메뉴 건너뛰기




Volumn 61, Issue 4, 1996, Pages 493-501

Domains of laminin

Author keywords

basement membrane; cell binding; epidermolysis bullosa; extracellular matrix; gene knock out; integrin; laminin; muscular dystrophy

Indexed keywords

LAMININ; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; SYNTHETIC PEPTIDE;

EID: 0029956106     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(19960616)61:4<493::AID-JCB2>3.0.CO;2-J     Document Type: Review
Times cited : (159)

References (51)
  • 2
    • 0027231255 scopus 로고
    • Ionic inter-actions in the coiled-coil domain of laminin determine the specificity of chain assembly
    • Beck K, Dixon TW, Engel J, Parry DAD (1993): Ionic inter-actions in the coiled-coil domain of laminin determine the specificity of chain assembly. J Mol Biol 231:311-323.
    • (1993) J Mol Biol , vol.231 , pp. 311-323
    • Beck, K.1    Dixon, T.W.2    Engel, J.3    Parry, D.A.D.4
  • 4
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeletal-extracellular matrix linkage
    • Campbell KP (1995): Three muscular dystrophies: Loss of cytoskeletal-extracellular matrix linkage. Cell 80:675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 5
    • 0028952738 scopus 로고
    • Mapping of network-forming, heparin-binding, and α1β1 integrin-recognition sites within the α-chain short arm of laminin-1
    • Colognato-Pyke H, O'Rear JJ, Yamada Y, Carbonetto S, Cheng Y-S, Yurchenco PD (1995): Mapping of network-forming, heparin-binding, and α1β1 integrin-recognition sites within the α-chain short arm of laminin-1. J Biol Chem 270:9398-9406.
    • (1995) J Biol Chem , vol.270 , pp. 9398-9406
    • Colognato-Pyke, H.1    O'Rear, J.J.2    Yamada, Y.3    Carbonetto, S.4    Cheng, Y.-S.5    Yurchenco, P.D.6
  • 6
    • 0025315789 scopus 로고
    • Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain
    • Deutzmann R, Aumailley M, Wiedemann H, Pysny W, Timpl R, Edgar D (1990): Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain. Eur J Biochem 191:513-522.
    • (1990) Eur J Biochem , vol.191 , pp. 513-522
    • Deutzmann, R.1    Aumailley, M.2    Wiedemann, H.3    Pysny, W.4    Timpl, R.5    Edgar, D.6
  • 7
    • 0024413453 scopus 로고
    • EGF-like domains in extracellular matrix proteins: Localized signals for growth and differentiation?
    • Engel J (1989): EGF-like domains in extracellular matrix proteins: Localized signals for growth and differentiation? FEBS Lett 251:1-7.
    • (1989) FEBS Lett , vol.251 , pp. 1-7
    • Engel, J.1
  • 8
    • 0026442649 scopus 로고
    • Laminins and other strange proteins
    • Engel J (1992): Laminins and other strange proteins. Biochemistry 31:10643-10651.
    • (1992) Biochemistry , vol.31 , pp. 10643-10651
    • Engel, J.1
  • 9
    • 0028088813 scopus 로고
    • Building synapses: Agrin and dystroglycan stick together
    • Fallon JR, Hall ZW (1994): Building synapses: Agrin and dystroglycan stick together. TINS 17:469-473.
    • (1994) TINS , vol.17 , pp. 469-473
    • Fallon, J.R.1    Hall, Z.W.2
  • 10
    • 0029143930 scopus 로고
    • Cloning and complete primary structure of the mouse laminin alpha 3 chain. Distinct expression pattern of the laminin alpha 3A and alpha 3B chain isoforms
    • Galliano MF, Aberdam D, Aguzzi A, Ortonne JP, Meneguzzi G (1995): Cloning and complete primary structure of the mouse laminin alpha 3 chain. Distinct expression pattern of the laminin alpha 3A and alpha 3B chain isoforms. J Biol Chem 270:21820-21826.
    • (1995) J Biol Chem , vol.270 , pp. 21820-21826
    • Galliano, M.F.1    Aberdam, D.2    Aguzzi, A.3    Ortonne, J.P.4    Meneguzzi, G.5
  • 11
    • 0028361337 scopus 로고
    • Integrin-mediated adhesion and signaling in tumorigenesis
    • Giancotti FG, Mainiero F (1994): Integrin-mediated adhesion and signaling in tumorigenesis. Biochim Biophys Acta 1198:47-64.
    • (1994) Biochim Biophys Acta , vol.1198 , pp. 47-64
    • Giancotti, F.G.1    Mainiero, F.2
  • 14
    • 0026779450 scopus 로고
    • Laminin chain assembly by triple and double stranded coiled-coil structures
    • Hunter I, Schulthess T, Engel J (1992): Laminin chain assembly by triple and double stranded coiled-coil structures. J Biol Chem 267:6006-6011.
    • (1992) J Biol Chem , vol.267 , pp. 6006-6011
    • Hunter, I.1    Schulthess, T.2    Engel, J.3
  • 15
    • 0024461745 scopus 로고
    • Protein oligormerization in the endoplasmic reticulum
    • Hurtley SM, Helenius A (1989): Protein oligormerization in the endoplasmic reticulum. Annu Rev Cell Biol 5:277-307.
    • (1989) Annu Rev Cell Biol , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 16
    • 0029008416 scopus 로고
    • Primary structure and expression of a novel human laminin α4 chain
    • Iivanainen A, Sainio K, Sariola H, Tryggvason K (1995): Primary structure and expression of a novel human laminin α4 chain. FEBS Lett 365:183-188.
    • (1995) FEBS Lett , vol.365 , pp. 183-188
    • Iivanainen, A.1    Sainio, K.2    Sariola, H.3    Tryggvason, K.4
  • 17
    • 0026481173 scopus 로고
    • UNC-6, a laminin-related protein, guides cell and pioneer axon migrations in C. elegans
    • Ishii N, Wadsworth WG, Stern BD, Culotti JG, Hedgecock EM (1992): UNC-6, a laminin-related protein, guides cell and pioneer axon migrations in C. elegans. Neuron 9:873-881.
    • (1992) Neuron , vol.9 , pp. 873-881
    • Ishii, N.1    Wadsworth, W.G.2    Stern, B.D.3    Culotti, J.G.4    Hedgecock, E.M.5
  • 18
    • 0026691698 scopus 로고
    • Sex hormone-binding globulin, androgen-binding protein, and vitamin K-dependent protein S are homologous to laminin A, merosin, and Drosophila crumbs protein
    • Joseph DR, Baker ME (1992). Sex hormone-binding globulin, androgen-binding protein, and vitamin K-dependent protein S are homologous to laminin A, merosin, and Drosophila crumbs protein. FASEB J 6:2477-2481.
    • (1992) FASEB J , vol.6 , pp. 2477-2481
    • Joseph, D.R.1    Baker, M.E.2
  • 19
    • 0028927770 scopus 로고
    • Characterization of laminin-binding integrins
    • Kramer RH (1994): Characterization of laminin-binding integrins. Meth Enzymol 245:129-146.
    • (1994) Meth Enzymol , vol.245 , pp. 129-146
    • Kramer, R.H.1
  • 20
    • 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
    • Leivo I, Engvall E (1988): 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 USA 85:1544-1548.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1544-1548
    • Leivo, I.1    Engvall, E.2
  • 21
  • 22
    • 0028919592 scopus 로고
    • Altered laminin 5 expression due to mutations in the gene encoding the β3 chain (LAMB3) in generalized atrophic benign epidermolysis bullosa
    • McGrath JA, Pulkkinen L, Christiano AM, Leigh IM, Eady RAJ, Uitto J (1995): Altered laminin 5 expression due to mutations in the gene encoding the β3 chain (LAMB3) in generalized atrophic benign epidermolysis bullosa. J Invest Dermatol 104:467-474.
    • (1995) J Invest Dermatol , vol.104 , pp. 467-474
    • McGrath, J.A.1    Pulkkinen, L.2    Christiano, A.M.3    Leigh, I.M.4    Eady, R.A.J.5    Uitto, J.6
  • 23
    • 0026093621 scopus 로고
    • Receptors for laminin on mammalian cells
    • Mecham RP (1991): Receptors for laminin on mammalian cells. FASEB J 5:2538-2546.
    • (1991) FASEB J , vol.5 , pp. 2538-2546
    • Mecham, R.P.1
  • 24
    • 0028802948 scopus 로고
    • Laminin receptors: Achieving specificity through cooperation
    • Mercurio AM (1995): Laminin receptors: Achieving specificity through cooperation. Trends Cell Biol 5:419-423.
    • (1995) Trends Cell Biol , vol.5 , pp. 419-423
    • Mercurio, A.M.1
  • 25
    • 0028860732 scopus 로고
    • Molecular cloning of a novel laminin chain, alpha 5, and widespread expression in adult mouse tissues
    • Miner JH, Lewis RM, Sanes JR (1995): Molecular cloning of a novel laminin chain, alpha 5, and widespread expression in adult mouse tissues. J Biol Chem 270:28523-28526.
    • (1995) J Biol Chem , vol.270 , pp. 28523-28526
    • Miner, J.H.1    Lewis, R.M.2    Sanes, J.R.3
  • 26
    • 0028908326 scopus 로고
    • Aberrant differentiation of neuromuscular junctions in mice lacking S-laminin/laminin β2
    • Noakes PG, Gautam M, Mudd J, Sanes JR, Merlie JP (1995): Aberrant differentiation of neuromuscular junctions in mice lacking S-laminin/laminin β2. Nature 374: 258-262.
    • (1995) Nature , vol.374 , pp. 258-262
    • Noakes, P.G.1    Gautam, M.2    Mudd, J.3    Sanes, J.R.4    Merlie, J.P.5
  • 27
    • 0027942507 scopus 로고
    • Assembly of synthetic laminin peptides into a triple-stranded coiled-coil structure
    • Nomizu M, Otaka A, Utani A, Roller PP, Yamada Y (1994): Assembly of synthetic laminin peptides into a triple-stranded coiled-coil structure. J Biol Chem 269:30386-30392.
    • (1994) J Biol Chem , vol.269 , pp. 30386-30392
    • Nomizu, M.1    Otaka, A.2    Utani, A.3    Roller, P.P.4    Yamada, Y.5
  • 28
    • 0026317977 scopus 로고
    • The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor and the neural cell adhesion molecule
    • Noonan DD, Fulle A, Valente P, Cai S, Horigan E, Sasaki M, Yamada Y, Hassell JR (1991): The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor and the neural cell adhesion molecule. J Biol Chem 266:22939-22947.
    • (1991) J Biol Chem , vol.266 , pp. 22939-22947
    • Noonan, D.D.1    Fulle, A.2    Valente, P.3    Cai, S.4    Horigan, E.5    Sasaki, M.6    Yamada, Y.7    Hassell, J.R.8
  • 29
    • 0027227388 scopus 로고
    • Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement membrane ligands
    • Pan T-C, Kluge M, Zhang R-Z, Mayer U, Timpl R, Chu M-L (1993): Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement membrane ligands. Eur J Biochem 215:733-740.
    • (1993) Eur J Biochem , vol.215 , pp. 733-740
    • Pan, T.-C.1    Kluge, M.2    Zhang, R.-Z.3    Mayer, U.4    Timpl, R.5    Chu, M.-L.6
  • 30
    • 0026584948 scopus 로고
    • A family of laminin-related proteins controlling ectodermal differentiation in Drosophila
    • Patthy L (1992): A family of laminin-related proteins controlling ectodermal differentiation in Drosophila. FEBS Lett 298:182-184.
    • (1992) FEBS Lett , vol.298 , pp. 182-184
    • Patthy, L.1
  • 32
    • 0028920977 scopus 로고
    • A motorneuron-selective stop signal in the synaptic protein S-laminin
    • Porter BE, Weis J, Sanes JR (1995): A motorneuron-selective stop signal in the synaptic protein S-laminin. Neuron 14:1-20.
    • (1995) Neuron , vol.14 , pp. 1-20
    • Porter, B.E.1    Weis, J.2    Sanes, J.R.3
  • 33
    • 0028180092 scopus 로고
    • Mutations in the γ2 chain gene (LAMC2) of kalinin/laminin 5 in the junctional forms of epidermolysis bullosa
    • Pulkkinen L, Christiano AM, Airenne T, Haakana H, Tryggvason K, Uitto J (1994): Mutations in the γ2 chain gene (LAMC2) of kalinin/laminin 5 in the junctional forms of epidermolysis bullosa. Nature Genetics 6:293-298.
    • (1994) Nature Genetics , vol.6 , pp. 293-298
    • Pulkkinen, L.1    Christiano, A.M.2    Airenne, T.3    Haakana, H.4    Tryggvason, K.5    Uitto, J.6
  • 36
    • 0028138219 scopus 로고
    • The netrins define a family of axon outgrowth-promoting proteins homologous to C. elegans UNC-6
    • Serafini T, Kennedy TE, Galko MJ, Mirzayan C, Jessell TM, Lavigne MT (1994): The netrins define a family of axon outgrowth-promoting proteins homologous to C. elegans UNC-6. Cell 78:409-424.
    • (1994) Cell , vol.78 , pp. 409-424
    • Serafini, T.1    Kennedy, T.E.2    Galko, M.J.3    Mirzayan, C.4    Jessell, T.M.5    Lavigne, M.T.6
  • 37
    • 0028318185 scopus 로고
    • Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain to dy locus
    • Sunada Y, Barzler SM, Kozak CA, Yamada Y, Campbell KP (1994): Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain to dy locus. J Biol Chem 269:13729-13782.
    • (1994) J Biol Chem , vol.269 , pp. 13729-13782
    • Sunada, Y.1    Barzler, S.M.2    Kozak, C.A.3    Yamada, Y.4    Campbell, K.P.5
  • 38
    • 0027520442 scopus 로고
    • Cell and heparin binding in the distal long arm of laminin: Identification of active and cryptic sites with recombinant and hybrid glycoprotein
    • Sung U, O'Rear JJ, Yurchenco PD (1993): Cell and heparin binding in the distal long arm of laminin: Identification of active and cryptic sites with recombinant and hybrid glycoprotein. J Cell Biol 123:1255-1268.
    • (1993) J Cell Biol , vol.123 , pp. 1255-1268
    • Sung, U.1    O'Rear, J.J.2    Yurchenco, P.D.3
  • 39
    • 0024558106 scopus 로고
    • Structure and biological activity of basement membrane proteins
    • Timpl R (1989): Structure and biological activity of basement membrane proteins. Eur J Biochem 180:487-502.
    • (1989) Eur J Biochem , vol.180 , pp. 487-502
    • Timpl, R.1
  • 42
    • 0026769035 scopus 로고
    • Neurexins: Synaptic cell surface protein related to the α-latrotoxin receptor and laminin
    • Ushkaryov YA, Petrenko AG, Geppert M, Sudhof TC (1992): Neurexins: Synaptic cell surface protein related to the α-latrotoxin receptor and laminin. Science 257:50-56.
    • (1992) Science , vol.257 , pp. 50-56
    • Ushkaryov, Y.A.1    Petrenko, A.G.2    Geppert, M.3    Sudhof, T.C.4
  • 43
    • 0028364085 scopus 로고
    • Laminin chain assembly. Specific sequences at the C terminus of the long arm are required for the formation of specific double- and triple-stranded coiled-coil structures
    • Utani A, Nomizu M, Timpl R, Roller PP, Yamada Y (1994): Laminin chain assembly. Specific sequences at the C terminus of the long arm are required for the formation of specific double- and triple-stranded coiled-coil structures. J Biol Chem 269:19167-19175.
    • (1994) J Biol Chem , vol.269 , pp. 19167-19175
    • Utani, A.1    Nomizu, M.2    Timpl, R.3    Roller, P.P.4    Yamada, Y.5
  • 47
    • 0029396750 scopus 로고
    • Laminin β2 chain and adhalin deficiency in the skeletal muscle of Walker-Warburg syndrome (cerebro-ocular dysplasiamuscular dystrophy)
    • Wewer UM, Durkin ME, Zhang X, Laursen H, Nielsen NH, Towfighi J, Engvall E, and Albrechtsen R (1995): Laminin β2 chain and adhalin deficiency in the skeletal muscle of Walker-Warburg syndrome (cerebro-ocular dysplasiamuscular dystrophy). Neurology 45:2099-2101.
    • (1995) Neurology , vol.45 , pp. 2099-2101
    • Wewer, U.M.1    Durkin, M.E.2    Zhang, X.3    Laursen, H.4    Nielsen, N.H.5    Towfighi, J.6    Engvall, E.7    Albrechtsen, R.8
  • 48
    • 0028334735 scopus 로고
    • Lack of M-laminin and defective muscle basement membrane in the dystrophic dy/dy mouse
    • Xu H, Christmas P, Wu ZR, Wewer UM, Engvall E (1994a): Lack of M-laminin and defective muscle basement membrane in the dystrophic dy/dy mouse. Proc Natl Acad Sci USA 91:5572-5576.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5572-5576
    • Xu, H.1    Christmas, P.2    Wu, Z.R.3    Wewer, U.M.4    Engvall, E.5
  • 49
    • 0028135436 scopus 로고
    • Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama2) gene
    • Xu H, Wu X-R, Wewer UM, Engvall E (1994b): Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama2) gene. Nature Genetics 8:297-302.
    • (1994) Nature Genetics , vol.8 , pp. 297-302
    • Xu, H.1    Wu, X.-R.2    Wewer, U.M.3    Engvall, E.4
  • 50
    • 0026468460 scopus 로고
    • Functional domains of cell adhesion molecules
    • Yamada Y, Kleinman HK (1992): Functional domains of cell adhesion molecules. Curr Opin Cell Biol 4:819-823.
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 819-823
    • Yamada, Y.1    Kleinman, H.K.2
  • 51
    • 0027313437 scopus 로고
    • Self-assembly and calcium-binding sites in laminin. A three-arm interaction model
    • Yurchenco PD, Cheng YS (1993): Self-assembly and calcium-binding sites in laminin. A three-arm interaction model. J Biol Chem 268:17286-17299.
    • (1993) J Biol Chem , vol.268 , pp. 17286-17299
    • Yurchenco, P.D.1    Cheng, Y.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.