venular walls in vivo. J Exp Med 2012; 209:1219-34; PMID:22615129; http://dx.doi.org/10.1084/jem.20111622
    • (2012) J Exp Med , vol.209 , pp. 1219-1234
    • Proebstl, D.1    Voisin, M.-B.2    Woodfin, A.3    Whiteford, J.4    D'Acquisto, F.5    Jones, G.E.6
  • 84
    • 19044398689 scopus 로고    scopus 로고
    • Angiogenesis and pericytes in the initiation of ectopic calcification
    • PMID:15890980
    • Collett GDM, Canfield AE. Angiogenesis and pericytes in the initiation of ectopic calcification. Circ Res 2005; 96:930-8; PMID:15890980; http://dx.doi.org/10.1161/01.RES.0000163634.51301.0d
    • (2005) Circ Res , vol.96 , pp. 930-938
    • Collett, G.D.M.1    Canfield, A.E.2
  • 85
    • 0022590909 scopus 로고
    • Crucial role of endothelium in the vasodilator response to increased flow in vivo
    • PMID: 3080370
    • Pohl U, Holtz J, Busse R, Bassenge E. Crucial role of endothelium in the vasodilator response to increased flow in vivo. Hypertension 1986; 8:37-44; PMID: 3080370; http://dx.doi.org/10.1161/01.HYP.8.1.37
    • (1986) Hypertension , vol.8 , pp. 37-44
    • Pohl, U.1    Holtz, J.2    Busse, R.3    Bassenge, E.4
  • 86
    • 0037214449 scopus 로고    scopus 로고
    • Regulation of endothelium-derived vasoactive autacoid production by hemodynamic forces
    • PMID:12498727
    • Busse R, Fleming I. Regulation of endothelium-derived vasoactive autacoid production by hemodynamic forces. Trends Pharmacol Sci 2003; 24:24-9; PMID:12498727; http://dx.doi.org/10.1016/S0165-6147(02)00005-6
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 24-29
    • Busse, R.1    Fleming, I.2
  • 87
    • 58049213928 scopus 로고    scopus 로고
    • Mechanotransduction in vascular physiology and atherogenesis
    • PMID:19197332
    • Hahn C, Schwartz MA. Mechanotransduction in vascular physiology and atherogenesis. Nat Rev Mol Cell Biol 2009; 10:53-62; PMID:19197332; http://dx.doi.org/10.1038/nrm2596
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 53-62
    • Hahn, C.1    Schwartz, M.A.2
  • 88
    • 0029827580 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (ERK1/2) activation by shear stress and adhesion in endothelial cells. Essential role for a herbimycin-sensitive kinase
    • PMID:8958227
    • Takahashi M, Berk BC. Mitogen-activated protein kinase (ERK1/2) activation by shear stress and adhesion in endothelial cells. Essential role for a herbimycin-sensitive kinase. J Clin Invest 1996; 98: 2623-31; PMID:8958227; http://dx.doi.org/10.1172/JCI119083
    • (1996) J Clin Invest , vol.98 , pp. 2623-2631
    • Takahashi, M.1    Berk, B.C.2
  • 89
    • 0035970008 scopus 로고    scopus 로고
    • Integrin-mediated mechanotransduction requires its dynamic interaction with specific extracellular matrix (ECM) ligands
    • PMID:11158591
    • Jalali S, del Pozo MA, Chen K, Miao H, Li Y, Schwartz MA, et al. Integrin-mediated mechanotransduction requires its dynamic interaction with specific extracellular matrix (ECM) ligands. Proc Natl Acad Sci U S A 2001; 98:1042-6; PMID:11158591; http://dx.doi.org/10.1073/pnas.98.3.1042
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1042-1046
    • Jalali, S.1    Del Pozo, M.A.2    Chen, K.3    Miao, H.4    Li, Y.5    Schwartz, M.A.6
  • 90
    • 0036843301 scopus 로고    scopus 로고
    • Role of integrins in endothelial mechanosensing of shear stress
    • PMID:12411390
    • Shyy JY, Chien S. Role of integrins in endothelial mechanosensing of shear stress. Circ Res 2002; 91: 769-75; PMID:12411390; http://dx.doi.org/10. 1161/01.RES.0000038487.19924.18
    • (2002) Circ Res , vol.91 , pp. 769-775
    • Shyy, J.Y.1    Chien, S.2
  • 91
    • 0033523026 scopus 로고    scopus 로고
    • The 67-kDa laminin-binding protein is involved in shear stress-dependent endothelial nitric-oxide synthase expression
    • PMID:10347148
    • Gloe T, Riedmayr S, Sohn HY, Pohl U. The 67-kDa laminin-binding protein is involved in shear stress-dependent endothelial nitric-oxide synthase expression. J Biol Chem 1999; 274:15996-6002; PMID:10347148; http://dx.doi.org/10.1074/jbc.274.23.15996
    • (1999) J Biol Chem , vol.274 , pp. 15996-16002
    • Gloe, T.1    Riedmayr, S.2    Sohn, H.Y.3    Pohl, U.4
  • 92
    • 0035801529 scopus 로고    scopus 로고
    • Activation of integrins in endothelial cells by fluid shear stress mediates Rho-dependent cytoskeletal alignment
    • PMID:11532928
    • Tzima E, del Pozo MA, Shattil SJ, Chien S, Schwartz MA. Activation of integrins in endothelial cells by fluid shear stress mediates Rho-dependent cytoskeletal alignment. EMBO J 2001; 20:4639-47; PMID:11532928; http://dx.doi.org/10.1093/emboj/20.17.4639
    • (2001) EMBO J , vol.20 , pp. 4639-4647
    • Tzima, E.1    Del Pozo, M.A.2    Shattil, S.J.3    Chien, S.4    Schwartz, M.A.5
  • 93
    • 0031044132 scopus 로고    scopus 로고
    • Integrin signaling transduces shear stress- Dependent vasodilation of coronary arterioles
    • 9048651
    • Muller JM, Chilian WM, Davis MJ. Integrin signaling transduces shear stress- dependent vasodilation of coronary arterioles. Circ Res 1997; 80:320-6; PMID: 9048651; http://dx.doi.org/10.1161/01.RES.80.3.320
    • (1997) Circ Res , vol.80
    • Muller, J.M.1    Chilian, W.M.2    Davis, M.J.3
  • 94
    • 33746478732 scopus 로고    scopus 로고
    • Cadherin:catenin complex: A novel regulator of vascular smooth muscle cell behaviour
    • PMID: 16438974
    • George SJ, Beeching CA. Cadherin:catenin complex: a novel regulator of vascular smooth muscle cell behaviour. Atherosclerosis 2006; 188:1-11; PMID: 16438974; http://dx.doi.org/10.1016/j.atherosclerosis.2005.12.017
    • (2006) Atherosclerosis , vol.188 , pp. 1-11
    • George, S.J.1    Beeching, C.A.2
  • 95
    • 0029048550 scopus 로고
    • Regulation of differentiation of vascular smooth muscle cells
    • PMID:7624392
    • Owens GK. Regulation of differentiation of vascular smooth muscle cells. Physiol Rev 1995; 75:487-517; PMID:7624392
    • (1995) Physiol Rev , vol.75 , pp. 487-517
    • Owens, G.K.1
  • 96
    • 0031456015 scopus 로고    scopus 로고
    • Smooth muscle migration in atherosclerosis and restenosis
    • PMID:9413408
    • Schwartz SM. Smooth muscle migration in atherosclerosis and restenosis. J Clin Invest 1997; 100(Suppl):S87-9; PMID:9413408
    • (1997) J Clin Invest , vol.100 , Issue.SUPPL.
    • Schwartz, S.M.1
  • 97
    • 0023713505 scopus 로고
    • Diverse effects of fibronectin and laminin on phenotypic properties of cultured arterial smooth muscle cells
    • PMID: 2455726
    • Hedin U, Bottger BA, Forsberg E, Johansson S, Thyberg J. Diverse effects of fibronectin and laminin on phenotypic properties of cultured arterial smooth muscle cells. J Cell Biol 1988; 107:307-19; PMID: 2455726; http://dx.doi.org/10. 1083/jcb.107.1.307
    • (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
  • 98
    • 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
    • PMID:9199669
    • Thyberg J, Blomgren K, Roy J, Tran PK, Hedin U. Phenotypic modulation of smooth muscle cells after arterial injury is associated with changes in the distribution of laminin and fibronectin. J Histochem Cytochem 1997; 45:837-46; PMID:9199669; http://dx.doi.org/10.1177/002215549704500608
    • (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
  • 99
    • 0025082803 scopus 로고
    • Changes in expression and organization of smooth-muscle-specific alpha-actin during fibronectin-mediated modulation of arterial smooth muscle cell phenotype
    • PMID:1703095
    • Hedin U, Sjölund M, Hultgårdh-Nilsson A, Thyberg J. Changes in expression and organization of smooth-muscle-specific alpha-actin during fibronectin-mediated modulation of arterial smooth muscle cell phenotype. Differentiation 1990; 44:222-31; PMID:1703095; http://dx.doi.org/10.1111/j.1432- 0436.1990.tb00621.x
    • (1990) Differentiation , vol.44 , pp. 222-231
    • Hedin, U.1    Sjölund, M.2    Hultgårdh-Nilsson, A.3    Thyberg, J.4
  • 100
    • 34848919248 scopus 로고    scopus 로고
    • Loss of the alpha7 integrin promotes extracellular signal-regulated kinase activation and altered vascular remodeling
    • PMID:17704212
    • Welser JV, Lange N, Singer CA, Elorza M, Scowen P, Keef KD, et al. Loss of the alpha7 integrin promotes extracellular signal-regulated kinase activation and altered vascular remodeling. Circ Res 2007; 101:672-81; PMID:17704212; http://dx.doi.org/10.1161/CIRCRESAHA.107.151415
    • (2007) Circ Res , vol.101 , pp. 672-681
    • Welser, J.V.1    Lange, N.2    Singer, C.A.3    Elorza, M.4    Scowen, P.5    Keef, K.D.6
  • 101
    • 34848874230 scopus 로고    scopus 로고
    • Alpha 7 beta 1 integrin: Putting the brakes on smooth muscle cell proliferation
    • PMID:17901369
    • Wilson E. Alpha 7 beta 1 integrin: putting the brakes on smooth muscle cell proliferation. Circ Res 2007; 101:651-3; PMID:17901369; http://dx.doi.org/10.1161/CIRCRESAHA.107.161877
    • (2007) Circ Res , vol.101 , pp. 651-653
    • Wilson, E.1
  • 102
    • 21644457637 scopus 로고    scopus 로고
    • αvβ3- And α5β1-integrin blockade inhibits myogenic constriction of skeletal muscle resistance arterioles
    • Martinez-Lemus LA, Crow T, Davis MJ, Meininger GA. αvβ3- and α5β1-integrin blockade inhibits myogenic constriction of skeletal muscle resistance arterioles. Am J Physiol 2005; 289:H322-9.
    • (2005) Am J Physiol , vol.289
    • Martinez-Lemus, L.A.1    Crow, T.2    Davis, M.J.3    Meininger, G.A.4


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