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Volumn 382, Issue 3, 2004, Pages 933-943

Mammalian and Drosophila cells adhere to the laminin α4 LG4 domain through syndecans, but not glypicans

Author keywords

Heparin; Laminin; RNA interference; Syndecans

Indexed keywords

BIOCHEMISTRY; BIODIVERSITY; CYTOLOGY; GROWTH KINETICS; PROTEINS;

EID: 4744337798     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040558     Document Type: Article
Times cited : (16)

References (47)
  • 1
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: The laminin family of heterotrimers
    • Colognato, H. and Yurchenco, P. D. (2000) Form and function: the laminin family of heterotrimers. Dev. Dyn. 218, 213-234
    • (2000) Dev. Dyn. , vol.218 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.D.2
  • 3
    • 0031661502 scopus 로고    scopus 로고
    • The role of laminins in basement membrane function
    • Aumailley, M. and Smyth, N. (1998) The role of laminins in basement membrane function. J. Anat. 193, 1-21
    • (1998) J. Anat. , vol.193 , pp. 1-21
    • Aumailley, M.1    Smyth, N.2
  • 6
    • 0034333005 scopus 로고    scopus 로고
    • Laminins of the neuromuscular system
    • Patton, B. L. (2000) Laminins of the neuromuscular system. Microsc. Res. Tech. 51, 247-261
    • (2000) Microsc. Res. Tech. , vol.51 , pp. 247-261
    • Patton, B.L.1
  • 10
    • 0023738917 scopus 로고
    • Enhanced synthesis and secretion of type IV collagen and entactin during adipose conversion of 3T3-L1 cells and production of unorthodox laminin complex
    • Aratani, Y. and Kitagawa, Y. (1988) Enhanced synthesis and secretion of type IV collagen and entactin during adipose conversion of 3T3-L1 cells and production of unorthodox laminin complex. J. Biol. Chem. 263, 16163-16169
    • (1988) J. Biol. Chem. , vol.263 , pp. 16163-16169
    • Aratani, Y.1    Kitagawa, Y.2
  • 11
    • 0025016115 scopus 로고
    • Production of two variant laminin forms by endothelial cells and shift of their relative levels by angiostatic steroids
    • Tokida, Y., Aratani, Y., Morita, A. and Kitagawa, Y. (1990) Production of two variant laminin forms by endothelial cells and shift of their relative levels by angiostatic steroids. J. Biol. Chem. 265, 18123-18129
    • (1990) J. Biol. Chem. , vol.265 , pp. 18123-18129
    • Tokida, Y.1    Aratani, Y.2    Morita, A.3    Kitagawa, Y.4
  • 12
    • 0031258668 scopus 로고    scopus 로고
    • Differentiation-dependent expression of laminin-8 (α4β1γ 1) mRNAs in mouse 3T3-L1 adipocytes
    • Niimi, T., Kumagai, C., Okano, M. and Kitagawa, Y. (1997) Differentiation-dependent expression of laminin-8 (α4β1γ1) mRNAs in mouse 3T3-L1 adipocytes. Matrix Biol. 16, 223-230
    • (1997) Matrix Biol. , vol.16 , pp. 223-230
    • Niimi, T.1    Kumagai, C.2    Okano, M.3    Kitagawa, Y.4
  • 13
    • 0030483413 scopus 로고    scopus 로고
    • The complete cDNA coding sequence and tissue-specific expression of the mouse laminin α4 chain
    • Liu, J. and Mayne, R. (1996) The complete cDNA coding sequence and tissue-specific expression of the mouse laminin α4 chain. Matrix Biol. 15, 433-437
    • (1996) Matrix Biol. , vol.15 , pp. 433-437
    • Liu, J.1    Mayne, R.2
  • 14
    • 0030018816 scopus 로고    scopus 로고
    • The structural organisation of LAMA4, the gene encoding laminin α4
    • Richards, A., Al-Imara, L. and Pope, F. M. (1996) The structural organisation of LAMA4, the gene encoding laminin α4. Eur. J. Biochem. 238, 813-821
    • (1996) Eur. J. Biochem. , vol.238 , pp. 813-821
    • Richards, A.1    Al-Imara, L.2    Pope, F.M.3
  • 15
    • 0030919488 scopus 로고    scopus 로고
    • The laminin α chains: Expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform
    • Miner, J. H., Patton, B. L., Lentz, S. I., Gilbert, D. J., Snider, W. D., Jenkins, N. A., Copeland, N. G. and Sanes, J. R. (1997) The laminin α chains: expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform. J. Cell Biol. 137, 685-701
    • (1997) J. Cell Biol. , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3    Gilbert, D.J.4    Snider, W.D.5    Jenkins, N.A.6    Copeland, N.G.7    Sanes, J.R.8
  • 18
    • 0034634679 scopus 로고    scopus 로고
    • Structural and functional analysis of the recombinant G domain of the laminin α4 chain and its proteolytic processing in tissues
    • Talts, J. F., Sasaki, T., Miosge, N., Gohring, W., Mann, K., Mayne, R. and Timpl, R. (2000) Structural and functional analysis of the recombinant G domain of the laminin α4 chain and its proteolytic processing in tissues. J. Biol. Chem. 275, 35192-35199
    • (2000) J. Biol. Chem. , vol.275 , pp. 35192-35199
    • Talts, J.F.1    Sasaki, T.2    Miosge, N.3    Gohring, W.4    Mann, K.5    Mayne, R.6    Timpl, R.7
  • 19
    • 0029008416 scopus 로고
    • Primary structure and expression of a novel human laminin α4 chain
    • Iivanainen, A., Sainio, H. and 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, H.2    Tryggvason, K.3
  • 20
    • 0030919488 scopus 로고    scopus 로고
    • The laminin α chains: Expression, developmental transitions, and chromosomal locations of α5, identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform
    • Miner, J. H., Patton, B. L., Lentz, S. I., Gilbert, D. J., Snider, W. D., Jenkins, N. A., Copeland, N. G. and Sanes, J. R. (1997) The laminin α chains: expression, developmental transitions, and chromosomal locations of α5, identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform. J. Cell Biol. 137, 685-701
    • (1997) J. Cell Biol. , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3    Gilbert, D.J.4    Snider, W.D.5    Jenkins, N.A.6    Copeland, N.G.7    Sanes, J.R.8
  • 21
    • 0035907327 scopus 로고    scopus 로고
    • Purification and characterization of human laminin-8. Laminin-8 stimulates cell adhesion and migration through α3β1 and α6β1 integrins
    • Fujiwara, H., Kikkawa, Y., Sanzen, N. and Sekiguchi, K. (2001) Purification and characterization of human laminin-8. Laminin-8 stimulates cell adhesion and migration through α3β1 and α6β1 integrins. J. Biol. Chem. 276, 17550-17558
    • (2001) J. Biol. Chem. , vol.276 , pp. 17550-17558
    • Fujiwara, H.1    Kikkawa, Y.2    Sanzen, N.3    Sekiguchi, K.4
  • 23
    • 0034686077 scopus 로고    scopus 로고
    • Recombinant laminin-8 (α4β1γ1): Production, purification, and interactions with integrins
    • Kortesmaa, J., Yurchenco, P. and Tryggvason, K. (2000) Recombinant laminin-8 (α4β1γ1): production, purification, and interactions with integrins. J. Biol. Chem. 275, 14853-14859
    • (2000) J. Biol. Chem. , vol.275 , pp. 14853-14859
    • Kortesmaa, J.1    Yurchenco, P.2    Tryggvason, K.3
  • 24
    • 0037059038 scopus 로고    scopus 로고
    • Complex interactions between the laminin α4 subunit and integrins regulate endothelial cell behavior in vitro and angiogenesis in vivo
    • Gonzalez, A. M., Gonzales, M., Herron, G. S., Nagavarapu, U., Hopkinson, S. B., Tsuruta, D. and Jones, J. C. R. (2002) Complex interactions between the laminin α4 subunit and integrins regulate endothelial cell behavior in vitro and angiogenesis in vivo. Proc. Natl. Acad. Sci. U.S.A. 99, 16075-16080
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16075-16080
    • Gonzalez, A.M.1    Gonzales, M.2    Herron, G.S.3    Nagavarapu, U.4    Hopkinson, S.B.5    Tsuruta, D.6    Jones, J.C.R.7
  • 25
    • 0034703032 scopus 로고    scopus 로고
    • High and low affinity heparin-binding sites in the G domain of the mouse laminin α4 chain
    • Yamaguchi, H., Yamashita, H., Mori, H., Okazaki, I., Nomizu, M., Beck, K. and Kitagawa, Y. (2000) High and low affinity heparin-binding sites in the G domain of the mouse laminin α4 chain. J. Biol. Chem. 275, 29458-29465
    • (2000) J. Biol. Chem. , vol.275 , pp. 29458-29465
    • Yamaguchi, H.1    Yamashita, H.2    Mori, H.3    Okazaki, I.4    Nomizu, M.5    Beck, K.6    Kitagawa, Y.7
  • 26
    • 0347914554 scopus 로고    scopus 로고
    • Heparin binds to the laminin α4 chain LG4 domain at a site different from that found for other laminins
    • Yamashita, H., Beck, K. and Kitagawa, Y. (2004) Heparin binds to the laminin α4 chain LG4 domain at a site different from that found for other laminins. J. Mol. Biol. 335, 1145-1149
    • (2004) J. Mol. Biol. , vol.335 , pp. 1145-1149
    • Yamashita, H.1    Beck, K.2    Kitagawa, Y.3
  • 28
    • 0030926051 scopus 로고    scopus 로고
    • Expression of the long arm sequence of mouse laminin α1, β1, or γ1 chain in COS1 cells and assembly of monkey-mouse hybrid laminin
    • Niimi, T., Miki, K. and Kitagawa, Y. (1997) Expression of the long arm sequence of mouse laminin α1, β1, or γ1 chain in COS1 cells and assembly of monkey-mouse hybrid laminin. J. Biochem. (Tokyo) 121, 854-861
    • (1997) J. Biochem. (Tokyo) , vol.121 , pp. 854-861
    • Niimi, T.1    Miki, K.2    Kitagawa, Y.3
  • 29
    • 0024580166 scopus 로고
    • Multiple distinct membrane heparan sulfate proteoglycans in human lung fibroblasts
    • Lories, V., Cassiman, J. J., Vanden Berghe, H. and David, G. (1989) Multiple distinct membrane heparan sulfate proteoglycans in human lung fibroblasts. J. Biol. Chem. 264, 7009-7016
    • (1989) J. Biol. Chem. , vol.264 , pp. 7009-7016
    • Lories, V.1    Cassiman, J.J.2    Vanden Berghe, H.3    David, G.4
  • 30
    • 0026593295 scopus 로고
    • Differential expression of cell surface heparan sulfate proteoglycans in human mammary epithelial cells and lung fibroblasts
    • Lories, V., Cassiman, J. J., Van den Berghe, H. and David, G. (1992) Differential expression of cell surface heparan sulfate proteoglycans in human mammary epithelial cells and lung fibroblasts. J. Biol. Chem. 267, 1116-1122
    • (1992) J. Biol. Chem. , vol.267 , pp. 1116-1122
    • Lories, V.1    Cassiman, J.J.2    Van Den Berghe, H.3    David, G.4
  • 31
    • 0026675026 scopus 로고
    • Molecular cloning of amphiglycan, a novel integral membrane heparan sulfate proteoglycan expressed by epithelial and fibroblastic cells
    • David, G., Van der Schueren, B., Marynen, P., Cassiman, J. J. and Van den Berghe, H. (1992) Molecular cloning of amphiglycan, a novel integral membrane heparan sulfate proteoglycan expressed by epithelial and fibroblastic cells. J. Cell Biol. 118, 961-969
    • (1992) J. Cell Biol. , vol.118 , pp. 961-969
    • David, G.1    Van Der Schueren, B.2    Marynen, P.3    Cassiman, J.J.4    Van Den Berghe, H.5
  • 32
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 33
    • 0025043808 scopus 로고
    • Identification of a lipid-anchored heparan sulfate proteoglycan in Schwann cells
    • Carey, D. J. and Stahl, R. C. (1990) Identification of a lipid-anchored heparan sulfate proteoglycan in Schwann cells. J. Cell Biol. 111, 2053-2062
    • (1990) J. Cell Biol. , vol.111 , pp. 2053-2062
    • Carey, D.J.1    Stahl, R.C.2
  • 34
    • 0025953905 scopus 로고
    • Phospholipase C release of basic fibroblast growth factor from human bone marrow cultures as a biologically active complex with a phosphatidylinositol- anchored heparan sulfate proteoglycan
    • Brunner, G., Gabrilove, J., Rifkin, D. B. and Wilson, E. L. (1991) Phospholipase C release of basic fibroblast growth factor from human bone marrow cultures as a biologically active complex with a phosphatidylinositol-anchored heparan sulfate proteoglycan. J. Cell Biol. 114, 1275-1283
    • (1991) J. Cell Biol. , vol.114 , pp. 1275-1283
    • Brunner, G.1    Gabrilove, J.2    Rifkin, D.B.3    Wilson, E.L.4
  • 35
    • 0035282226 scopus 로고    scopus 로고
    • Drosophila mitochondrial transcription factor A (d-TFAM) is dispensable for the transcription of mitochondrial DNA in Kc167 cells
    • Goto, A., Matsushima, Y., Kadowaki, T. and Kitagawa, Y. (2001) Drosophila mitochondrial transcription factor A (d-TFAM) is dispensable for the transcription of mitochondrial DNA in Kc167 cells. Biochem. J. 354, 43-48
    • (2001) Biochem. J. , vol.354 , pp. 43-48
    • Goto, A.1    Matsushima, Y.2    Kadowaki, T.3    Kitagawa, Y.4
  • 36
    • 0035890496 scopus 로고    scopus 로고
    • α-, β-, or γ-chain-specific RNA interference of laminin assembly in Drosophila Kc167 cells
    • Goto, A., Aoki, M., Ichihara, S. and Kitagawa, Y. (2001) α-, β-, or γ-chain-specific RNA interference of laminin assembly in Drosophila Kc167 cells. Biochem. J. 360, 167-172
    • (2001) Biochem. J. , vol.360 , pp. 167-172
    • Goto, A.1    Aoki, M.2    Ichihara, S.3    Kitagawa, Y.4
  • 37
    • 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, J. J. and Yurchenco, P. D. (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
  • 38
    • 0035152025 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are critical for the organization of the extracellular distribution of Wingless
    • Baeg, G. H., Lin, X., Khare, N., Baumgartner, S. and Perrimon, N. (2001) Heparan sulfate proteoglycans are critical for the organization of the extracellular distribution of Wingless. Development 128, 87-94
    • (2001) Development , vol.128 , pp. 87-94
    • Baeg, G.H.1    Lin, X.2    Khare, N.3    Baumgartner, S.4    Perrimon, N.5
  • 39
    • 0029844909 scopus 로고    scopus 로고
    • Glycosaminoglycans can modulate extracellular localization of the wingless protein and promote signal transduction
    • Reichsman, F., Smith, L. and Cumberledge, S. (1996) Glycosaminoglycans can modulate extracellular localization of the wingless protein and promote signal transduction. J. Cell Biol. 135, 819-827
    • (1996) J. Cell Biol. , vol.135 , pp. 819-827
    • Reichsman, F.1    Smith, L.2    Cumberledge, S.3
  • 41
    • 0032477786 scopus 로고    scopus 로고
    • De novo adipogenesis in mice at the site of injection of basement membrane and basic fibroblast growth factor
    • Kawaguchi, N., Toriyama, K., Nicodemou-Lena, E., Inou, K., Torii, S. and Kitagawa, Y. (1998) De novo adipogenesis in mice at the site of injection of basement membrane and basic fibroblast growth factor. Proc. Natl. Acad. Sci. U.S.A. 95, 1062-1066
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 1062-1066
    • Kawaguchi, N.1    Toriyama, K.2    Nicodemou-Lena, E.3    Inou, K.4    Torii, S.5    Kitagawa, Y.6
  • 42
    • 0032746544 scopus 로고    scopus 로고
    • Syndecan-4 and integrins: Combinatorial signaling in cell adhesion
    • Couchman, J. R. and Woods, A. (1999) Syndecan-4 and integrins: combinatorial signaling in cell adhesion. J. Cell Sci. 112, 3415-3420
    • (1999) J. Cell Sci. , vol.112 , pp. 3415-3420
    • Couchman, J.R.1    Woods, A.2
  • 43
    • 0030889054 scopus 로고    scopus 로고
    • Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C
    • Oh, E. S., Woods, A. and Couchman, J. R. (1997) Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C. J. Biol. Chem. 272, 8133-8136
    • (1997) J. Biol. Chem. , vol.272 , pp. 8133-8136
    • Oh, E.S.1    Woods, A.2    Couchman, J.R.3
  • 44
    • 0032562706 scopus 로고    scopus 로고
    • Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity
    • Oh, E. S., Woods, A., Lim, S. T., Theibert, A. W. and Couchman, J. R. (1998) Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity. J. Biol. Chem. 273, 10624-10629
    • (1998) J. Biol. Chem. , vol.273 , pp. 10624-10629
    • Oh, E.S.1    Woods, A.2    Lim, S.T.3    Theibert, A.W.4    Couchman, J.R.5
  • 45
    • 0030911243 scopus 로고    scopus 로고
    • Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C
    • Oh, E. S., Woods, A. and Couchman, J. R. (1997) Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C. J. Biol. Chem. 272, 11805-11811
    • (1997) J. Biol. Chem. , vol.272 , pp. 11805-11811
    • Oh, E.S.1    Woods, A.2    Couchman, J.R.3
  • 47
    • 0032746544 scopus 로고    scopus 로고
    • Syndecan-4 and integrins: Combinatorial signaling in cell adhesion
    • Couchman, J. R. and Woods, A. (1999) Syndecan-4 and integrins: combinatorial signaling in cell adhesion. J. Cell Sci. 112, 3415-3420
    • (1999) J. Cell Sci. , vol.112 , pp. 3415-3420
    • Couchman, J.R.1    Woods, A.2


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