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Volumn 32, Issue 19, 2011, Pages 4327-4335

Cell behavior on protein matrices containing laminin α1 peptide AG73

Author keywords

Collagen; ECM(extra cellular matrix); Fibroconectin; Integrin; Laminin; Peptide

Indexed keywords

BINDING PEPTIDE; BIOLOGICAL ACTIVITIES; CELL ATTACHMENTS; CELL BEHAVIORS; CELL SPREADING; CELLULAR FUNCTION; COLLAGEN MATRICES; EXTRACELLULAR MATRICES; EXTRACELLULAR MATRIX PROTEIN; FIBROCONECTIN; FOCAL ADHESION KINASE; IN-CELL; INTEGRINS; LAMININ; MIXED METHOD; NEURITE OUTGROWTH; STRESS FIBERS;

EID: 79955147262     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2011.02.052     Document Type: Article
Times cited : (11)

References (48)
  • 1
    • 78649737455 scopus 로고    scopus 로고
    • The extracellular matrix at a glance
    • Frantz C., Stewart K.M., Weaver V.M. The extracellular matrix at a glance. J Cell Sci 2010, 123(Pt 24):4195-4200.
    • (2010) J Cell Sci , vol.123 , Issue.PART 24 , pp. 4195-4200
    • Frantz, C.1    Stewart, K.M.2    Weaver, V.M.3
  • 2
    • 72449145261 scopus 로고    scopus 로고
    • Nanoscale engineering of biomimetic surfaces: cues from the extracellular matrix
    • von der Mark K., Park J., Bauer S., Schmuki P. Nanoscale engineering of biomimetic surfaces: cues from the extracellular matrix. Cell Tissue Res 2010, 339(1):131-153.
    • (2010) Cell Tissue Res , vol.339 , Issue.1 , pp. 131-153
    • von der Mark, K.1    Park, J.2    Bauer, S.3    Schmuki, P.4
  • 3
    • 47749121495 scopus 로고    scopus 로고
    • Collagen scaffolds for tissue engineering
    • Glowacki J., Mizuno S. Collagen scaffolds for tissue engineering. Biopolymers 2008, 89(5):338-344.
    • (2008) Biopolymers , vol.89 , Issue.5 , pp. 338-344
    • Glowacki, J.1    Mizuno, S.2
  • 4
    • 42449118993 scopus 로고    scopus 로고
    • Collagen tissue engineering: development of novel biomaterials and applications
    • Cen L., Liu W., Cui L., Zhang W., Cao Y. Collagen tissue engineering: development of novel biomaterials and applications. Pediatr Res 2008, 63(5):492-496.
    • (2008) Pediatr Res , vol.63 , Issue.5 , pp. 492-496
    • Cen, L.1    Liu, W.2    Cui, L.3    Zhang, W.4    Cao, Y.5
  • 5
    • 3843135199 scopus 로고    scopus 로고
    • Integrin-mediated cell adhesion to type I collagen fibrils
    • Jokinen J., Dadu E., Nykvist P., Kapyla J., White D.J., Ivaska J., et al. Integrin-mediated cell adhesion to type I collagen fibrils. J Biol Chem 2004, 279(30):31956-31963.
    • (2004) J Biol Chem , vol.279 , Issue.30 , pp. 31956-31963
    • Jokinen, J.1    Dadu, E.2    Nykvist, P.3    Kapyla, J.4    White, D.J.5    Ivaska, J.6
  • 6
    • 0037414766 scopus 로고    scopus 로고
    • Collagen I initiates endothelial cell morphogenesis by inducing actin polymerization through suppression of cyclic AMP and protein kinase A.
    • Whelan M.C., Senger D.R. Collagen I initiates endothelial cell morphogenesis by inducing actin polymerization through suppression of cyclic AMP and protein kinase A. J Biol Chem 2003, 278(1):327-334.
    • (2003) J Biol Chem , vol.278 , Issue.1 , pp. 327-334
    • Whelan, M.C.1    Senger, D.R.2
  • 7
    • 0027471434 scopus 로고
    • Expression of integrin alpha 1 beta 1 is regulated by nerve growth factor and dexamethasone in PC12 cells. Functional consequences for adhesion and neurite outgrowth
    • Zhang Z., Tarone G., Turner D.C. Expression of integrin alpha 1 beta 1 is regulated by nerve growth factor and dexamethasone in PC12 cells. Functional consequences for adhesion and neurite outgrowth. J Biol Chem 1993, 268(8):5557-5565.
    • (1993) J Biol Chem , vol.268 , Issue.8 , pp. 5557-5565
    • Zhang, Z.1    Tarone, G.2    Turner, D.C.3
  • 8
    • 0030087944 scopus 로고    scopus 로고
    • Supramolecular assembly of basement membranes
    • Timpl R., Brown J.C. Supramolecular assembly of basement membranes. Bioessays 1996, 18(2):123-132.
    • (1996) Bioessays , vol.18 , Issue.2 , pp. 123-132
    • Timpl, R.1    Brown, J.C.2
  • 9
    • 77956755675 scopus 로고    scopus 로고
    • Basement membrane components are key players in specialized extracellular matrices
    • Kruegel J., Miosge N. Basement membrane components are key players in specialized extracellular matrices. Cell Mol Life Sci 2010, 67(17):2879-2895.
    • (2010) Cell Mol Life Sci , vol.67 , Issue.17 , pp. 2879-2895
    • Kruegel, J.1    Miosge, N.2
  • 10
  • 11
    • 0029100640 scopus 로고
    • Identification of cell binding sites in the laminin alpha 1 chain carboxyl-terminal globular domain by systematic screening of synthetic peptides
    • Nomizu M., Kim W.H., Yamamura K., Utani A., Song S.Y., Otaka A., et al. Identification of cell binding sites in the laminin alpha 1 chain carboxyl-terminal globular domain by systematic screening of synthetic peptides. J Biol Chem 1995, 270(35):20583-20590.
    • (1995) J Biol Chem , vol.270 , Issue.35 , pp. 20583-20590
    • Nomizu, M.1    Kim, W.H.2    Yamamura, K.3    Utani, A.4    Song, S.Y.5    Otaka, A.6
  • 12
    • 14444275787 scopus 로고    scopus 로고
    • Identification of cell binding sequences in mouse laminin gamma1 chain by systematic peptide screening
    • Nomizu M., Kuratomi Y., Song S.Y., Ponce M.L., Hoffman M.P., Powell S.K., et al. Identification of cell binding sequences in mouse laminin gamma1 chain by systematic peptide screening. J Biol Chem 1997, 272(51):32198-32205.
    • (1997) J Biol Chem , vol.272 , Issue.51 , pp. 32198-32205
    • Nomizu, M.1    Kuratomi, Y.2    Song, S.Y.3    Ponce, M.L.4    Hoffman, M.P.5    Powell, S.K.6
  • 15
    • 0242318380 scopus 로고    scopus 로고
    • Syndecan binding sites in the laminin alpha1 chain G domain
    • Suzuki N., Ichikawa N., Kasai S., Yamada M., Nishi N., Morioka H., et al. Syndecan binding sites in the laminin alpha1 chain G domain. Biochemistry 2003, 42(43):12625-12633.
    • (2003) Biochemistry , vol.42 , Issue.43 , pp. 12625-12633
    • Suzuki, N.1    Ichikawa, N.2    Kasai, S.3    Yamada, M.4    Nishi, N.5    Morioka, H.6
  • 16
    • 24644486909 scopus 로고    scopus 로고
    • Functional sites in the laminin alpha chains
    • Suzuki N., Yokoyama F., Nomizu M. Functional sites in the laminin alpha chains. Connect Tissue Res 2005, 46(3):142-152.
    • (2005) Connect Tissue Res , vol.46 , Issue.3 , pp. 142-152
    • Suzuki, N.1    Yokoyama, F.2    Nomizu, M.3
  • 17
    • 0035933868 scopus 로고    scopus 로고
    • Cell type-specific differences in glycosaminoglycans modulate the biological activity of a heparin-binding peptide (RKRLQVQLSIRT) from the G domain of the laminin alpha1 chain
    • Hoffman M.P., Engbring J.A., Nielsen P.K., Vargas J., Steinberg Z., Karmand A.J., et al. Cell type-specific differences in glycosaminoglycans modulate the biological activity of a heparin-binding peptide (RKRLQVQLSIRT) from the G domain of the laminin alpha1 chain. J Biol Chem 2001, 276(25):22077-22085.
    • (2001) J Biol Chem , vol.276 , Issue.25 , pp. 22077-22085
    • Hoffman, M.P.1    Engbring, J.A.2    Nielsen, P.K.3    Vargas, J.4    Steinberg, Z.5    Karmand, A.J.6
  • 18
    • 0032531219 scopus 로고    scopus 로고
    • Laminin-1 and the RKRLQVQLSIRT laminin-1 alpha1 globular domain peptide stimulate matrix metalloproteinase secretion by PC12 cells
    • Weeks B.S., Nomizu M., Ramchandran R.S., Yamada Y., Kleinman H.K. Laminin-1 and the RKRLQVQLSIRT laminin-1 alpha1 globular domain peptide stimulate matrix metalloproteinase secretion by PC12 cells. Exp Cell Res 1998, 243(2):375-382.
    • (1998) Exp Cell Res , vol.243 , Issue.2 , pp. 375-382
    • Weeks, B.S.1    Nomizu, M.2    Ramchandran, R.S.3    Yamada, Y.4    Kleinman, H.K.5
  • 19
    • 0030579058 scopus 로고    scopus 로고
    • Identification of synthetic peptides derived from laminin alpha1 and alpha2 chains with cell type specificity for neurite outgrowth
    • Richard B.L., Nomizu M., Yamada Y., Kleinman H.K. Identification of synthetic peptides derived from laminin alpha1 and alpha2 chains with cell type specificity for neurite outgrowth. Exp Cell Res 1996, 228(1):98-105.
    • (1996) Exp Cell Res , vol.228 , Issue.1 , pp. 98-105
    • Richard, B.L.1    Nomizu, M.2    Yamada, Y.3    Kleinman, H.K.4
  • 20
    • 0032582650 scopus 로고    scopus 로고
    • Laminin-1 and laminin-2 G-domain synthetic peptides bind syndecan-1 and are involved in acinar formation of a human submandibular gland cell line
    • Hoffman M.P., Nomizu M., Roque E., Lee S., Jung D.W., Yamada Y., et al. Laminin-1 and laminin-2 G-domain synthetic peptides bind syndecan-1 and are involved in acinar formation of a human submandibular gland cell line. J Biol Chem 1998, 273(44):28633-28641.
    • (1998) J Biol Chem , vol.273 , Issue.44 , pp. 28633-28641
    • Hoffman, M.P.1    Nomizu, M.2    Roque, E.3    Lee, S.4    Jung, D.W.5    Yamada, Y.6
  • 21
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110(6):673-687.
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 22
    • 0035724579 scopus 로고    scopus 로고
    • Function and interactions of integrins
    • van der Flier A., Sonnenberg A. Function and interactions of integrins. Cell Tissue Res 2001, 305(3):285-298.
    • (2001) Cell Tissue Res , vol.305 , Issue.3 , pp. 285-298
    • van der Flier, A.1    Sonnenberg, A.2
  • 23
    • 0036745861 scopus 로고    scopus 로고
    • Integrins in development: moving on, responding to, and sticking to the extracellular matrix
    • Bokel C., Brown N.H. Integrins in development: moving on, responding to, and sticking to the extracellular matrix. Dev Cell 2002, 3(3):311-321.
    • (2002) Dev Cell , vol.3 , Issue.3 , pp. 311-321
    • Bokel, C.1    Brown, N.H.2
  • 24
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • Arnaout M.A., Goodman S.L., Xiong J.P. Structure and mechanics of integrin-based cell adhesion. Curr Opin Cell Biol 2007, 19(5):495-507.
    • (2007) Curr Opin Cell Biol , vol.19 , Issue.5 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.P.3
  • 25
    • 27344440003 scopus 로고    scopus 로고
    • Detection of integrins in human cataract lens epithelial cells and two mammalian lens epithelial cell lines
    • McLean S.M., Mathew M.R., Kelly J.B., Murray S.B., Bennett H.G., Webb L.A., et al. Detection of integrins in human cataract lens epithelial cells and two mammalian lens epithelial cell lines. Br J Ophthalmol 2005, 89(11):1506-1509.
    • (2005) Br J Ophthalmol , vol.89 , Issue.11 , pp. 1506-1509
    • McLean, S.M.1    Mathew, M.R.2    Kelly, J.B.3    Murray, S.B.4    Bennett, H.G.5    Webb, L.A.6
  • 26
    • 0041825303 scopus 로고    scopus 로고
    • Dimensions and dynamics in integrin function
    • Yamada K.M., Pankov R., Cukierman E. Dimensions and dynamics in integrin function. Braz J Med Biol Res 2003, 36(8):959-966.
    • (2003) Braz J Med Biol Res , vol.36 , Issue.8 , pp. 959-966
    • Yamada, K.M.1    Pankov, R.2    Cukierman, E.3
  • 28
    • 0034729437 scopus 로고    scopus 로고
    • Syndecan-regulated receptor signaling
    • Rapraeger A.C. Syndecan-regulated receptor signaling. J Cell Biol 2000, 149(5):995-998.
    • (2000) J Cell Biol , vol.149 , Issue.5 , pp. 995-998
    • Rapraeger, A.C.1
  • 29
    • 0035479818 scopus 로고    scopus 로고
    • Syndecan-4 and focal adhesion function
    • Woods A., Couchman J.R. Syndecan-4 and focal adhesion function. Curr Opin Cell Biol 2001, 13(5):578-583.
    • (2001) Curr Opin Cell Biol , vol.13 , Issue.5 , pp. 578-583
    • Woods, A.1    Couchman, J.R.2
  • 31
    • 62149091091 scopus 로고    scopus 로고
    • Signal co-operation between integrins and other receptor systems
    • Streuli C.H., Akhtar N. Signal co-operation between integrins and other receptor systems. Biochem J 2009, 418(3):491-506.
    • (2009) Biochem J , vol.418 , Issue.3 , pp. 491-506
    • Streuli, C.H.1    Akhtar, N.2
  • 33
    • 33646195306 scopus 로고    scopus 로고
    • Specific structural features of syndecans and heparan sulfate chains are needed for cell signaling
    • Lopes C.C., Dietrich C.P., Nader H.B. Specific structural features of syndecans and heparan sulfate chains are needed for cell signaling. Braz J Med Biol Res 2006, 39(2):157-167.
    • (2006) Braz J Med Biol Res , vol.39 , Issue.2 , pp. 157-167
    • Lopes, C.C.1    Dietrich, C.P.2    Nader, H.B.3
  • 34
    • 36448970493 scopus 로고    scopus 로고
    • Synergistic control of cell adhesion by integrins and syndecans
    • Morgan M.R., Humphries M.J., Bass M.D. Synergistic control of cell adhesion by integrins and syndecans. Nat Rev Mol Cell Biol 2007, 8(12):957-969.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.12 , pp. 957-969
    • Morgan, M.R.1    Humphries, M.J.2    Bass, M.D.3
  • 36
    • 0034193169 scopus 로고    scopus 로고
    • Participation of syndecan 2 in the induction of stress fiber formation in cooperation with integrin alpha5beta1: structural characteristics of heparan sulfate chains with avidity to COOH-terminal heparin-binding domain of fibronectin
    • Kusano Y., Oguri K., Nagayasu Y., Munesue S., Ishihara M., Saiki I., et al. Participation of syndecan 2 in the induction of stress fiber formation in cooperation with integrin alpha5beta1: structural characteristics of heparan sulfate chains with avidity to COOH-terminal heparin-binding domain of fibronectin. Exp Cell Res 2000, 256(2):434-444.
    • (2000) Exp Cell Res , vol.256 , Issue.2 , pp. 434-444
    • Kusano, Y.1    Oguri, K.2    Nagayasu, Y.3    Munesue, S.4    Ishihara, M.5    Saiki, I.6
  • 37
    • 0242413064 scopus 로고    scopus 로고
    • Biological activities of homologous loop regions in the laminin alpha chain G domains
    • Suzuki N., Nakatsuka H., Mochizuki M., Nishi N., Kadoya Y., Utani A., et al. Biological activities of homologous loop regions in the laminin alpha chain G domains. J Biol Chem 2003, 278(46):45697-45705.
    • (2003) J Biol Chem , vol.278 , Issue.46 , pp. 45697-45705
    • Suzuki, N.1    Nakatsuka, H.2    Mochizuki, M.3    Nishi, N.4    Kadoya, Y.5    Utani, A.6
  • 38
    • 0038322472 scopus 로고    scopus 로고
    • Laminin-1 peptide-conjugated chitosan membranes as a novel approach for cell engineering
    • Mochizuki M., Kadoya Y., Wakabayashi Y., Kato K., Okazaki I., Yamada M., et al. Laminin-1 peptide-conjugated chitosan membranes as a novel approach for cell engineering. FASEB J 2003, 17(8):875-877.
    • (2003) FASEB J , vol.17 , Issue.8 , pp. 875-877
    • Mochizuki, M.1    Kadoya, Y.2    Wakabayashi, Y.3    Kato, K.4    Okazaki, I.5    Yamada, M.6
  • 40
    • 77955280915 scopus 로고    scopus 로고
    • Syndecan- and integrin-binding peptides synergistically accelerate cell adhesion
    • Hozumi K., Kobayashi K., Katagiri F., Kikkawa Y., Kadoya Y., Nomizu M. Syndecan- and integrin-binding peptides synergistically accelerate cell adhesion. FEBS Lett 2010, 584(15):3381-3385.
    • (2010) FEBS Lett , vol.584 , Issue.15 , pp. 3381-3385
    • Hozumi, K.1    Kobayashi, K.2    Katagiri, F.3    Kikkawa, Y.4    Kadoya, Y.5    Nomizu, M.6
  • 41
    • 33845914882 scopus 로고    scopus 로고
    • Laminin alpha1 chain LG4 module promotes cell attachment through syndecans and cell spreading through integrin alpha2beta1
    • Hozumi K., Suzuki N., Nielsen P.K., Nomizu M., Yamada Y. Laminin alpha1 chain LG4 module promotes cell attachment through syndecans and cell spreading through integrin alpha2beta1. J Biol Chem 2006, 281(43):32929-32940.
    • (2006) J Biol Chem , vol.281 , Issue.43 , pp. 32929-32940
    • Hozumi, K.1    Suzuki, N.2    Nielsen, P.K.3    Nomizu, M.4    Yamada, Y.5
  • 42
    • 58249090749 scopus 로고    scopus 로고
    • Mixed peptide-chitosan membranes to mimic the biological activities of a multifunctional laminin alpha1 chain LG4 module
    • Hozumi K., Yamagata N., Otagiri D., Fujimori C., Kikkawa Y., Kadoya Y., et al. Mixed peptide-chitosan membranes to mimic the biological activities of a multifunctional laminin alpha1 chain LG4 module. Biomaterials 2009, 30(8):1596-1603.
    • (2009) Biomaterials , vol.30 , Issue.8 , pp. 1596-1603
    • Hozumi, K.1    Yamagata, N.2    Otagiri, D.3    Fujimori, C.4    Kikkawa, Y.5    Kadoya, Y.6
  • 43
    • 0025036846 scopus 로고
    • Binding of human syndecan to extracellular matrix proteins
    • Elenius K., Salmivirta M., Inki P., Mali M., Jalkanen M. Binding of human syndecan to extracellular matrix proteins. J Biol Chem 1990, 265(29):17837-17843.
    • (1990) J Biol Chem , vol.265 , Issue.29 , pp. 17837-17843
    • Elenius, K.1    Salmivirta, M.2    Inki, P.3    Mali, M.4    Jalkanen, M.5
  • 44
    • 18644373288 scopus 로고    scopus 로고
    • Ile-Lys-Val-Ala-Val (IKVAV)-containing laminin alpha1 chain peptides form amyloid-like fibrils
    • Yamada M., Kadoya Y., Kasai S., Kato K., Mochizuki M., Nishi N., et al. Ile-Lys-Val-Ala-Val (IKVAV)-containing laminin alpha1 chain peptides form amyloid-like fibrils. FEBS Lett 2002, 530(1-3):48-52.
    • (2002) FEBS Lett , vol.530 , Issue.1-3 , pp. 48-52
    • Yamada, M.1    Kadoya, Y.2    Kasai, S.3    Kato, K.4    Mochizuki, M.5    Nishi, N.6
  • 45
    • 33751566549 scopus 로고    scopus 로고
    • Laminin peptide-conjugated chitosan membrane: application for keratinocyte delivery in wounded skin
    • Ikemoto S., Mochizuki M., Yamada M., Takeda A., Uchinuma E., Yamashina S., et al. Laminin peptide-conjugated chitosan membrane: application for keratinocyte delivery in wounded skin. J Biomed Mater Res A 2006, 79(3):716-722.
    • (2006) J Biomed Mater Res A , vol.79 , Issue.3 , pp. 716-722
    • Ikemoto, S.1    Mochizuki, M.2    Yamada, M.3    Takeda, A.4    Uchinuma, E.5    Yamashina, S.6
  • 47
    • 0025250619 scopus 로고
    • A neuronal cell line (PC12) expresses two beta 1-class integrins-alpha 1 beta 1 and alpha 3 beta 1-that recognize different neurite outgrowth-promoting domains in laminin
    • Tomaselli K.J., Hall D.E., Flier L.A., Gehlsen K.R., Turner D.C., Carbonetto S., et al. A neuronal cell line (PC12) expresses two beta 1-class integrins-alpha 1 beta 1 and alpha 3 beta 1-that recognize different neurite outgrowth-promoting domains in laminin. Neuron 1990, 5(5):651-662.
    • (1990) Neuron , vol.5 , Issue.5 , pp. 651-662
    • Tomaselli, K.J.1    Hall, D.E.2    Flier, L.A.3    Gehlsen, K.R.4    Turner, D.C.5    Carbonetto, S.6


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