메뉴 건너뛰기




Volumn 10, Issue 5, 1998, Pages 620-628

Molecular interactions of the syndecan core proteins

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; MEMBRANE PROTEIN; PROTEOHEPARAN SULFATE; SCLEROPROTEIN; SYNDECAN;

EID: 0031672037     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80038-0     Document Type: Article
Times cited : (102)

References (63)
  • 1
    • 0030660196 scopus 로고    scopus 로고
    • Syndecans: Multifunctional cell-surface co-receptors
    • Carey DJ. Syndecans: multifunctional cell-surface co-receptors. Biochem J. 327:1997;1-16.
    • (1997) Biochem J , vol.327 , pp. 1-16
    • Carey, D.J.1
  • 2
    • 0032080892 scopus 로고    scopus 로고
    • Syndecans: Synergistic activators of cell adhesion
    • Woods A, Couchman JR. Syndecans: synergistic activators of cell adhesion. Trends Cell Biol. 8:1998;189-192.
    • (1998) Trends Cell Biol , vol.8 , pp. 189-192
    • Woods, A.1    Couchman, J.R.2
  • 3
    • 0030669701 scopus 로고    scopus 로고
    • Structure - Activity relationship of heparan sulphate
    • Gallagher JT. Structure - activity relationship of heparan sulphate. Biochem Soc Trans. 25:1997;1206-1209.
    • (1997) Biochem Soc Trans , vol.25 , pp. 1206-1209
    • Gallagher, J.T.1
  • 4
    • 0030775796 scopus 로고    scopus 로고
    • Cell-surface heparan sulfate proteoglycans: Dynamic molecules mediating ligand catabolism
    • of special interest. The internalization of proteoglycans, largely through catabolism of their glycosaminoglycan chains, has been documented previously. This paper addresses the determinants of the syndecan core protein necessary for its uptake and localization to internalization sites on the membrane
    • Williams KJ, Fuki IV. Cell-surface heparan sulfate proteoglycans: dynamic molecules mediating ligand catabolism. of special interest Curr Opin Lipidol. 8:1997;253-262 The internalization of proteoglycans, largely through catabolism of their glycosaminoglycan chains, has been documented previously. This paper addresses the determinants of the syndecan core protein necessary for its uptake and localization to internalization sites on the membrane.
    • (1997) Curr Opin Lipidol , vol.8 , pp. 253-262
    • Williams, K.J.1    Fuki, I.V.2
  • 5
    • 0030330635 scopus 로고    scopus 로고
    • The glypican family of heparan sulfate proteoglycans: Major cell-surface proteoglycans of the developing nervous system
    • Lander AD, Stipp CS, Ivins JK. The glypican family of heparan sulfate proteoglycans: major cell-surface proteoglycans of the developing nervous system. Perspect Dev Neurobiol. 3:1996;347-358.
    • (1996) Perspect Dev Neurobiol , vol.3 , pp. 347-358
    • Lander, A.D.1    Stipp, C.S.2    Ivins, J.K.3
  • 6
    • 0032514259 scopus 로고    scopus 로고
    • Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells
    • of outstanding interest. This work provides exciting evidence for the potential linkage of syndecans to the cytoskeleton and a means of anchorage at the basolateral surface of epithelial cells
    • Cohen AR, Woods DF, Marfatia SM, Walther Z, Chishti AH, Anderson JM. Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells. of outstanding interest J Cell Biol. 142:1998;129-138 This work provides exciting evidence for the potential linkage of syndecans to the cytoskeleton and a means of anchorage at the basolateral surface of epithelial cells.
    • (1998) J Cell Biol , vol.142 , pp. 129-138
    • Cohen, A.R.1    Woods, D.F.2    Marfatia, S.M.3    Walther, Z.4    Chishti, A.H.5    Anderson, J.M.6
  • 7
    • 0031457554 scopus 로고    scopus 로고
    • Syntenin, a PDZ protein that binds syndecan cytoplasmic domains
    • of outstanding interest. This is the first report of PDZ protein binding to syndecan cytoplasmic domains and suggests a mechanism for syndecan clustering and anchorage at the plasma membrane
    • Grootjans JJ, Zimmermann P, Reekmans G, Smets A, Degeest G, Durr J, David G. Syntenin, a PDZ protein that binds syndecan cytoplasmic domains. of outstanding interest Proc Natl Acad Sci USA. 94:1997;13683-13688 This is the first report of PDZ protein binding to syndecan cytoplasmic domains and suggests a mechanism for syndecan clustering and anchorage at the plasma membrane.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13683-13688
    • Grootjans, J.J.1    Zimmermann, P.2    Reekmans, G.3    Smets, A.4    Degeest, G.5    Durr, J.6    David, G.7
  • 8
    • 0032514263 scopus 로고    scopus 로고
    • Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    • of outstanding interest. Another exciting report of CASK binding to syndecans, here, syndecan-2 in the synapse. The synapse is an excellent example of receptor clustering and anchorage to a highly organized membrane domain and may serve as a paradigm for syndecan anchorage in other types of cells
    • Hsueh Y-P, Yang F-C, Kharazia V, Naisbitt S, Cohen AR, Weinberg RJ, Sheng M. Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses. of outstanding interest J Cell Biol. 142:1998;139-151 Another exciting report of CASK binding to syndecans, here, syndecan-2 in the synapse. The synapse is an excellent example of receptor clustering and anchorage to a highly organized membrane domain and may serve as a paradigm for syndecan anchorage in other types of cells.
    • (1998) J Cell Biol , vol.142 , pp. 139-151
    • Hsueh Y-P1    Yang F-C2    Kharazia, V.3    Naisbitt, S.4    Cohen, A.R.5    Weinberg, R.J.6    Sheng, M.7
  • 9
    • 0030889054 scopus 로고    scopus 로고
    • Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C
    • of outstanding interest. This paper, together with [10-12], documents the binding of activated PKCα to the syndecan-4 cytoplasmic domain. This pioneering work is the first clear evidence for intracellular signaling molecules binding directly to syndecans. The localization of syndecan-4 in focal adhesions makes it a central player in the signaling that occurs in these structures
    • Oh ES, Woods A, Couchman JR. Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C. of outstanding interest J Biol Chem. 272:1997;8133-8136 This paper, together with [10-12], documents the binding of activated PKCα to the syndecan-4 cytoplasmic domain. This pioneering work is the first clear evidence for intracellular signaling molecules binding directly to syndecans. The localization of syndecan-4 in focal adhesions makes it a central player in the signaling that occurs in these structures.
    • (1997) J Biol Chem , vol.272 , pp. 8133-8136
    • Oh, E.S.1    Woods, A.2    Couchman, J.R.3
  • 10
    • 0030911243 scopus 로고    scopus 로고
    • Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C
    • of outstanding interest. See annotation to [9]
    • Oh ES, Woods A, Couchman JR. Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C. of outstanding interest J Biol Chem. 272:1997;11805-11811 See annotation to [9].
    • (1997) J Biol Chem , vol.272 , pp. 11805-11811
    • Oh, E.S.1    Woods, A.2    Couchman, J.R.3
  • 11
    • 0032562706 scopus 로고    scopus 로고
    • Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity
    • of outstanding interest. See annotation to [9]
    • Oh ES, Woods A, Lim ST, Theibert AW, Couchman JR. Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity. of outstanding interest J Biol Chem. 273:1998;10624-10629 See annotation to [9].
    • (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
  • 12
    • 0032557438 scopus 로고    scopus 로고
    • Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate
    • of outstanding interest. See annotation to [9]
    • Lee D, Oh ES, Woods A, Couchman JR, Lee W. Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate. of outstanding interest J Biol Chem. 273:1998;13022-13029 See annotation to [9].
    • (1998) J Biol Chem , vol.273 , pp. 13022-13029
    • Lee, D.1    Oh, E.S.2    Woods, A.3    Couchman, J.R.4    Lee, W.5
  • 13
    • 0029953925 scopus 로고    scopus 로고
    • Syndecans, signaling and cell adhesion
    • Couchman JR, Woods A. Syndecans, signaling and cell adhesion. J Cell Biochem. 61:1996;578-584.
    • (1996) J Cell Biochem , vol.61 , pp. 578-584
    • Couchman, J.R.1    Woods, A.2
  • 14
    • 0028880289 scopus 로고
    • Protein kinase C regulates the recruitment of syndecan-4 into focal contacts
    • Baciu PC, Goetinck PF. Protein kinase C regulates the recruitment of syndecan-4 into focal contacts. Mol Biol Cell. 6:1995;1503-1513.
    • (1995) Mol Biol Cell , vol.6 , pp. 1503-1513
    • Baciu, P.C.1    Goetinck, P.F.2
  • 15
    • 0030960152 scopus 로고    scopus 로고
    • Identification of an adhesion site within the syndecan-4 extracellular protein domain
    • of special interest of outstanding interest. This paper, together with the following report [16], is the first work showing that syndecan extracellular protein domains have roles in molecular interactions apart from their heparan sulfate chains
    • McFall AJ, Rapraeger AC. Identification of an adhesion site within the syndecan-4 extracellular protein domain. of special interest of outstanding interest J Biol Chem. 272:1997;12901-12904 This paper, together with the following report [16], is the first work showing that syndecan extracellular protein domains have roles in molecular interactions apart from their heparan sulfate chains.
    • (1997) J Biol Chem , vol.272 , pp. 12901-12904
    • McFall, A.J.1    Rapraeger, A.C.2
  • 16
    • 0032561184 scopus 로고    scopus 로고
    • Characterization of the high-affinity cell binding domain in the cell surface proteoglycan syndecan-4
    • of outstanding interest of special interest
    • McFall AJ, Rapraeger AC. Characterization of the high-affinity cell binding domain in the cell surface proteoglycan syndecan-4. of outstanding interest of special interest J Biol Chem. 1998; See annotation to [15].
    • (1998) J Biol Chem
    • McFall, A.J.1    Rapraeger, A.C.2
  • 17
    • 0028842497 scopus 로고
    • Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region
    • Asundi VK, Carey DJ. Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region. J Biol Chem. 270:1995;26404-26410.
    • (1995) J Biol Chem , vol.270 , pp. 26404-26410
    • Asundi, V.K.1    Carey, D.J.2
  • 18
    • 0027315260 scopus 로고
    • A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation
    • Woods A, McCarthy JB, Furcht LT, Couchman JR. A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation. Mol Biol Cell. 4:1993;605-613.
    • (1993) Mol Biol Cell , vol.4 , pp. 605-613
    • Woods, A.1    McCarthy, J.B.2    Furcht, L.T.3    Couchman, J.R.4
  • 19
  • 20
    • 0031749471 scopus 로고    scopus 로고
    • Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2
    • of special interest. This and the following two reports [21,22] begin to look at the regulation and physiological significance of syndecan shedding. This places the shed ectodomains and their multifunctional heparan sulfate chains within wound sites where they are likely to be key regulators of wound healing processes
    • Kato M, Wang H, Kainulainen V, Fitzgerald ML, Ledbetter S, Omitz DM, Bernfield M. Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2. of special interest Nat Med. 4:1998;691-697 This and the following two reports [21,22] begin to look at the regulation and physiological significance of syndecan shedding. This places the shed ectodomains and their multifunctional heparan sulfate chains within wound sites where they are likely to be key regulators of wound healing processes.
    • (1998) Nat Med , vol.4 , pp. 691-697
    • Kato, M.1    Wang, H.2    Kainulainen, V.3    Fitzgerald, M.L.4    Ledbetter, S.5    Omitz, D.M.6    Bernfield, M.7
  • 21
    • 0030967612 scopus 로고    scopus 로고
    • Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor receptor activation
    • of special interest. See annotation to [20]
    • Subramanian SV, Fitzgerald ML, Bernfield M. Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor receptor activation. of special interest J Biol Chem. 272:1997;14713-14720 See annotation to [20].
    • (1997) J Biol Chem , vol.272 , pp. 14713-14720
    • Subramanian, S.V.1    Fitzgerald, M.L.2    Bernfield, M.3
  • 22
    • 0032496145 scopus 로고    scopus 로고
    • Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids
    • of special interest. See annotation to [20]
    • Kainulainen V, Wang H, Schick C, Bernfield M. Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids. of special interest J Biol Chem. 273:1998;11563-11569 See annotation to [20].
    • (1998) J Biol Chem , vol.273 , pp. 11563-11569
    • Kainulainen, V.1    Wang, H.2    Schick, C.3    Bernfield, M.4
  • 23
    • 0032575578 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans as adhesive and anti-invasive molecules: Syndecans and glypicans have distinct functions
    • of special interest. An interesting paper that extends the work from this group and begins to analyze the domains of syndecan-1 that influence signaling during cell invasion
    • Liu W, Litwack ED, Stanley MJ, Langford JK, Lander AD, Sanderson RA. Heparan sulfate proteoglycans as adhesive and anti-invasive molecules: syndecans and glypicans have distinct functions. of special interest J Biol Chem. 273:1998;22825-22832 An interesting paper that extends the work from this group and begins to analyze the domains of syndecan-1 that influence signaling during cell invasion.
    • (1998) J Biol Chem , vol.273 , pp. 22825-22832
    • Liu, W.1    Litwack, E.D.2    Stanley, M.J.3    Langford, J.K.4    Lander, A.D.5    Sanderson, R.A.6
  • 24
    • 0030293766 scopus 로고    scopus 로고
    • Protein - Protein interactions: PDZ domain networks
    • Fanning AS, Anderson J. Protein - protein interactions: PDZ domain networks. Curr Biol. 6:1996;1385-1388.
    • (1996) Curr Biol , vol.6 , pp. 1385-1388
    • Fanning, A.S.1    Anderson, J.2
  • 26
    • 0029914941 scopus 로고    scopus 로고
    • CASK: A novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins
    • Hata Y, Butz S, Sudhof TC. CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J Neurosci. 16:1996;2488-2494.
    • (1996) J Neurosci , vol.16 , pp. 2488-2494
    • Hata, Y.1    Butz, S.2    Sudhof, T.C.3
  • 27
    • 0030763609 scopus 로고    scopus 로고
    • The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C. Analysis of the binding interface by in vitro mutagenesis
    • Marfatia SM, Morais-Cabral JH, Kim AC, Byron O, Chishti AH. The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C. Analysis of the binding interface by in vitro mutagenesis. J Biol Chem. 272:1997;24191-24197.
    • (1997) J Biol Chem , vol.272 , pp. 24191-24197
    • Marfatia, S.M.1    Morais-Cabral, J.H.2    Kim, A.C.3    Byron, O.4    Chishti, A.H.5
  • 28
    • 0029143156 scopus 로고
    • Tight junctions, membrane-associated guanylate kinases and cell signaling
    • Kim SK. Tight junctions, membrane-associated guanylate kinases and cell signaling. Curr Opin Cell Biol. 7:1995;641-649.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 641-649
    • Kim, S.K.1
  • 29
    • 0028917977 scopus 로고
    • Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein
    • Marfatia SM, Leu RA, Branton D, Chishti AH. Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein. J Biol Chem. 270:1995;715-719.
    • (1995) J Biol Chem , vol.270 , pp. 715-719
    • Marfatia, S.M.1    Leu, R.A.2    Branton, D.3    Chishti, A.H.4
  • 33
    • 0030926546 scopus 로고    scopus 로고
    • Deciphering the function of neurexins at cellular junctions
    • Littleton JT, Bhat MA, Bellen HJ. Deciphering the function of neurexins at cellular junctions. J Cell Biol. 137:1997;793-796.
    • (1997) J Cell Biol , vol.137 , pp. 793-796
    • Littleton, J.T.1    Bhat, M.A.2    Bellen, H.J.3
  • 34
    • 0032562591 scopus 로고    scopus 로고
    • Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth
    • of outstanding interest. An important paper that is the first description of tyrosine kinases isolated from cell extracts through interaction with a syndecan cytoplasmic domain; furthermore, the activity of the kinase complex is regulated by extracellular ligands binding the heparan sulfate chains on the syndecans
    • Kinnunen T, Kaksonen M, Saarinen J, Kalkkinen N, Peng HB, Rauvala H. Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth. of outstanding interest J Biol Chem. 273:1998;10702-10708 An important paper that is the first description of tyrosine kinases isolated from cell extracts through interaction with a syndecan cytoplasmic domain; furthermore, the activity of the kinase complex is regulated by extracellular ligands binding the heparan sulfate chains on the syndecans.
    • (1998) J Biol Chem , vol.273 , pp. 10702-10708
    • Kinnunen, T.1    Kaksonen, M.2    Saarinen, J.3    Kalkkinen, N.4    Peng, H.B.5    Rauvala, H.6
  • 35
    • 0030905752 scopus 로고    scopus 로고
    • HB-GAM (heparin-binding growth-associated molecule) and heparin-type glycans in the development and plasticity of neuron-target contacts
    • Rauvala H, Peng HB. HB-GAM (heparin-binding growth-associated molecule) and heparin-type glycans in the development and plasticity of neuron-target contacts. Prog Neurobiol. 52:1997;127-144.
    • (1997) Prog Neurobiol , vol.52 , pp. 127-144
    • Rauvala, H.1    Peng, H.B.2
  • 36
    • 0031214383 scopus 로고    scopus 로고
    • Serine phosphorylation of syndecan-2 proteoglycan cytoplasmic domain
    • Oh ES, Couchman JR, Woods A. Serine phosphorylation of syndecan-2 proteoglycan cytoplasmic domain. Arch Biochem Biophys. 344:1997;67-74.
    • (1997) Arch Biochem Biophys , vol.344 , pp. 67-74
    • Oh, E.S.1    Couchman, J.R.2    Woods, A.3
  • 37
  • 38
    • 0029929433 scopus 로고    scopus 로고
    • Phosphorylation of a membrane-intercalated proteoglycan, syndecan-2, expressed in a stroma-inducing clone from a mouse Lewis lung carcinoma
    • Itano N, Oguri K, Nagayasu Y, Kusano Y, Nakanishi H, David G, Okayama M. Phosphorylation of a membrane-intercalated proteoglycan, syndecan-2, expressed in a stroma-inducing clone from a mouse Lewis lung carcinoma. Biochem J. 315:1996;925-930.
    • (1996) Biochem J , vol.315 , pp. 925-930
    • Itano, N.1    Oguri, K.2    Nagayasu, Y.3    Kusano, Y.4    Nakanishi, H.5    David, G.6    Okayama, M.7
  • 39
    • 0032080332 scopus 로고    scopus 로고
    • Regulation of syndecan-4 phosphorylation in vivo
    • of special interest. An important paper that is one of the first descriptions of endogenous syndecan phosphorylation on serine. Importantly, it also shows regulation by FGF-2, a potential ligand for the syndecan
    • Horowitz A, Simons M. Regulation of syndecan-4 phosphorylation in vivo. of special interest J Biol Chem. 273:1998;10914-10918 An important paper that is one of the first descriptions of endogenous syndecan phosphorylation on serine. Importantly, it also shows regulation by FGF-2, a potential ligand for the syndecan.
    • (1998) J Biol Chem , vol.273 , pp. 10914-10918
    • Horowitz, A.1    Simons, M.2
  • 40
    • 17544378558 scopus 로고    scopus 로고
    • The cytoplasmic domain of syndecan-1 is required for cytoskeleton association but not detergent insolubility. Identification of essential cytoplasmic domain residues
    • Carey DJ, Bendt KM, Stahl RC. The cytoplasmic domain of syndecan-1 is required for cytoskeleton association but not detergent insolubility. Identification of essential cytoplasmic domain residues. J Biol Chem. 271:1996;15253-15260.
    • (1996) J Biol Chem , vol.271 , pp. 15253-15260
    • Carey, D.J.1    Bendt, K.M.2    Stahl, R.C.3
  • 41
    • 0031960011 scopus 로고    scopus 로고
    • Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition
    • Daniels DL, Cohen AR, Anderson JM, Brunger AT. Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition. Nat Struct Biol. 5:1998;317-325.
    • (1998) Nat Struct Biol , vol.5 , pp. 317-325
    • Daniels, D.L.1    Cohen, A.R.2    Anderson, J.M.3    Brunger, A.T.4
  • 42
    • 0029853095 scopus 로고    scopus 로고
    • Pervanadate activation of intracellular kinases leads to tyrosine phosphorylation and shedding of syndecan-1
    • Reiland J, Ott VL, Lebakken CS, Yeaman C, McCarthy J, Rapraeger AC. Pervanadate activation of intracellular kinases leads to tyrosine phosphorylation and shedding of syndecan-1. Biochem J. 319:1996;39-47.
    • (1996) Biochem J , vol.319 , pp. 39-47
    • Reiland, J.1    Ott, V.L.2    Lebakken, C.S.3    Yeaman, C.4    McCarthy, J.5    Rapraeger, A.C.6
  • 43
    • 0031576407 scopus 로고    scopus 로고
    • Phosphorylation of recombinant N-syndecan (syndecan 3) core protein
    • Asundi VK, Carey DJ. Phosphorylation of recombinant N-syndecan (syndecan 3) core protein. Biochem Biophys Res Commun. 240:1997;502-506.
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 502-506
    • Asundi, V.K.1    Carey, D.J.2
  • 44
    • 0029919670 scopus 로고    scopus 로고
    • Syndecan-1 mediates cell spreading in transfected human lymphoblastoid (Rajl) cells
    • Lebakken CS, Rapraeger AC. Syndecan-1 mediates cell spreading in transfected human lymphoblastoid (Rajl) cells. J Cell Biol. 132:1996;1209-1221.
    • (1996) J Cell Biol , vol.132 , pp. 1209-1221
    • Lebakken, C.S.1    Rapraeger, A.C.2
  • 46
    • 0024556678 scopus 로고
    • Molecular cloning of syndecan, an integral membrane proteoglycan
    • Saunders S, Jalkanen M, O'Farrell S, Bernfield M. Molecular cloning of syndecan, an integral membrane proteoglycan. J Cell Biol. 108:1989;1547-1556.
    • (1989) J Cell Biol , vol.108 , pp. 1547-1556
    • Saunders, S.1    Jalkanen, M.2    O'Farrell, S.3    Bernfield, M.4
  • 47
    • 0025240364 scopus 로고
    • Sequence of human syndecan indicates a novel gene family of integral membrane proteoglycans
    • Mali M, Jaakkola P, Arvilommi AM, Jalkanen M. Sequence of human syndecan indicates a novel gene family of integral membrane proteoglycans. J Biol Chem. 265:1990;6884-6889.
    • (1990) J Biol Chem , vol.265 , pp. 6884-6889
    • Mali, M.1    Jaakkola, P.2    Arvilommi, A.M.3    Jalkanen, M.4
  • 48
    • 0026756376 scopus 로고
    • Molecular cloning and expression of two distinct cDNA-encoding heparan sulfate proteoglycan core proteins from a rat endothelial cell line
    • Kojima T, Shworak NW, Rosenberg RD. Molecular cloning and expression of two distinct cDNA-encoding heparan sulfate proteoglycan core proteins from a rat endothelial cell line. J Biol Chem. 267:1992;4870-4877.
    • (1992) J Biol Chem , vol.267 , pp. 4870-4877
    • Kojima, T.1    Shworak, N.W.2    Rosenberg, R.D.3
  • 49
    • 0025103944 scopus 로고
    • Ligand-affinity cloning and structure of a cell surface heparan sulfate proteoglycan that binds basic fibroblast growth factor
    • Kiefer MC, Stephans JC, Crawford K, Okino K, Barr PJ. Ligand-affinity cloning and structure of a cell surface heparan sulfate proteoglycan that binds basic fibroblast growth factor. Proc Natl Acad Sci USA. 87:1990;6985-6989.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6985-6989
    • Kiefer, M.C.1    Stephans, J.C.2    Crawford, K.3    Okino, K.4    Barr, P.J.5
  • 50
    • 0028892362 scopus 로고
    • Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans
    • Zhang L, David G, Esko JD. Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans. J Biol Chem. 270:1995;27127-27135.
    • (1995) J Biol Chem , vol.270 , pp. 27127-27135
    • Zhang, L.1    David, G.2    Esko, J.D.3
  • 51
    • 0030273128 scopus 로고    scopus 로고
    • Embryonic expression patterns of Xenopus syndecans
    • Teel AL, Yost HJ. Embryonic expression patterns of Xenopus syndecans. Mech Dev. 59:1996;115-127.
    • (1996) Mech Dev , vol.59 , pp. 115-127
    • Teel, A.L.1    Yost, H.J.2
  • 52
    • 0027378157 scopus 로고
    • Spatial and temporal changes in the expression of fibroglycan (syndecan-2) during mouse embryonic development
    • David G, Bai XM, Van der Schueren B, Marynen P, Cassiman JJ, Van den Berghe H. Spatial and temporal changes in the expression of fibroglycan (syndecan-2) during mouse embryonic development. Development. 119:1993;841-854.
    • (1993) Development , vol.119 , pp. 841-854
    • David, G.1    Bai, X.M.2    Van Der Schueren, B.3    Marynen, P.4    Cassiman, J.J.5    Van Den Berghe, H.6
  • 53
    • 0024507583 scopus 로고
    • Partial primary structure of the 48- And 90-kilodalton core proteins of cell surface-associated heparan sulfate proteoglycans of lung fibroblasts. Prediction of an integral membrane domain and evidence for multiple distinct core proteins at the cell surface of human lung fibroblasts
    • Marynen P, Zhang J, Cassiman JJ, Van den Berghe H, David G. Partial primary structure of the 48- and 90-kilodalton core proteins of cell surface-associated heparan sulfate proteoglycans of lung fibroblasts. Prediction of an integral membrane domain and evidence for multiple distinct core proteins at the cell surface of human lung fibroblasts. J Biol Chem. 264:1989;7017-7024.
    • (1989) J Biol Chem , vol.264 , pp. 7017-7024
    • Marynen, P.1    Zhang, J.2    Cassiman, J.J.3    Van Den Berghe, H.4    David, G.5
  • 54
    • 0026742962 scopus 로고
    • Molecular cloning of the major cell surface heparan sulfate proteoglycan from rat liver
    • Pierce A, Lyon M, Hampson IN, Cowling GJ, Gallagher JT. Molecular cloning of the major cell surface heparan sulfate proteoglycan from rat liver. J Biol Chem. 267:1992;3894-3900.
    • (1992) J Biol Chem , vol.267 , pp. 3894-3900
    • Pierce, A.1    Lyon, M.2    Hampson, I.N.3    Cowling, G.J.4    Gallagher, J.T.5
  • 55
    • 0029008877 scopus 로고
    • Expression of a Xenopus counterpart of mammalian syndecan 2 during embryogenesis
    • Rosenblum ND, Botelho BB, Bemfield M. Expression of a Xenopus counterpart of mammalian syndecan 2 during embryogenesis. Biochem J. 309:1995;69-76.
    • (1995) Biochem J , vol.309 , pp. 69-76
    • Rosenblum, N.D.1    Botelho, B.B.2    Bemfield, M.3
  • 58
    • 0026508469 scopus 로고
    • Syndecan 3: A member of the syndecan family of membrane-intercalated proteoglycans that is expressed in high amounts at the onset of chicken limb cartilage differentiation
    • Gould SE, Upholt WB, Kosher RA. Syndecan 3: a member of the syndecan family of membrane-intercalated proteoglycans that is expressed in high amounts at the onset of chicken limb cartilage differentiation. Proc Natl Acad Sci USA. 89:1992;3271-3275.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3271-3275
    • Gould, S.E.1    Upholt, W.B.2    Kosher, R.A.3
  • 59
    • 0030831336 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization, promoter activity, and tissue-specific expression of the mouse ryudocan gene
    • Tsuzuki S, Kojima T, Katsumi A, Yamazaki T, Sugiura I, Saito H. Molecular cloning, genomic organization, promoter activity, and tissue-specific expression of the mouse ryudocan gene. J Biochem (Tokyo). 122:1997;17-24.
    • (1997) J Biochem (Tokyo) , vol.122 , pp. 17-24
    • Tsuzuki, S.1    Kojima, T.2    Katsumi, A.3    Yamazaki, T.4    Sugiura, I.5    Saito, H.6
  • 60
    • 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 JJ, Van den Berghe H. Molecular cloning of amphiglycan, a novel integral membrane heparan sulfate proteoglycan expressed by epithelial and fibroblastic cells. J Cell Biol. 118:1992;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
  • 61
    • 0028127744 scopus 로고
    • Molecular cloning and genomic organization of chicken syndecan-4
    • Baciu PC, Acaster C, Goetinck PF. Molecular cloning and genomic organization of chicken syndecan-4. J Biol Chem. 269:1994;696-703.
    • (1994) J Biol Chem , vol.269 , pp. 696-703
    • Baciu, P.C.1    Acaster, C.2    Goetinck, P.F.3
  • 63
    • 0000104067 scopus 로고    scopus 로고
    • Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family
    • Parra M, Gascard P, Walensky LD, Snyder SH, Mohandas N, Conboy JG. Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family. Genomics. 49:1998;298-306.
    • (1998) Genomics , vol.49 , pp. 298-306
    • Parra, M.1    Gascard, P.2    Walensky, L.D.3    Snyder, S.H.4    Mohandas, N.5    Conboy, J.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.