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Volumn 161, Issue 6, 2003, Pages 1179-1189

Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly

Author keywords

Cell adhesion; ERK; Focal adhesions; G proteins; Thrombospondin

Indexed keywords

CALRETICULIN; CELL PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; THROMBOSPONDIN;

EID: 0037477628     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200302069     Document Type: Article
Times cited : (140)

References (69)
  • 1
    • 0033546416 scopus 로고    scopus 로고
    • Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules
    • Arosa, F.A., O. de Jesus, G. Porto, A.M. Carmo, and M. de Sousa. 1999. Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules. J. Biol. Chem. 274:16917-16922.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16917-16922
    • Arosa, F.A.1    De Jesus, O.2    Porto, G.3    Carmo, A.M.4    De Sousa, M.5
  • 2
    • 0025231645 scopus 로고
    • The human alpha 2-macroglobulin receptor: Identification of a 420-kD cell surface glycoprotein specific for the activated conformation of alpha 2-macroglobulin
    • Ashcom, J.D., S.E. Tiller, K. Dickerson, J.L. Cravens, W.S. Argraves, and D.K. Strickland. 1990. The human alpha 2-macroglobulin receptor: identification of a 420-kD cell surface glycoprotein specific for the activated conformation of alpha 2-macroglobulin. J. Cell Biol. 110:1041-1048.
    • (1990) J. Cell Biol. , vol.110 , pp. 1041-1048
    • Ashcom, J.D.1    Tiller, S.E.2    Dickerson, K.3    Cravens, J.L.4    Argraves, W.S.5    Strickland, D.K.6
  • 3
    • 0027474006 scopus 로고
    • Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins
    • Aukhil, I., P. Joshi, Y. Yan, and H.P. Erickson. 1993. Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins. J. Biol. Chem. 268:2542-2553.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2542-2553
    • Aukhil, I.1    Joshi, P.2    Yan, Y.3    Erickson, H.P.4
  • 5
    • 0035374620 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated low density lipoprotein receptor-related protein 1 (LRP1) associates with the adapter protein SHC in SRC-transformed cells
    • Barnes, H., B. Larsen, M. Tyers, and P. van Der Geer. 2001. Tyrosine-phosphorylated low density lipoprotein receptor-related protein 1 (LRP1) associates with the adapter protein SHC in SRC-transformed cells. J. Biol. Chem. 276:19119-19125.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19119-19125
    • Barnes, H.1    Larsen, B.2    Tyers, M.3    Van Der Geer, P.4
  • 6
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu, S., R.J. Binder, T. Ramalingam, and P.K. Srivastava. 2001. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity. 14:303-313.
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 7
    • 0034252620 scopus 로고    scopus 로고
    • CD91: A receptor for heat shock protein gp96
    • Binder, R.J., D.K. Han, and P.K. Srivastava. 2000. CD91: a receptor for heat shock protein gp96. Nat. Immunol. 1:151-155.
    • (2000) Nat. Immunol. , vol.1 , pp. 151-155
    • Binder, R.J.1    Han, D.K.2    Srivastava, P.K.3
  • 8
    • 0037013188 scopus 로고    scopus 로고
    • Platelet-derived growth factor mediates tyrosine phosphorylation of the cytoplasmic domain of the low density lipoprotein receptor-related protein in caveolae
    • Boucher, P., P. Liu, M. Gotthardt, T. Hiesberger, R.G. Anderson, and J. Herz. 2002. Platelet-derived growth factor mediates tyrosine phosphorylation of the cytoplasmic domain of the low density lipoprotein receptor-related protein in caveolae. J. Biol. Chem. 277:15507-15513.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15507-15513
    • Boucher, P.1    Liu, P.2    Gotthardt, M.3    Hiesberger, T.4    Anderson, R.G.5    Herz, J.6
  • 10
    • 0033572799 scopus 로고    scopus 로고
    • Activation of human neutrophils by a synthetic anti-microbial peptide, KLKLLLLLKLK-NH2, via cell surface calreticulin
    • Cho, J.H., K. Homma, S. Kanegasaki, and S. Natori. 1999. Activation of human neutrophils by a synthetic anti-microbial peptide, KLKLLLLLKLK-NH2, via cell surface calreticulin. Eur. J. Biochem. 266:878-885.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 878-885
    • Cho, J.H.1    Homma, K.2    Kanegasaki, S.3    Natori, S.4
  • 11
    • 0034993230 scopus 로고    scopus 로고
    • Activation of human monocyte cell line U937 via cell surface calreticulin
    • Cho, J.H., K.J. Homma, S. Kanegasaki, and S. Natori. 2001. Activation of human monocyte cell line U937 via cell surface calreticulin. Cell Stress Chaperones. 6:148-152.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 148-152
    • Cho, J.H.1    Homma, K.J.2    Kanegasaki, S.3    Natori, S.4
  • 13
    • 0032211833 scopus 로고    scopus 로고
    • C1q-how many functions? How many receptors?
    • Eggleton, P., K.B. Reid, and A.J. Tenner. 1998. C1q-how many functions? How many receptors? Trends Cell Biol. 8:428-431.
    • (1998) Trends Cell Biol. , vol.8 , pp. 428-431
    • Eggleton, P.1    Reid, K.B.2    Tenner, A.J.3
  • 14
    • 0031451149 scopus 로고    scopus 로고
    • The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled
    • Ermekova, K.S., N. Zambrano, H. Linn, G. Minopoli, F. Gertler, T. Russo, and M. Sudol. 1997. The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled. J. Biol. Chem. 272:32869-32877.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32869-32877
    • Ermekova, K.S.1    Zambrano, N.2    Linn, H.3    Minopoli, G.4    Gertler, F.5    Russo, T.6    Sudol, M.7
  • 15
    • 0031689148 scopus 로고    scopus 로고
    • Regulation of myogenesis by fibroblast growth factors requires beta-gamma subunits of pertussis toxin-sensitive G proteins
    • Fedorov, Y.V., N.C. Jones, and B.B. Olwin. 1998. Regulation of myogenesis by fibroblast growth factors requires beta-gamma subunits of pertussis toxin-sensitive G proteins. Mol. Cell. Biol. 18:5780-5787.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5780-5787
    • Fedorov, Y.V.1    Jones, N.C.2    Olwin, B.B.3
  • 16
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A.G. 1987. G proteins: transducers of receptor-generated signals. Annu. Rev. Biochem. 56:615-649.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 18
    • 0029007213 scopus 로고
    • Identification of the low density lipoprotein receptor-related protein (LRP) as an endocytic receptor for thrombospondin-1
    • Godyna, S., G. Liau, I. Popa, S. Stefansson, and W.S. Argraves. 1995. Identification of the low density lipoprotein receptor-related protein (LRP) as an endocytic receptor for thrombospondin-1. J. Cell Biol. 129:1403-1410.
    • (1995) J. Cell Biol. , vol.129 , pp. 1403-1410
    • Godyna, S.1    Liau, G.2    Popa, I.3    Stefansson, S.4    Argraves, W.S.5
  • 19
    • 0034680794 scopus 로고    scopus 로고
    • Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
    • Goicoechea, S., A.W. Orr, M.A. Pallero, P. Eggleton, and J.E. Murphy-Ullrich. 2000. Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin. J. Biol. Chem. 275:36358-36368.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36358-36368
    • Goicoechea, S.1    Orr, A.W.2    Pallero, M.A.3    Eggleton, P.4    Murphy-Ullrich, J.E.5
  • 20
    • 0037020093 scopus 로고    scopus 로고
    • The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin
    • Goicoechea, S., M.A. Pallero, P. Eggleton, M. Michalak, and J.E. Murphy-Ullrich. 2002. The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin. J. Biol. Chem. 277:37219-37228.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37219-37228
    • Goicoechea, S.1    Pallero, M.A.2    Eggleton, P.3    Michalak, M.4    Murphy-Ullrich, J.E.5
  • 21
    • 0032373710 scopus 로고    scopus 로고
    • Low-density-lipoprotein-receptor-related protein (LRP) interacts with a GTP-binding protein
    • Goretzki, L., and B.M. Mueller. 1998. Low-density-lipoprotein-receptor-related protein (LRP) interacts with a GTP-binding protein. Biochem. J. 336:381-386.
    • (1998) Biochem. J. , vol.336 , pp. 381-386
    • Goretzki, L.1    Mueller, B.M.2
  • 22
    • 0034682827 scopus 로고    scopus 로고
    • Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction
    • Gotthardt, M., M. Trommsdorff, M.F. Nevitt, J. Shelton, J.A. Richardson, W. Stockinger, J. Nimpf, and J. Herz. 2000. Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. J. Biol. Chem. 275:25616-25624.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25616-25624
    • Gotthardt, M.1    Trommsdorff, M.2    Nevitt, M.F.3    Shelton, J.4    Richardson, J.A.5    Stockinger, W.6    Nimpf, J.7    Herz, J.8
  • 24
    • 0031915139 scopus 로고    scopus 로고
    • Thrombospondin signaling of focal adhesion disassembly requires activation of phosphoinositide 3-kinase
    • Greenwood, J.A., M.A. Pallero, A.B. Theibert, and J.E. Murphy-Ullrich. 1998. Thrombospondin signaling of focal adhesion disassembly requires activation of phosphoinositide 3-kinase. J. Biol. Chem. 273:1755-1763.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1755-1763
    • Greenwood, J.A.1    Pallero, M.A.2    Theibert, A.B.3    Murphy-Ullrich, J.E.4
  • 26
    • 0034723183 scopus 로고    scopus 로고
    • i with the insulin-like growth factor-I receptor. Release of Gβγ subunits upon receptor activation
    • i with the insulin-like growth factor-I receptor. Release of Gβγ subunits upon receptor activation. J. Biol. Chem. 275:2255-2258.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2255-2258
    • Hallak, H.1    Seiler, A.E.2    Green, J.S.3    Ross, B.N.4    Rubin, R.5
  • 27
    • 0034668838 scopus 로고    scopus 로고
    • Neuronal apoptosis by apolipoprotein E4 through low-density lipoprotein receptor-related protein and heterotrimeric GTPases
    • Hashimoto, Y., H. Jiang, T. Niikura, Y. Ito, A. Hagiwara, K. Umezawa, Y. Abe, Y. Murayama, and I. Nishimoto. 2000. Neuronal apoptosis by apolipoprotein E4 through low-density lipoprotein receptor-related protein and heterotrimeric GTPases. J. Neurosci. 20:8401-8409.
    • (2000) J. Neurosci. , vol.20 , pp. 8401-8409
    • Hashimoto, Y.1    Jiang, H.2    Niikura, T.3    Ito, Y.4    Hagiwara, A.5    Umezawa, K.6    Abe, Y.7    Murayama, Y.8    Nishimoto, I.9
  • 28
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • Herz, J., and D.K. Strickland. 2001. LRP: a multifunctional scavenger and signaling receptor. J. Clin. Invest. 108:779-784.
    • (2001) J. Clin. Invest. , vol.108 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 29
    • 0025369190 scopus 로고
    • Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment
    • Herz, J., R.C. Kowal, J.L. Goldstein, and M.S. Brown. 1990. Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment. EMBO J. 9:1769-1776.
    • (1990) EMBO J. , vol.9 , pp. 1769-1776
    • Herz, J.1    Kowal, R.C.2    Goldstein, J.L.3    Brown, M.S.4
  • 30
    • 0031695808 scopus 로고    scopus 로고
    • Cell-to-cell contact and extracellular matrix cell adhesion and the extracellular matrix: Recent progress and emerging themes
    • Horwitz, A.R., and Z. Werb. 1998. Cell-to-cell contact and extracellular matrix cell adhesion and the extracellular matrix: recent progress and emerging themes. Curr. Opin. Cell Biol. 10:563-565.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 563-565
    • Horwitz, A.R.1    Werb, Z.2
  • 31
    • 0035292695 scopus 로고    scopus 로고
    • Structural, biochemical and signaling properties of the low-density lipoprotein receptor gene family
    • Hussain, M.M. 2001. Structural, biochemical and signaling properties of the low-density lipoprotein receptor gene family. Front. Biosci. 6:D417-D428.
    • (2001) Front. Biosci. , vol.6
    • Hussain, M.M.1
  • 32
    • 0035279679 scopus 로고    scopus 로고
    • The ins and outs of calreticulin: From the ER lumen to the extracellular space
    • Johnson, S., M. Michalak, M. Opas, and P. Eggleton. 2001. The ins and outs of calreticulin: from the ER lumen to the extracellular space. Trends Cell Biol. 11:122-129.
    • (2001) Trends Cell Biol. , vol.11 , pp. 122-129
    • Johnson, S.1    Michalak, M.2    Opas, M.3    Eggleton, P.4
  • 34
    • 0026662463 scopus 로고
    • The 39-kDa receptor-associated protein interacts with two members of the low density lipoprotein receptor family, alpha 2-macroglobulin receptor and glycoprotein. 330
    • Kounnas, M.Z., W.S. Argraves, and D.K. Strickland. 1992a. The 39-kDa receptor-associated protein interacts with two members of the low density lipoprotein receptor family, alpha 2-macroglobulin receptor and glycoprotein. 330. J. Biol. Chem. 267:21162-21166.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21162-21166
    • Kounnas, M.Z.1    Argraves, W.S.2    Strickland, D.K.3
  • 35
    • 0026690341 scopus 로고
    • The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A
    • Kounnas, M.Z., R.E. Morris, M.R. Thompson, D.J. FitzGerald, D.K. Strickland, and C.B. Saelinger. 1992b. The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A. J. Biol. Chem. 267:12420-12423.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12420-12423
    • Kounnas, M.Z.1    Morris, R.E.2    Thompson, M.R.3    FitzGerald, D.J.4    Strickland, D.K.5    Saelinger, C.B.6
  • 36
    • 0032559021 scopus 로고    scopus 로고
    • Evidence that C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin and interferes with complement activation
    • Kovacs, H., I.D. Campbell, P. Strong, S. Johnson, F.J. Ward, K.B. Reid, and P. Eggleton. 1998. Evidence that C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin and interferes with complement activation. Biochemistry. 37:17865-17874.
    • (1998) Biochemistry , vol.37 , pp. 17865-17874
    • Kovacs, H.1    Campbell, I.D.2    Strong, P.3    Johnson, S.4    Ward, F.J.5    Reid, K.B.6    Eggleton, P.7
  • 38
    • 0034595799 scopus 로고    scopus 로고
    • The YXXL motif, but not the two NPXY motifs, serves as the dominant endocytosis signal for low density lipoprotein receptor-related protein
    • Li, Y., M.P. Marzolo, P. van Kerkhof, G.J. Strous, and G. Bu. 2000. The YXXL motif, but not the two NPXY motifs, serves as the dominant endocytosis signal for low density lipoprotein receptor-related protein. J. Biol. Chem. 275:17187-17194.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17187-17194
    • Li, Y.1    Marzolo, M.P.2    Van Kerkhof, P.3    Strous, G.J.4    Bu, G.5
  • 39
    • 18544378303 scopus 로고    scopus 로고
    • Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of the low density lipoprotein receptor-related protein (LRP). Evidence for integrated co-receptot function between LRP and the PDGF
    • Loukinova, E., S. Ranganathan, S. Kuznetsov, N. Gorlatova, M.M. Migliorini, D. Loukinov, P.G. Ulery, I. Mikhailenko, D.A. Lawrence, and D.K. Strickland. 2002. Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of the low density lipoprotein receptor-related protein (LRP). Evidence for integrated co-receptot function between LRP and the PDGF. J. Biol. Chem. 277:15499-15506.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15499-15506
    • Loukinova, E.1    Ranganathan, S.2    Kuznetsov, S.3    Gorlatova, N.4    Migliorini, M.M.5    Loukinov, D.6    Ulery, P.G.7    Mikhailenko, I.8    Lawrence, D.A.9    Strickland, D.K.10
  • 40
    • 0037044716 scopus 로고    scopus 로고
    • Evidence of functional modulation of the MEKK/JNK/cJun signaling cascade by the low density lipoprotein receptor-related protein (LRP)
    • Lutz, C., J. Nimpf, M. Jenny, K. Boecklinger, C. Enzinger, G. Utermann, G. Baier-Bitterlich, and G. Baier. 2002. Evidence of functional modulation of the MEKK/JNK/cJun signaling cascade by the low density lipoprotein receptor-related protein (LRP). J. Biol. Chem. 277:43143-43151.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43143-43151
    • Lutz, C.1    Nimpf, J.2    Jenny, M.3    Boecklinger, K.4    Enzinger, C.5    Utermann, G.6    Baier-Bitterlich, G.7    Baier, G.8
  • 41
    • 0028912587 scopus 로고
    • The 39-kDa receptor-associated protein modulates lipoprotein catabolism by binding to LDL receptors
    • Medh, J.D., G.L. Fry, S.L. Bowen, M.W. Pladet, D.K. Strickland, and D.A. Chappell. 1995. The 39-kDa receptor-associated protein modulates lipoprotein catabolism by binding to LDL receptors. J. Biol. Chem. 270:536-540.
    • (1995) J. Biol. Chem. , vol.270 , pp. 536-540
    • Medh, J.D.1    Fry, G.L.2    Bowen, S.L.3    Pladet, M.W.4    Strickland, D.K.5    Chappell, D.A.6
  • 42
    • 0030965616 scopus 로고    scopus 로고
    • Cellular internalization and degradation of thrombospondin-1 is mediated by the amino-terminal heparin binding domain (HBD). High affinity interaction of dimeric HBD with the low density lipoprotein receptor-related protein
    • Mikhailenko, I., D. Krylov, K.M. Argraves, D.D. Roberts, G. Liau, and D.K. Strickland. 1997. Cellular internalization and degradation of thrombospondin-1 is mediated by the amino-terminal heparin binding domain (HBD). High affinity interaction of dimeric HBD with the low density lipoprotein receptor-related protein. J. Biol. Chem. 272:6784-6791.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6784-6791
    • Mikhailenko, I.1    Krylov, D.2    Argraves, K.M.3    Roberts, D.D.4    Liau, G.5    Strickland, D.K.6
  • 43
    • 0032577684 scopus 로고    scopus 로고
    • Binding of receptor-recognized forms of alpha2-macroglobulin to the alpha2-macroglobulin signaling receptor activates phosphatidylinoskol 3-kinase
    • Misra, U.K., and S.V. Pizzo. 1998. Binding of receptor-recognized forms of alpha2-macroglobulin to the alpha2-macroglobulin signaling receptor activates phosphatidylinoskol 3-kinase. J. Biol. Chem. 273:13399-13402.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13399-13402
    • Misra, U.K.1    Pizzo, S.V.2
  • 44
    • 0033572241 scopus 로고    scopus 로고
    • Ligation of low-density lipoprotein receptor-related retain with antibodies elevates intracellular calcium and inositiol 1,45-trisphosphate in macrophages
    • Misra, U.K., G. Gawdi, and S.V. Pizzo. 1999. Ligation of low-density lipoprotein receptor-related retain with antibodies elevates intracellular calcium and inositiol 1,45-trisphosphate in macrophages. Arch. Biochem. Biophys. 372:238-247.
    • (1999) Arch. Biochem. Biophys. , vol.372 , pp. 238-247
    • Misra, U.K.1    Gawdi, G.2    Pizzo, S.V.3
  • 45
    • 0035058769 scopus 로고    scopus 로고
    • The de-adhesive activity of matricellular proteins: Is intermediate cell adhesion an adaptive state?
    • Murphy-Ullrich, J.E. 2001. The de-adhesive activity of matricellular proteins: is intermediate cell adhesion an adaptive state? J. Clin. Invest. 107:785-790.
    • (2001) J. Clin. Invest. , vol.107 , pp. 785-790
    • Murphy-Ullrich, J.E.1
  • 46
    • 0024415409 scopus 로고
    • Thrombospondin modulates focal adhesions in endothelial cells
    • Murphy-Ullrich, J.E., and M. Höök. 1989. Thrombospondin modulates focal adhesions in endothelial cells. J. Cell Biol. 109:1309-1319.
    • (1989) J. Cell Biol. , vol.109 , pp. 1309-1319
    • Murphy-Ullrich, J.E.1    Höök, M.2
  • 47
    • 0026321941 scopus 로고
    • Focal adhesion integrity is down regulated by the alternatively spliced domain of human tenascin
    • Murphy-Ullrich, J.E., V.A. Lightner, I. Aukhil, Y.Z. Yan, H.P. Erickson, and M. Höök. 1991. Focal adhesion integrity is down regulated by the alternatively spliced domain of human tenascin. J. Cell Biol. 115:1127-1136.
    • (1991) J. Cell Biol. , vol.115 , pp. 1127-1136
    • Murphy-Ullrich, J.E.1    Lightner, V.A.2    Aukhil, I.3    Yan, Y.Z.4    Erickson, H.P.5    Höök, M.6
  • 48
    • 0027377783 scopus 로고
    • Heparin-binding peptides from thrombospondins 1 and 2 contain focal adhesion-labilizing activity
    • Murphy-Ullrich, J.E., S. Gurusiddappa, W.A. Frazier, and M. Höök. 1993. Heparin-binding peptides from thrombospondins 1 and 2 contain focal adhesion-labilizing activity. J. Biol. Chem. 268:26784-26789.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26784-26789
    • Murphy-Ullrich, J.E.1    Gurusiddappa, S.2    Frazier, W.A.3    Höök, M.4
  • 49
    • 0037012039 scopus 로고    scopus 로고
    • Discrimination between phosphotyrosine-mediated signaling properties of conventional and neuronal Shc adapter molecules
    • Nakamura, T., M. Komiya, N. Gotoh, S. Koizumi, M. Shibuya, and N. Mori. 2002. Discrimination between phosphotyrosine-mediated signaling properties of conventional and neuronal Shc adapter molecules. Oncogene. 21:22-31.
    • (2002) Oncogene , vol.21 , pp. 22-31
    • Nakamura, T.1    Komiya, M.2    Gotoh, N.3    Koizumi, S.4    Shibuya, M.5    Mori, N.6
  • 50
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden, C.A., A. deCathelineau, P.R. Hoffmann, D. Bratton, B. Ghebrehiwet, V.A. Fadok, and P.M. Henson. 2001. C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J. Exp. Med. 194:781-795.
    • (2001) J. Exp. Med. , vol.194 , pp. 781-795
    • Ogden, C.A.1    DeCathelineau, A.2    Hoffmann, P.R.3    Bratton, D.4    Ghebrehiwet, B.5    Fadok, V.A.6    Henson, P.M.7
  • 51
    • 0037036434 scopus 로고    scopus 로고
    • Thrombospondin stimulates focal adhesion disassembly through Gi- and phosphoinositide 3-kinase-dependent activation
    • Orr, A.W., M.A. Palleto, and J.E. Murphy-Ullrich. 2002. Thrombospondin stimulates focal adhesion disassembly through Gi- and phosphoinositide 3-kinase-dependent activation. J. Biol. Chem. 277:20453-20460.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20453-20460
    • Orr, A.W.1    Palleto, M.A.2    Murphy-Ullrich, J.E.3
  • 52
    • 0035873090 scopus 로고    scopus 로고
    • Calreticulin, a potential cell surface receptor involved in cell penetration of anti-DNA antibodies
    • Seddiki, N., F. Nato, P. Lafaye, Z. Amoura, J.C. Piette, and J.C. Mazie. 2001. Calreticulin, a potential cell surface receptor involved in cell penetration of anti-DNA antibodies. J. Immunol. 166:6423-6429.
    • (2001) J. Immunol. , vol.166 , pp. 6423-6429
    • Seddiki, N.1    Nato, F.2    Lafaye, P.3    Amoura, Z.4    Piette, J.C.5    Mazie, J.C.6
  • 53
    • 0031689432 scopus 로고    scopus 로고
    • Interaction of C1q and the collectins with the potential receptors calreticulin (cC1qR/collectin receptor) and megalin
    • Sim, R.B., S.K. Moestrup, G.R. Stuart, N.J. Lynch, J. Lu, W.J. Schwaeble, and R. Malhotra. 1998. Interaction of C1q and the collectins with the potential receptors calreticulin (cC1qR/collectin receptor) and megalin. Immunobiology. 199:208-224.
    • (1998) Immunobiology , vol.199 , pp. 208-224
    • Sim, R.B.1    Moestrup, S.K.2    Stuart, G.R.3    Lynch, N.J.4    Lu, J.5    Schwaeble, W.J.6    Malhotra, R.7
  • 54
    • 0032513248 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 contains a cryptic high affinity binding site for the low density lipoprotein receptor-related protein
    • Stefansson, S., S. Muhammad, X.F. Cheng, F.D. Battey, D.K. Strickland, and D.A. Lawrence. 1998. Plasminogen activator inhibitor-1 contains a cryptic high affinity binding site for the low density lipoprotein receptor-related protein. J. Biol. Chem. 273:6358-6366.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6358-6366
    • Stefansson, S.1    Muhammad, S.2    Cheng, X.F.3    Battey, F.D.4    Strickland, D.K.5    Lawrence, D.A.6
  • 56
    • 0025080835 scopus 로고
    • Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor
    • Strickland, D.K., J.D. Ashcom, S. Williams, W.H. Burgess, M. Migliorini, and W.S. Argraves. 1990. Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor. J. Biol. Chem. 265:17401-17404.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17401-17404
    • Strickland, D.K.1    Ashcom, J.D.2    Williams, S.3    Burgess, W.H.4    Migliorini, M.5    Argraves, W.S.6
  • 57
    • 0025784021 scopus 로고
    • Primary structure of alpha 2-macroglobulin receptor-associated protein. Human homologue of a Heymann nephritis antigen
    • Strickland, D.K., J.D. Ashcom, S. Williams, F. Battey, E. Behre, K. McTigue, J.F. Battey, and W.S. Argraves. 1991. Primary structure of alpha 2-macroglobulin receptor-associated protein. Human homologue of a Heymann nephritis antigen. J. Biol. Chem. 266:13364-13369.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13364-13369
    • Strickland, D.K.1    Ashcom, J.D.2    Williams, S.3    Battey, F.4    Behre, E.5    McTigue, K.6    Battey, J.F.7    Argraves, W.S.8
  • 58
    • 0031459567 scopus 로고    scopus 로고
    • The C1q and collectin binding site within C1q receptor (cell surface calreticulin)
    • Stuart, G.R., N.J. Lynch, A.J. Day, W.J. Schwaeble, and R.B. Sim. 1997. The C1q and collectin binding site within C1q receptor (cell surface calreticulin). Immunopharmacology. 38:73-80.
    • (1997) Immunopharmacology , vol.38 , pp. 73-80
    • Stuart, G.R.1    Lynch, N.J.2    Day, A.J.3    Schwaeble, W.J.4    Sim, R.B.5
  • 60
    • 0032509346 scopus 로고    scopus 로고
    • Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein
    • Trommsdorff, M., J.P. Borg, B. Margolis, and J. Herz. 1998. Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J. Biol. Chem. 273:33556-33560.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33556-33560
    • Trommsdorff, M.1    Borg, J.P.2    Margolis, B.3    Herz, J.4
  • 62
    • 0030763447 scopus 로고    scopus 로고
    • Rapid elevation of neuronal cytoplasmic calcium by apolipoprotein E peptide
    • Wang, X.S., and E. Gruenstein. 1997. Rapid elevation of neuronal cytoplasmic calcium by apolipoprotein E peptide. J. Cell. Physiol. 173:73-83.
    • (1997) J. Cell. Physiol. , vol.173 , pp. 73-83
    • Wang, X.S.1    Gruenstein, E.2
  • 64
    • 0029054487 scopus 로고
    • Cell surface calreticuiin is a putative mannoside lectin which triggers mouse melanoma cell spreading
    • Whire, T.K., Q. Zhu, and M.L. Tanzer. 1995. Cell surface calreticuiin is a putative mannoside lectin which triggers mouse melanoma cell spreading. J. Biol. Chem. 270:15926-15929.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15926-15929
    • Whire, T.K.1    Zhu, Q.2    Tanzer, M.L.3
  • 65
    • 0026793036 scopus 로고
    • A novel mechanism for controlling the activity of alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein. Multiple regulatory sites for 39-kDa receptor-associated protein
    • Williams, S.E., J.D. Ashcom, W.S. Argraves, and D.K. Strickland. 1992. A novel mechanism for controlling the activity of alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein. Multiple regulatory sites for 39-kDa receptor-associated protein. J. Biol. Chem. 267:9035-9040.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9035-9040
    • Williams, S.E.1    Ashcom, J.D.2    Argraves, W.S.3    Strickland, D.K.4
  • 66
    • 0028343888 scopus 로고
    • Genetic deficiency in low density lipoprotein receptor-related protein confers cellular resistance to Pseudomonas exotoxin A. Evidence that this protein is required for uptake and degradation of multiple ligands
    • Willnow, T.E., and J. Herz. 1994. Genetic deficiency in low density lipoprotein receptor-related protein confers cellular resistance to Pseudomonas exotoxin A. Evidence that this protein is required for uptake and degradation of multiple ligands. J. Cell Sci. 107:719-726.
    • (1994) J. Cell Sci. , vol.107 , pp. 719-726
    • Willnow, T.E.1    Herz, J.2
  • 67
    • 0030022402 scopus 로고    scopus 로고
    • The low-density-lipoprotein receptor-related protein (LRP) is processed by furin in vivo and in vitro
    • Wilinow, T.E., J.M. Moehring, N.M. Inocencio, T.J. Moehring, and J. Herz. 1996. The low-density-lipoprotein receptor-related protein (LRP) is processed by furin in vivo and in vitro. Biochem. J. 313:71-76.
    • (1996) Biochem. J. , vol.313 , pp. 71-76
    • Wilinow, T.E.1    Moehring, J.M.2    Inocencio, N.M.3    Moehring, T.J.4    Herz, J.5
  • 68
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • Yamada, K.M., and B. Geiger. 1997. Molecular interactions in cell adhesion complexes. Curr. Opin. Cell Biol. 9:76-85.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2


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