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Volumn 34, Issue 3, 2014, Pages 487-498

Low-density lipoprotein receptor-related protein-1: Role in the regulation of vascular integrity

Author keywords

Aneurysm; Elastin; Extracellular matrix; fVIII; LRP1

Indexed keywords

ANEURYSM; ELASTIN; EXTRACELLULAR MATRIX; FVIII; LRP1;

EID: 84894557027     PISSN: 10795642     EISSN: 15244636     Source Type: Journal    
DOI: 10.1161/ATVBAHA.113.301924     Document Type: Review
Times cited : (85)

References (149)
  • 1
    • 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 JD, Tiller SE, Dickerson K, Cravens JL, Argraves WS, Strickland DK. 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. 1990;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
  • 2
    • 0024971241 scopus 로고
    • Purification of the rat hepatic α2-macroglobulin receptor as an approximately 440 kDa single chain polypeptide
    • Moestrup SK, Gliemann J. Purification of the rat hepatic α2-macroglobulin receptor as an approximately 440 kDa single chain polypeptide. J Biol Chem. 1989;264:15574-15577
    • (1989) J Biol Chem , vol.264 , pp. 15574-15577
    • Moestrup, S.K.1    Gliemann, J.2
  • 3
    • 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 DK, Ashcom JD, Williams S, Burgess WH, Migliorini M, Argraves WS. 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. 1990;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
  • 5
    • 0001665337 scopus 로고
    • Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor
    • Herz J, Hamann U, Rogne S, Myklebost O, Gausepohl H, Stanley KK. Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor. EMBO J. 1988;7:4119-4127
    • (1988) EMBO J. , vol.7 , pp. 4119-4127
    • Herz, J.1    Hamann, U.2    Rogne, S.3    Myklebost, O.4    Gausepohl, H.5    Stanley, K.K.6
  • 6
    • 0040177065 scopus 로고
    • Low density lipoprotein receptor-related protein mediates uptake of cholesteryl esters derived from apoprotein E-enriched lipoproteins
    • Kowal RC, Herz J, Goldstein JL, Esser V, Brown MS. Low density lipoprotein receptor-related protein mediates uptake of cholesteryl esters derived from apoprotein E-enriched lipoproteins. Proc Natl Acad Sci U S A. 1989;86:5810-5814
    • (1989) Proc Natl Acad Sci U S A. , vol.86 , pp. 5810-5814
    • Kowal, R.C.1    Herz, J.2    Goldstein, J.L.3    Esser, V.4    Brown, M.S.5
  • 7
    • 0032004972 scopus 로고    scopus 로고
    • Inducible inactivation of hepatic LRP gene by cre-mediated recombination confirms role of LRP in clearance of chylomicron remnants
    • Rohlmann A, Gotthardt M, Hammer RE, Herz J. Inducible inactivation of hepatic LRP gene by cre-mediated recombination confirms role of LRP in clearance of chylomicron remnants. J Clin Invest. 1998;101:689-695
    • (1998) J Clin Invest , vol.101 , pp. 689-695
    • Rohlmann, A.1    Gotthardt, M.2    Hammer, R.E.3    Herz, J.4
  • 8
    • 84945173643 scopus 로고    scopus 로고
    • CARDIoGRAM Consortium; Global BPgen Consortium; DIAGRAM Consortium; VRCNZ Consortium. Abdominal aortic aneurysm is associated with a variant in low-density lipoprotein receptor-related protein 1
    • Bown MJ, Jones GT, Harrison SC, et al CARDIoGRAM Consortium; Global BPgen Consortium; DIAGRAM Consortium; VRCNZ Consortium. Abdominal aortic aneurysm is associated with a variant in low-density lipoprotein receptor-related protein 1. Am J Hum Genet. 2011;89:619-627
    • (2011) Am J Hum Genet , vol.89 , pp. 619-627
    • Bown, M.J.1    Jones, G.T.2    Harrison, S.C.3
  • 9
    • 77955505564 scopus 로고    scopus 로고
    • Biological, clinical and population relevance of 95 loci for blood lipids
    • Teslovich TM, Musunuru K, Smith AV, et al. Biological, clinical and population relevance of 95 loci for blood lipids. Nature. 2010;466:707-713
    • (2010) Nature , vol.466 , pp. 707-713
    • Teslovich, T.M.1    Musunuru, K.2    Smith, A.V.3
  • 10
    • 2342591299 scopus 로고    scopus 로고
    • Large scale association analysis for identification of genes underlying premature coronary heart disease: Cumulative perspective from analysis of 111 candidate genes
    • GeneQuest Investigators
    • McCarthy JJ, Parker A, Salem R, Moliterno DJ, Wang Q, Plow EF, Rao S, Shen G, Rogers WJ, Newby LK, Cannata R, Glatt K, Topol EJ; GeneQuest Investigators. Large scale association analysis for identification of genes underlying premature coronary heart disease: Cumulative perspective from analysis of 111 candidate genes. J Med Genet. 2004;41:334-341
    • (2004) J Med Genet , vol.41 , pp. 334-341
    • McCarthy, J.J.1    Parker, A.2    Salem, R.3    Moliterno, D.J.4    Wang, Q.5    Plow, E.F.6    Rao, S.7    Shen, G.8    Rogers, W.J.9    Newby, L.K.10    Cannata, R.11    Glatt, K.12    Topol, E.J.13
  • 11
    • 0345824713 scopus 로고    scopus 로고
    • Tissue-Type plasminogen activator induces opening of the blood-brain barrier via the LDL receptor-related protein
    • Yepes M, Sandkvist M, Moore EG, Bugge TH, Strickland DK, Lawrence DA. Tissue-Type plasminogen activator induces opening of the blood-brain barrier via the LDL receptor-related protein. J Clin Invest. 2003;112:1533-1540
    • (2003) J Clin Invest , vol.112 , pp. 1533-1540
    • Yepes, M.1    Sandkvist, M.2    Moore, E.G.3    Bugge, T.H.4    Strickland, D.K.5    Lawrence, D.A.6
  • 12
    • 34147143557 scopus 로고    scopus 로고
    • Tissue-Type plasminogen activator-mediated shedding of astrocytic low-density lipoprotein receptor-related protein increases the permeability of the neurovascular unit
    • Polavarapu R, Gongora MC, Yi H, Ranganthan S, Lawrence DA, Strickland D, Yepes M. Tissue-Type plasminogen activator-mediated shedding of astrocytic low-density lipoprotein receptor-related protein increases the permeability of the neurovascular unit. Blood. 2007;109:3270-3278
    • (2007) Blood , vol.109 , pp. 3270-3278
    • Polavarapu, R.1    Gongora, M.C.2    Yi, H.3    Ranganthan, S.4    Lawrence, D.A.5    Strickland, D.6    Yepes, M.7
  • 14
    • 80052241959 scopus 로고    scopus 로고
    • Molecular basis for the interaction of the LDL receptor-related protein 1 (LRP1) with the integrin alpambeta2: Identification of binding sites within alphambeta2 for LRP1
    • Ranganathan S, Cao C, Catania J, Migliorini M, Zhang L, Strickland DK. Molecular basis for the interaction of the LDL receptor-related protein 1 (LRP1) with the integrin alpambeta2: Identification of binding sites within alphambeta2 for LRP1. J Biol Chem. 2011;286:30535-30541
    • (2011) J Biol Chem , vol.286 , pp. 30535-30541
    • Ranganathan, S.1    Cao, C.2    Catania, J.3    Migliorini, M.4    Zhang, L.5    Strickland, D.K.6
  • 16
    • 0037432766 scopus 로고    scopus 로고
    • LRP: Role in vascular wall integrity and protection from atherosclerosis
    • Boucher P, Gotthardt M, Li WP, Anderson RG, Herz J. LRP: Role in vascular wall integrity and protection from atherosclerosis. Science. 2003;300:329-332
    • (2003) Science , vol.300 , pp. 329-332
    • Boucher, P.1    Gotthardt, M.2    Li, W.P.3    Anderson, R.G.4    Herz, J.5
  • 17
    • 44149093500 scopus 로고    scopus 로고
    • LRP1 functions as an atheroprotective integrator of TGFbeta and PDFG signals in the vascular wall: Implications for Marfan syndrome
    • Boucher P, Li WP, Matz RL, Takayama Y, Auwerx J, Anderson RG, Herz J. LRP1 functions as an atheroprotective integrator of TGFbeta and PDFG signals in the vascular wall: Implications for Marfan syndrome. PLoS One. 2007;2:e448
    • (2007) PLoS One , vol.2
    • Boucher, P.1    Li, W.P.2    Matz, R.L.3    Takayama, Y.4    Auwerx, J.5    Anderson, R.G.6    Herz, J.7
  • 18
    • 73949126499 scopus 로고    scopus 로고
    • Smooth muscle LDL receptor-related protein-1 inactivation reduces vascular reactivity and promotes injury-induced neointima formation
    • Basford JE, Moore ZW, Zhou L, Herz J, Hui DY. Smooth muscle LDL receptor-related protein-1 inactivation reduces vascular reactivity and promotes injury-induced neointima formation. Arterioscler Thromb Vasc Biol. 2009;29:1772-1778
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 1772-1778
    • Basford, J.E.1    Moore, Z.W.2    Zhou, L.3    Herz, J.4    Hui, D.Y.5
  • 20
    • 33947715605 scopus 로고    scopus 로고
    • Deletion of macrophage LDL receptor-related protein increases atherogenesis in the mouse
    • Overton CD, Yancey PG, Major AS, Linton MF, Fazio S. Deletion of macrophage LDL receptor-related protein increases atherogenesis in the mouse. Circ Res. 2007;100:670-677
    • (2007) Circ Res , vol.100 , pp. 670-677
    • Overton, C.D.1    Yancey, P.G.2    Major, A.S.3    Linton, M.F.4    Fazio, S.5
  • 23
    • 0026439778 scopus 로고
    • LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation
    • Herz J, Clouthier DE, Hammer RE. LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation. Cell. 1992;71:411-421
    • (1992) Cell , vol.71 , pp. 411-421
    • Herz, J.1    Clouthier, D.E.2    Hammer, R.E.3
  • 24
    • 0027229924 scopus 로고
    • Correction: LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation
    • Herz J, Couthier DE, Hammer RE. Correction: LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation. Cell. 1993;73:428
    • (1993) Cell , vol.73 , pp. 428
    • Herz, J.1    Couthier, D.E.2    Hammer, R.E.3
  • 26
    • 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 SE, Ashcom JD, Argraves WS, Strickland DK. 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. 1992;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
  • 28
    • 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 MZ, Argraves WS, Strickland DK. 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. 1992;267:21162-21166
    • (1992) J Biol Chem , vol.267 , pp. 21162-21166
    • Kounnas, M.Z.1    Argraves, W.S.2    Strickland, D.K.3
  • 29
    • 0025786502 scopus 로고
    • 39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor
    • Herz J, Goldstein JL, Strickland DK, Ho YK, Brown MS. 39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor. J Biol Chem. 1991;266:21232-21238
    • (1991) J Biol Chem , vol.266 , pp. 21232-21238
    • Herz, J.1    Goldstein, J.L.2    Strickland, D.K.3    Ho, Y.K.4    Brown, M.S.5
  • 30
    • 0028988551 scopus 로고
    • 39 kDa receptor-Associated protein is an ER resident protein and molecular chaperone for LDL receptorrelated protein
    • Bu G, Geuze HJ, Strous GJ, Schwartz AL. 39 kDa receptor-Associated protein is an ER resident protein and molecular chaperone for LDL receptorrelated protein. EMBO J. 1995;14:2269-2280
    • (1995) EMBO J. , vol.14 , pp. 2269-2280
    • Bu, G.1    Geuze, H.J.2    Strous, G.J.3    Schwartz, A.L.4
  • 31
    • 0029887302 scopus 로고    scopus 로고
    • RAP, a specialized chaperone, prevents ligand-induced ER retention and degradation of LDL receptor-related endocytic receptors
    • Willnow TE, Rohlmann A, Horton J, Otani H, Braun JR, Hammer RE, Herz J. RAP, a specialized chaperone, prevents ligand-induced ER retention and degradation of LDL receptor-related endocytic receptors. EMBO J. 1996;15:2632-2639
    • (1996) EMBO J. , vol.15 , pp. 2632-2639
    • Willnow, T.E.1    Rohlmann, A.2    Horton, J.3    Otani, H.4    Braun, J.R.5    Hammer, R.E.6    Herz, J.7
  • 32
    • 0029079403 scopus 로고
    • Functional expression of low density lipoprotein receptor-related protein is controlled by receptorassociated protein in vivo
    • Willnow TE, Armstrong SA, Hammer RE, Herz J. Functional expression of low density lipoprotein receptor-related protein is controlled by receptorassociated protein in vivo. Proc Natl Acad Sci U S A. 1995;92:4537-4541
    • (1995) Proc Natl Acad Sci U S A. , vol.92 , pp. 4537-4541
    • Willnow, T.E.1    Armstrong, S.A.2    Hammer, R.E.3    Herz, J.4
  • 34
    • 34547173322 scopus 로고    scopus 로고
    • Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptors
    • Yasui N, Nogi T, Kitao T, Nakano Y, Hattori M, Takagi J. Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptors. Proc Natl Acad Sci U S A. 2007;104:9988-9993
    • (2007) Proc Natl Acad Sci U S A. , vol.104 , pp. 9988-9993
    • Yasui, N.1    Nogi, T.2    Kitao, T.3    Nakano, Y.4    Hattori, M.5    Takagi, J.6
  • 35
    • 2342648870 scopus 로고    scopus 로고
    • X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein
    • Verdaguer N, Fita I, Reithmayer M, Moser R, Blaas D. X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein. Nat Struct Mol Biol. 2004;11:429-434
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 429-434
    • Verdaguer, N.1    Fita, I.2    Reithmayer, M.3    Moser, R.4    Blaas, D.5
  • 37
    • 33646046808 scopus 로고    scopus 로고
    • Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors
    • Fisher C, Beglova N, Blacklow SC. Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors. Mol Cell. 2006;22:277-283
    • (2006) Mol Cell , vol.22 , pp. 277-283
    • Fisher, C.1    Beglova, N.2    Blacklow, S.C.3
  • 38
    • 77649092080 scopus 로고    scopus 로고
    • Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids
    • Lee CJ, De Biasio A, Beglova N. Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids. Structure. 2010;18:366-376
    • (2010) Structure , vol.18 , pp. 366-376
    • Lee, C.J.1    De Biasio, A.2    Beglova, N.3
  • 40
    • 84873671045 scopus 로고    scopus 로고
    • Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: Insight from the nmr structure of the 10th complement type repeat domain alone and in complex with gentamicin
    • Dagil R, O'Shea C, Nykjær A, Bonvin AM, Kragelund BB. Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: Insight from the nmr structure of the 10th complement type repeat domain alone and in complex with gentamicin. J Biol Chem. 2013;288:4424-4435
    • (2013) J Biol Chem , vol.288 , pp. 4424-4435
    • Dagil, R.1    O'Shea, C.2    Nykjær, A.3    Bonvin, A.M.4    Kragelund, B.B.5
  • 41
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L, Chothia C, Janin J. The atomic structure of protein-protein recognition sites. J Mol Biol. 1999;285:2177-2198
    • (1999) J Mol Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 42
    • 0032696798 scopus 로고    scopus 로고
    • Regulation of factor VIII expression and activity by von Willebrand factor
    • Kaufman RJ, Pipe SW. Regulation of factor VIII expression and activity by von Willebrand factor. Thromb Haemost. 1999;82:201-208
    • (1999) Thromb Haemost , vol.82 , pp. 201-208
    • Kaufman, R.J.1    Pipe, S.W.2
  • 43
    • 33646839132 scopus 로고    scopus 로고
    • Factor VIII structure and function
    • Fay PJ. Factor VIII structure and function. Int J Hematol. 2006;83:103-108
    • (2006) Int J Hematol , vol.83 , pp. 103-108
    • Fay, P.J.1
  • 45
    • 38049160762 scopus 로고    scopus 로고
    • The factor VIII C1 domain contributes to platelet binding
    • Hsu TC, Pratt KP, Thompson AR. The factor VIII C1 domain contributes to platelet binding. Blood. 2008;111:200-208
    • (2008) Blood , vol.111 , pp. 200-208
    • Hsu, T.C.1    Pratt, K.P.2    Thompson, A.R.3
  • 46
    • 0023151843 scopus 로고
    • Formation and functioning of the factor IXa-VIII complex on the surface of endothelial cells
    • Váradi K, Elödi S. Formation and functioning of the factor IXa-VIII complex on the surface of endothelial cells. Blood. 1987;69:442-445
    • (1987) Blood , vol.69 , pp. 442-445
    • Váradi, K.1    Elödi, S.2
  • 47
    • 0025745241 scopus 로고
    • Functional difference between intrinsic and extrinsic coagulation pathways. Kinetics of factor X activation on human monocytes and alveolar macrophages
    • McGee MP, Li LC. Functional difference between intrinsic and extrinsic coagulation pathways. Kinetics of factor X activation on human monocytes and alveolar macrophages. J Biol Chem. 1991;266:8079-8085
    • (1991) J Biol Chem , vol.266 , pp. 8079-8085
    • McGee, M.P.1    Li, L.C.2
  • 48
    • 0026447620 scopus 로고
    • Diffusion control in blood coagulation. Activation of factor X by factors IXa/VIIIa assembled on human monocyte membranes
    • McGee MP, Li LC, Xiong H. Diffusion control in blood coagulation. Activation of factor X by factors IXa/VIIIa assembled on human monocyte membranes. J Biol Chem. 1992;267:24333-24339
    • (1992) J Biol Chem , vol.267 , pp. 24333-24339
    • McGee, M.P.1    Li, L.C.2    Xiong, H.3
  • 49
    • 0033621486 scopus 로고    scopus 로고
    • Role of the low density lipoprotein-related protein receptor in mediation of factor VIII catabolism
    • Saenko EL, Yakhyaev AV, Mikhailenko I, Strickland DK, Sarafanov AG. Role of the low density lipoprotein-related protein receptor in mediation of factor VIII catabolism. J Biol Chem. 1999;274:37685-37692
    • (1999) J Biol Chem , vol.274 , pp. 37685-37692
    • Saenko, E.L.1    Yakhyaev, A.V.2    Mikhailenko, I.3    Strickland, D.K.4    Sarafanov, A.G.5
  • 51
    • 0035853843 scopus 로고    scopus 로고
    • Cell surface heparan sulfate proteoglycans participate in factor VIII catabolism mediated by low density lipoprotein receptor-related protein
    • Sarafanov AG, Ananyeva NM, Shima M, Saenko EL. Cell surface heparan sulfate proteoglycans participate in factor VIII catabolism mediated by low density lipoprotein receptor-related protein. J Biol Chem. 2001;276:11970-11979
    • (2001) J Biol Chem , vol.276 , pp. 11970-11979
    • Sarafanov, A.G.1    Ananyeva, N.M.2    Shima, M.3    Saenko, E.L.4
  • 53
    • 23044478501 scopus 로고    scopus 로고
    • LDL receptor cooperates with LDL receptor-related protein in regulating plasma levels of coagulation factor VIII in vivo
    • Bovenschen N, Mertens K, Hu L, Havekes LM, van Vlijmen BJ. LDL receptor cooperates with LDL receptor-related protein in regulating plasma levels of coagulation factor VIII in vivo. Blood. 2005;106:906-912
    • (2005) Blood , vol.106 , pp. 906-912
    • Bovenschen, N.1    Mertens, K.2    Hu, L.3    Havekes, L.M.4    Van Vlijmen, B.J.5
  • 54
    • 0034161385 scopus 로고    scopus 로고
    • Involvement of low-density lipoprotein receptor-related protein (LRP) in the clearance of factor VIII in von Willebrand factor-deficient mice
    • Schwarz HP, Lenting PJ, Binder B, Mihaly J, Denis C, Dorner F, Turecek PL. Involvement of low-density lipoprotein receptor-related protein (LRP) in the clearance of factor VIII in von Willebrand factor-deficient mice. Blood. 2000;95:1703-1708
    • (2000) Blood , vol.95 , pp. 1703-1708
    • Schwarz, H.P.1    Lenting, P.J.2    Binder, B.3    Mihaly, J.4    Denis, C.5    Dorner, F.6    Turecek, P.L.7
  • 55
    • 0017754787 scopus 로고
    • Stabilization of factor VIII in plasma by the von Willebrand factor. Studies on posttransfusion and dissociated factor VIII and in patients with von Willebrand's disease
    • Weiss HJ, Sussman II, Hoyer LW. Stabilization of factor VIII in plasma by the von Willebrand factor. Studies on posttransfusion and dissociated factor VIII and in patients with von Willebrand's disease. J Clin Invest. 1977;60:390-404
    • (1977) J Clin Invest , vol.60 , pp. 390-404
    • Weiss, H.J.1    Sussman, I.I.2    Hoyer, L.W.3
  • 57
    • 33846007667 scopus 로고    scopus 로고
    • Atherogenic remnant lipoproteins: Role for proteoglycans in trapping, transferring, and internalizing
    • Mahley RW, Huang Y. Atherogenic remnant lipoproteins: Role for proteoglycans in trapping, transferring, and internalizing. J Clin Invest. 2007;117:94-98
    • (2007) J Clin Invest , vol.117 , pp. 94-98
    • Mahley, R.W.1    Huang, Y.2
  • 58
    • 33745281224 scopus 로고    scopus 로고
    • Proteolytic cleavage of factor VIII heavy chain is required to expose the binding-site for low-density lipoprotein receptor-related protein within the A2 domain
    • Bovenschen N, van Stempvoort G, Voorberg J, Mertens K, Meijer AB. Proteolytic cleavage of factor VIII heavy chain is required to expose the binding-site for low-density lipoprotein receptor-related protein within the A2 domain. J Thromb Haemost. 2006;4:1487-1493
    • (2006) J Thromb Haemost , vol.4 , pp. 1487-1493
    • Bovenschen, N.1    Van Stempvoort, G.2    Voorberg, J.3    Mertens, K.4    Meijer, A.B.5
  • 59
    • 33745284559 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein (LRP)-mediated clearance of activated blood coagulation co-factors and proteases clearance mechanism or regulation?
    • Strickland DK, Medved L. Low-density lipoprotein receptor-related protein (LRP)-mediated clearance of activated blood coagulation co-factors and proteases: Clearance mechanism or regulation? J Thromb Haemost. 2006;4:1484-1486
    • (2006) J Thromb Haemost , vol.4 , pp. 1484-1486
    • Strickland, D.K.1    Medved, L.2
  • 61
    • 1842530336 scopus 로고    scopus 로고
    • An experimental model to study the in vivo survival of von Willebrand factor. Basic aspects and application to the R1205H mutation
    • Lenting PJ, Westein E, Terraube V, Ribba AS, Huizinga EG, Meyer D, de Groot PG, Denis CV. An experimental model to study the in vivo survival of von Willebrand factor. Basic aspects and application to the R1205H mutation. J Biol Chem. 2004;279:12102-12109
    • (2004) J Biol Chem , vol.279 , pp. 12102-12109
    • Lenting, P.J.1    Westein, E.2    Terraube, V.3    Ribba, A.S.4    Huizinga, E.G.5    Meyer, D.6    De Groot, P.G.7    Denis, C.V.8
  • 66
    • 0036271051 scopus 로고    scopus 로고
    • Orchestration of coagulation protease signaling by tissue factor
    • Riewald M, Ruf W. Orchestration of coagulation protease signaling by tissue factor. Trends Cardiovasc Med. 2002;12:149-154
    • (2002) Trends Cardiovasc Med , vol.12 , pp. 149-154
    • Riewald, M.1    Ruf, W.2
  • 68
    • 0028355715 scopus 로고
    • The low density lipoprotein receptor-related protein mediates the cellular degradation of tissue factor pathway inhibitor
    • Warshawsky I, Broze GJ Jr, Schwartz AL. The low density lipoprotein receptor-related protein mediates the cellular degradation of tissue factor pathway inhibitor. Proc Natl Acad Sci U S A. 1994;91:6664-6668
    • (1994) Proc Natl Acad Sci U S A. , vol.91 , pp. 6664-6668
    • Warshawsky, I.1    Broze Jr., G.J.2    Schwartz, A.L.3
  • 69
    • 0033582516 scopus 로고    scopus 로고
    • Down-regulation of monocyte tissue factor mediated by tissue factor pathway inhibitor and the low density lipoprotein receptor-related protein
    • Hamik A, Setiadi H, Bu G, McEver RP, Morrissey JH. Down-regulation of monocyte tissue factor mediated by tissue factor pathway inhibitor and the low density lipoprotein receptor-related protein. J Biol Chem. 1999;274:4962-4969
    • (1999) J Biol Chem , vol.274 , pp. 4962-4969
    • Hamik, A.1    Setiadi, H.2    Bu, G.3    McEver, R.P.4    Morrissey, J.H.5
  • 70
    • 0028944244 scopus 로고
    • The urokinase-Type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae
    • Stahl A, Mueller BM. The urokinase-Type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae. J Cell Biol. 1995;129:335-344
    • (1995) J Cell Biol , vol.129 , pp. 335-344
    • Stahl, A.1    Mueller, B.M.2
  • 71
    • 0029294650 scopus 로고
    • The structure and function of the urokinase receptor, a membrane protein governing plasminogen activation on the cell surface
    • Behrendt N, Rønne E, Danø K. The structure and function of the urokinase receptor, a membrane protein governing plasminogen activation on the cell surface. Biol Chem Hoppe Seyler. 1995;376:269-279
    • (1995) Biol Chem Hoppe Seyler , vol.376 , pp. 269-279
    • Behrendt, N.1    Rønne, E.2    Danø, K.3
  • 72
    • 0027550662 scopus 로고
    • Urokinase and urokinase receptor: A paracrine/autocrine system regulating cell migration and invasiveness
    • Blasi F. Urokinase and urokinase receptor: A paracrine/autocrine system regulating cell migration and invasiveness. Bioessays. 1993;15:105-111
    • (1993) Bioessays , vol.15 , pp. 105-111
    • Blasi, F.1
  • 73
    • 80051682259 scopus 로고    scopus 로고
    • Regulation of the urokinase receptor (uPAR) by LDL receptor-related protein-1 (LRP1
    • Gonias SL, Gaultier A, Jo M. Regulation of the urokinase receptor (uPAR) by LDL receptor-related protein-1 (LRP1). Curr Pharm Des. 2011;17:1962-1969
    • (2011) Curr Pharm Des , vol.17 , pp. 1962-1969
    • Gonias, S.L.1    Gaultier, A.2    Jo, M.3
  • 74
    • 84890389234 scopus 로고    scopus 로고
    • LDL receptor-related protein-1: A regulator of inflammation in atherosclerosis, cancer, and injury to the nervous system
    • October 12 doi: 10.1016/j.ajpath.2013.08.029. Accessed December 3 2013
    • Gonias SL, Campana WM. LDL receptor-related protein-1: A regulator of inflammation in atherosclerosis, cancer, and injury to the nervous system. Am J Pathol. October 12, 2013. doi: 10.1016/j.ajpath.2013.08.029. http://ajp.amjpathol.org/article/S0002-9440%2813%2900652-4/abstract. Accessed December 3, 2013
    • (2013) Am J Pathol
    • Gonias, S.L.1    Campana, W.M.2
  • 76
    • 58749110564 scopus 로고    scopus 로고
    • Gamma-secretase limits the inflammatory response through the processing of LRP1
    • 1:ra15
    • Zurhove K, Nakajima C, Herz J, Bock HH, May P. Gamma-secretase limits the inflammatory response through the processing of LRP1. Sci Signal. 2008;1:ra15
    • (2008) Sci Signal
    • Zurhove, K.1    Nakajima, C.2    Herz, J.3    Bock, H.H.4    May, P.5
  • 78
    • 77952002497 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein 1 (LRP1) forms a signaling complex with platelet-derived growth factor receptor-beta in endosomes and regulates activation of the MAPK pathway
    • Muratoglu SC, Mikhailenko I, Newton C, Migliorini M, Strickland DK. Low density lipoprotein receptor-related protein 1 (LRP1) forms a signaling complex with platelet-derived growth factor receptor-beta in endosomes and regulates activation of the MAPK pathway. J Biol Chem. 2010;285:14308-14317
    • (2010) J Biol Chem , vol.285 , pp. 14308-14317
    • Muratoglu, S.C.1    Mikhailenko, I.2    Newton, C.3    Migliorini, M.4    Strickland, D.K.5
  • 79
    • 84894539731 scopus 로고    scopus 로고
    • PDGF mediates tyrosine phosphorylation of the cytoplasmic domain of the LDL receptor-related protein (LRP) in caveolae
    • Boucher P, Liu P, Gotthardt M, Hiesberger T, Anderson RGW, Herz J. PDGF mediates tyrosine phosphorylation of the cytoplasmic domain of the LDL receptor-related protein (LRP) in caveolae. J Biol Chem. 2002;M200428200
    • (2002) J Biol Chem
    • Boucher, P.1    Liu, P.2    Gotthardt, M.3    Hiesberger, T.4    Anderson, R.G.W.5    Herz, J.6
  • 80
    • 23044455604 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein 1 (LRP1) controls endocytosis and c-CBL-mediated ubiquitination of the platelet-derived growth factor receptor beta (PDGFR beta
    • Takayama Y, May P, Anderson RG, Herz J. Low density lipoprotein receptor-related protein 1 (LRP1) controls endocytosis and c-CBL-mediated ubiquitination of the platelet-derived growth factor receptor beta (PDGFR beta). J Biol Chem. 2005;280:18504-18510
    • (2005) J Biol Chem , vol.280 , pp. 18504-18510
    • Takayama, Y.1    May, P.2    Anderson, R.G.3    Herz, J.4
  • 82
    • 0035798710 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein/alpha2-macroglobulin receptor is a receptor for connective tissue growth factor
    • Segarini PR, Nesbitt JE, Li D, Hays LG, Yates JR 3rd, Carmichael DF. The low density lipoprotein receptor-related protein/alpha2-macroglobulin receptor is a receptor for connective tissue growth factor. J Biol Chem. 2001;276:40659-40667
    • (2001) J Biol Chem , vol.276 , pp. 40659-40667
    • Segarini, P.R.1    Nesbitt, J.E.2    Li, D.3    Hays, L.G.4    Yates III, J.R.5    Carmichael, D.F.6
  • 84
    • 10044274113 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the LDL receptor-related protein (LRP) and activation of the ERK pathway are required for connective tissue growth factor to potentiate myofibroblast differentiation
    • Yang M, Huang H, Li J, Li D, Wang H. Tyrosine phosphorylation of the LDL receptor-related protein (LRP) and activation of the ERK pathway are required for connective tissue growth factor to potentiate myofibroblast differentiation. FASEB J. 2004;18:1920-1921
    • (2004) FASEB J. , vol.18 , pp. 1920-1921
    • Yang, M.1    Huang, H.2    Li, J.3    Li, D.4    Wang, H.5
  • 85
    • 84868601059 scopus 로고    scopus 로고
    • LRP1 mediates Hedgehog-induced endocytosis of the GPC3-Hedgehog complex
    • Capurro MI, Shi W, Filmus J. LRP1 mediates Hedgehog-induced endocytosis of the GPC3-Hedgehog complex. J Cell Sci. 2012;125(Pt 14):3380-3389
    • (2012) J Cell Sci , vol.125 , Issue.PART 14 , pp. 3380-3389
    • Capurro, M.I.1    Shi, W.2    Filmus, J.3
  • 87
    • 37249028744 scopus 로고    scopus 로고
    • Midkine and LDL-receptor-related protein 1 contribute to the anchorage-independent cell growth of cancer cells
    • Chen S, Bu G, Takei Y, Sakamoto K, Ikematsu S, Muramatsu T, Kadomatsu K. Midkine and LDL-receptor-related protein 1 contribute to the anchorage-independent cell growth of cancer cells. J Cell Sci. 2007;120(Pt 22):4009-4015
    • (2007) J Cell Sci , vol.120 , Issue.PART 22 , pp. 4009-4015
    • Chen, S.1    Bu, G.2    Takei, Y.3    Sakamoto, K.4    Ikematsu, S.5    Muramatsu, T.6    Kadomatsu, K.7
  • 88
    • 84862917877 scopus 로고    scopus 로고
    • Midkine prevented hypoxic injury of mouse embryonic stem cells through activation of Akt and HIF-1α via low-density lipoprotein receptor-related protein-1
    • Lee SH, Suh HN, Lee YJ, Seo BN, Ha JW, Han HJ. Midkine prevented hypoxic injury of mouse embryonic stem cells through activation of Akt and HIF-1α via low-density lipoprotein receptor-related protein-1. J Cell Physiol. 2012;227:1731-1739
    • (2012) J Cell Physiol , vol.227 , pp. 1731-1739
    • Lee, S.H.1    Suh, H.N.2    Lee, Y.J.3    Seo, B.N.4    Ha, J.W.5    Han, H.J.6
  • 89
    • 79851497711 scopus 로고    scopus 로고
    • Lipoprotein receptor LRP1 regulates leptin signaling and energy homeostasis in the adult central nervous system
    • Liu Q, Zhang J, Zerbinatti C, Zhan Y, Kolber BJ, Herz J, Muglia LJ, Bu G. Lipoprotein receptor LRP1 regulates leptin signaling and energy homeostasis in the adult central nervous system. PLoS Biol. 2011;9:e1000575
    • (2011) PLoS Biol , vol.9
    • Liu, Q.1    Zhang, J.2    Zerbinatti, C.3    Zhan, Y.4    Kolber, B.J.5    Herz, J.6    Muglia, L.J.7    Bu, G.8
  • 92
    • 0028921870 scopus 로고
    • Low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor mediates the cellular internalization and degradation of thrombospondin. A process facilitated by cell-surface proteoglycans
    • Mikhailenko I, Kounnas MZ, Strickland DK. Low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor mediates the cellular internalization and degradation of thrombospondin. A process facilitated by cell-surface proteoglycans. J Biol Chem. 1995;270:9543-9549
    • (1995) J Biol Chem , vol.270 , pp. 9543-9549
    • Mikhailenko, I.1    Kounnas, M.Z.2    Strickland, D.K.3
  • 93
    • 0029868041 scopus 로고    scopus 로고
    • Cellular internalization and degradation of antithrombin III-Thrombin, heparin cofactor II-Thrombin, and alpha 1-Antitrypsin-Trypsin complexes is mediated by the low density lipoprotein receptor-related protein
    • Kounnas MZ, Church FC, Argraves WS, Strickland DK. Cellular internalization and degradation of antithrombin III-Thrombin, heparin cofactor II-Thrombin, and alpha 1-Antitrypsin-Trypsin complexes is mediated by the low density lipoprotein receptor-related protein. J Biol Chem. 1996;271:6523-6529
    • (1996) J Biol Chem , vol.271 , pp. 6523-6529
    • Kounnas, M.Z.1    Church, F.C.2    Argraves, W.S.3    Strickland, D.K.4
  • 94
    • 70349327570 scopus 로고    scopus 로고
    • Ligand binding to LRP1 transactivates Trk receptors by a Src family kinase-dependent pathway
    • 2:ra18
    • Shi Y, Mantuano E, Inoue G, Campana WM, Gonias SL. Ligand binding to LRP1 transactivates Trk receptors by a Src family kinase-dependent pathway. Sci Signal. 2009;2:ra18
    • (2009) Sci Signal
    • Shi, Y.1    Mantuano, E.2    Inoue, G.3    Campana, W.M.4    Gonias, S.L.5
  • 95
    • 0025302165 scopus 로고
    • Opposing Effects of Apolipoproteins E and C on Lipoprotein Binding to LDL receptor Related Protein
    • Kowal RC, Herz J, Weisgraber KH, Mahley RW, Brown MS, Goldstein JL. Opposing Effects of Apolipoproteins E and C on Lipoprotein Binding to LDL receptor Related Protein. J Biol Chem. 1990;265:10771-10779
    • (1990) J Biol Chem , vol.265 , pp. 10771-10779
    • Kowal, R.C.1    Herz, J.2    Weisgraber, K.H.3    Mahley, R.W.4    Brown, M.S.5    Goldstein, J.L.6
  • 96
    • 0024449363 scopus 로고
    • The LDL-receptorrelated protein, LRP, is an apolipoprotein E-binding protein
    • Beisiegel U, Weber W, Ihrke G, Herz J, Stanley KK. The LDL-receptorrelated protein, LRP, is an apolipoprotein E-binding protein. Nature. 1989;341:162-164
    • (1989) Nature , vol.341 , pp. 162-164
    • Beisiegel, U.1    Weber, W.2    Ihrke, G.3    Herz, J.4    Stanley, K.K.5
  • 98
    • 33847240080 scopus 로고    scopus 로고
    • Apolipoprotein E-containing lipoproteins protect neurons from apoptosis via a signaling pathway involving low-density lipoprotein receptor-related protein-1
    • Hayashi H, Campenot RB, Vance DE, Vance JE. Apolipoprotein E-containing lipoproteins protect neurons from apoptosis via a signaling pathway involving low-density lipoprotein receptor-related protein-1. J Neurosci. 2007;27:1933-1941
    • (2007) J Neurosci , vol.27 , pp. 1933-1941
    • Hayashi, H.1    Campenot, R.B.2    Vance, D.E.3    Vance, J.E.4
  • 99
    • 0026756089 scopus 로고
    • Low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor is an hepatic receptor for tissue-Type plasminogen activator
    • Bu G, Williams S, Strickland DK, Schwartz AL. Low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor is an hepatic receptor for tissue-Type plasminogen activator. Proc Natl Acad Sci U S A. 1992;89:7427-7431
    • (1992) Proc Natl Acad Sci U S A. , vol.89 , pp. 7427-7431
    • Bu, G.1    Williams, S.2    Strickland, D.K.3    Schwartz, A.L.4
  • 100
    • 59649103200 scopus 로고    scopus 로고
    • The low-density lipoprotein receptor-related protein 1 mediates tissue-Type plasminogen activatorinduced microglial activation in the ischemic brain
    • Zhang C, An J, Strickland DK, Yepes M. The low-density lipoprotein receptor-related protein 1 mediates tissue-Type plasminogen activatorinduced microglial activation in the ischemic brain. Am J Pathol. 2009;174:586-594
    • (2009) Am J Pathol , vol.174 , pp. 586-594
    • Zhang, C.1    An, J.2    Strickland, D.K.3    Yepes, M.4
  • 101
    • 33644869414 scopus 로고    scopus 로고
    • Tissue-Type plasminogen activator acts as a cytokine that triggers intracellular signal transduction and induces matrix metalloproteinase-9 gene expression
    • Hu K, Yang J, Tanaka S, Gonias SL, Mars WM, Liu Y. Tissue-Type plasminogen activator acts as a cytokine that triggers intracellular signal transduction and induces matrix metalloproteinase-9 gene expression. J Biol Chem. 2006;281:2120-2127
    • (2006) J Biol Chem , vol.281 , pp. 2120-2127
    • Hu, K.1    Yang, J.2    Tanaka, S.3    Gonias, S.L.4    Mars, W.M.5    Liu, Y.6
  • 102
    • 84888376836 scopus 로고    scopus 로고
    • LRP1 assembles unique co-receptor systems to initiate cell-signaling in response to tissue-Type plasminogen activator and myelin-Associated glycoprotein
    • Mantuano E, Lam MS, Gonias SL. LRP1 assembles unique co-receptor systems to initiate cell-signaling in response to tissue-Type plasminogen activator and myelin-Associated glycoprotein. J Biol Chem. 2013;288:34009-34018
    • (2013) J Biol Chem , vol.288 , pp. 34009-34018
    • Mantuano, E.1    Lam, M.S.2    Gonias, S.L.3
  • 103
    • 84875616437 scopus 로고    scopus 로고
    • LDL receptor-related protein-1 is a sialic-Acid-independent receptor for myelin-Associated glycoprotein that functions in neurite outgrowth inhibition by MAG and CNS myelin
    • Stiles TL, Dickendesher TL, Gaultier A, Fernandez-Castaneda A, Mantuano E, Giger RJ, Gonias SL. LDL receptor-related protein-1 is a sialic-Acid- independent receptor for myelin-Associated glycoprotein that functions in neurite outgrowth inhibition by MAG and CNS myelin. J Cell Sci. 2013;126(Pt 1):209-220
    • (2013) J Cell Sci , vol.126 , Issue.PART 1 , pp. 209-220
    • Stiles, T.L.1    Dickendesher, T.L.2    Gaultier, A.3    Fernandez-Castaneda, A.4    Mantuano, E.5    Giger, R.J.6    Gonias, S.L.7
  • 104
    • 36549071997 scopus 로고    scopus 로고
    • Mutations in smooth muscle alpha-Actin (ACTA2) lead to thoracic aortic aneurysms and dissections
    • Guo DC, Pannu H, Tran-Fadulu V, et al. Mutations in smooth muscle alpha-Actin (ACTA2) lead to thoracic aortic aneurysms and dissections. Nat Genet. 2007;39:1488-1493
    • (2007) Nat Genet , vol.39 , pp. 1488-1493
    • Guo, D.C.1    Pannu, H.2    Tran-Fadulu, V.3
  • 105
    • 65149088429 scopus 로고    scopus 로고
    • Mutations in smooth muscle alpha-Actin (ACTA2) cause coronary artery disease, stroke, and Moyamoya disease, along with thoracic aortic disease
    • Guo DC, Papke CL, Tran-Fadulu V, et al. Mutations in smooth muscle alpha-Actin (ACTA2) cause coronary artery disease, stroke, and Moyamoya disease, along with thoracic aortic disease. Am J Hum Genet. 2009;84:617-627
    • (2009) Am J Hum Genet , vol.84 , pp. 617-627
    • Guo, D.C.1    Papke, C.L.2    Tran-Fadulu, V.3
  • 106
    • 84880795141 scopus 로고    scopus 로고
    • Genetics of thoracic aortic aneurysm: At the crossroad of transforming growth factor-β signaling and vascular smooth muscle cell contractility
    • Gillis E, Van Laer L, Loeys BL. Genetics of thoracic aortic aneurysm: At the crossroad of transforming growth factor-β signaling and vascular smooth muscle cell contractility. Circ Res. 2013;113:327-340
    • (2013) Circ Res , vol.113 , pp. 327-340
    • Gillis, E.1    Van Laer, L.2    Loeys, B.L.3
  • 107
    • 33646367900 scopus 로고    scopus 로고
    • Regulation of the composition of the extracellular matrix by low density lipoprotein receptor-related protein-1: Activities based on regulation of mRNA expression
    • Gaultier A, Salicioni AM, Arandjelovic S, Gonias SL. Regulation of the composition of the extracellular matrix by low density lipoprotein receptor-related protein-1: Activities based on regulation of mRNA expression. J Biol Chem. 2006;281:7332-7340
    • (2006) J Biol Chem , vol.281 , pp. 7332-7340
    • Gaultier, A.1    Salicioni, A.M.2    Arandjelovic, S.3    Gonias, S.L.4
  • 109
    • 1642385055 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein-1 promotes beta1 integrin maturation and transport to the cell surface
    • Salicioni AM, Gaultier A, Brownlee C, Cheezum MK, Gonias SL. Low density lipoprotein receptor-related protein-1 promotes beta1 integrin maturation and transport to the cell surface. J Biol Chem. 2004;279:10005-10012
    • (2004) J Biol Chem , vol.279 , pp. 10005-10012
    • Salicioni, A.M.1    Gaultier, A.2    Brownlee, C.3    Cheezum, M.K.4    Gonias, S.L.5
  • 110
    • 36849007621 scopus 로고    scopus 로고
    • Tissue-Type plasminogen activator promotes murine myofibroblast activation through LDL receptor-related protein 1-mediated integrin signaling
    • Hu K, Wu C, Mars WM, Liu Y. Tissue-Type plasminogen activator promotes murine myofibroblast activation through LDL receptor-related protein 1-mediated integrin signaling. J Clin Invest. 2007;117:3821-3832
    • (2007) J Clin Invest , vol.117 , pp. 3821-3832
    • Hu, K.1    Wu, C.2    Mars, W.M.3    Liu, Y.4
  • 111
    • 0026379091 scopus 로고
    • Elastin synthesis and fiber assembly
    • Mecham RP. Elastin synthesis and fiber assembly. Ann N Y Acad Sci. 1991;624:137-146
    • (1991) Ann N Y Acad Sci , vol.624 , pp. 137-146
    • Mecham, R.P.1
  • 112
    • 67650875881 scopus 로고    scopus 로고
    • Vascular extracellular matrix and arterial mechanics
    • Wagenseil JE, Mecham RP. Vascular extracellular matrix and arterial mechanics. Physiol Rev. 2009;89:957-989
    • (2009) Physiol Rev , vol.89 , pp. 957-989
    • Wagenseil, J.E.1    Mecham, R.P.2
  • 113
    • 79956330132 scopus 로고    scopus 로고
    • Lessons on the pathogenesis of aneurysm from heritable conditions
    • Lindsay ME, Dietz HC. Lessons on the pathogenesis of aneurysm from heritable conditions. Nature. 2011;473:308-316
    • (2011) Nature , vol.473 , pp. 308-316
    • Lindsay, M.E.1    Dietz, H.C.2
  • 114
    • 70349093134 scopus 로고    scopus 로고
    • LRP1 regulates architecture of the vascular wall by controlling PDGFRbeta-dependent phosphatidylinositol 3-kinase activation
    • Zhou L, Takayama Y, Boucher P, Tallquist MD, Herz J. LRP1 regulates architecture of the vascular wall by controlling PDGFRbeta-dependent phosphatidylinositol 3-kinase activation. PLoS One. 2009;4:e6922
    • (2009) PLoS One , vol.4
    • Zhou, L.1    Takayama, Y.2    Boucher, P.3    Tallquist, M.D.4    Herz, J.5
  • 115
    • 79960983554 scopus 로고    scopus 로고
    • Overexpression of HTRA1 leads to ultrastructural changes in the elastic layer of Bruch's membrane via cleavage of extracellular matrix components
    • Vierkotten S, Muether PS, Fauser S. Overexpression of HTRA1 leads to ultrastructural changes in the elastic layer of Bruch's membrane via cleavage of extracellular matrix components. PLoS One. 2011;6:e22959
    • (2011) PLoS One , vol.6
    • Vierkotten, S.1    Muether, P.S.2    Fauser, S.3
  • 116
    • 59449107340 scopus 로고    scopus 로고
    • Membrane-Type 1 matrix metalloproteinase regulates macrophagedependent elastolytic activity and aneurysm formation in vivo
    • Xiong W, Knispel R, MacTaggart J, Greiner TC, Weiss SJ, Baxter BT. Membrane-Type 1 matrix metalloproteinase regulates macrophagedependent elastolytic activity and aneurysm formation in vivo. J Biol Chem. 2009;284:1765-1771
    • (2009) J Biol Chem , vol.284 , pp. 1765-1771
    • Xiong, W.1    Knispel, R.2    MacTaggart, J.3    Greiner, T.C.4    Weiss, S.J.5    Baxter, B.T.6
  • 118
    • 70849136597 scopus 로고    scopus 로고
    • Connective tissue growth factor-(CTGF, CCN2)-A marker, mediator and therapeutic target for renal fibrosis
    • Phanish MK, Winn SK, Dockrell ME. Connective tissue growth factor-(CTGF, CCN2)-A marker, mediator and therapeutic target for renal fibrosis. Nephron Exp Nephrol. 2010;114:e83-e92
    • (2010) Nephron Exp Nephrol , vol.114
    • Phanish, M.K.1    Winn, S.K.2    Dockrell, M.E.3
  • 119
    • 84886730249 scopus 로고    scopus 로고
    • A pilot study on low-density lipoprotein receptor-related protein-1 in chinese patients with abdominal aortic aneurysm
    • Chan CY, Chan YC, Cheuk BL, Cheng SW. A Pilot Study on Low-density Lipoprotein Receptor-related Protein-1 in Chinese Patients with Abdominal Aortic Aneurysm. Eur J Vasc Endovasc Surg. 2013;46:549-556
    • (2013) Eur J Vasc Endovasc Surg , vol.46 , pp. 549-556
    • Chan, C.Y.1    Chan, Y.C.2    Cheuk, B.L.3    Cheng, S.W.4
  • 120
    • 0023069717 scopus 로고
    • Platelet-derived growth factor
    • Ross R. Platelet-derived growth factor. Annu Rev Med. 1987;38:71-79
    • (1987) Annu Rev Med , vol.38 , pp. 71-79
    • Ross, R.1
  • 121
    • 0026418308 scopus 로고
    • Inhibition of neointimal smooth muscle accumulation after angioplasty by an antibody to PDGF
    • Ferns GA, Raines EW, Sprugel KH, Motani AS, Reidy MA, Ross R. Inhibition of neointimal smooth muscle accumulation after angioplasty by an antibody to PDGF. Science. 1991;253:1129-1132
    • (1991) Science , vol.253 , pp. 1129-1132
    • Ferns, G.A.1    Raines, E.W.2    Sprugel, K.H.3    Motani, A.S.4    Reidy, M.A.5    Ross, R.6
  • 123
  • 124
    • 0026534274 scopus 로고
    • Platelet-derived growth factor promotes smooth muscle migration and intimal thickening in a rat model of balloon angioplasty
    • Jawien A, Bowen-Pope DF, Lindner V, Schwartz SM, Clowes AW. Platelet-derived growth factor promotes smooth muscle migration and intimal thickening in a rat model of balloon angioplasty. J Clin Invest. 1992;89:507-511
    • (1992) J Clin Invest , vol.89 , pp. 507-511
    • Jawien, A.1    Bowen-Pope, D.F.2    Lindner, V.3    Schwartz, S.M.4    Clowes, A.W.5
  • 125
    • 0027207192 scopus 로고
    • Recombinant platelet-derived growth factor B gene expression in porcine arteries induce intimal hyperplasia in vivo
    • Nabel EG, Yang Z, Liptay S, San H, Gordon D, Haudenschild CC, Nabel GJ. Recombinant platelet-derived growth factor B gene expression in porcine arteries induce intimal hyperplasia in vivo. J Clin Invest. 1993;91:1822-1829
    • (1993) J Clin Invest , vol.91 , pp. 1822-1829
    • Nabel, E.G.1    Yang, Z.2    Liptay, S.3    San, H.4    Gordon, D.5    Haudenschild, C.C.6    Nabel, G.J.7
  • 127
    • 79958811041 scopus 로고    scopus 로고
    • Disruption of platelet-derived growth factordependent phosphatidylinositol 3-kinase and phospholipase Cγ 1 activity abolishes vascular smooth muscle cell proliferation and migration and attenuates neointima formation in vivo
    • Caglayan E, Vantler M, Leppänen O, Gerhardt F, Mustafov L, Ten Freyhaus H, Kappert K, Odenthal M, Zimmermann WH, Tallquist MD, Rosenkranz S. Disruption of platelet-derived growth factordependent phosphatidylinositol 3-kinase and phospholipase Cγ 1 activity abolishes vascular smooth muscle cell proliferation and migration and attenuates neointima formation in vivo. J Am Coll Cardiol. 2011;57:2527-2538
    • (2011) J Am Coll Cardiol , vol.57 , pp. 2527-2538
    • Caglayan, E.1    Vantler, M.2    Leppänen, O.3    Gerhardt, F.4    Mustafov, L.5    Ten Freyhaus, H.6    Kappert, K.7    Odenthal, M.8    Zimmermann, W.H.9    Tallquist, M.D.10    Rosenkranz, S.11
  • 128
    • 33745880884 scopus 로고    scopus 로고
    • PDGFR alpha-positive B cells are neural stem cells in the adult SVZ that form glioma-like growths in response to increased PDGF signaling
    • Jackson EL, Garcia-Verdugo JM, Gil-Perotin S, Roy M, Quinones-Hinojosa A, VandenBerg S, Alvarez-Buylla A. PDGFR alpha-positive B cells are neural stem cells in the adult SVZ that form glioma-like growths in response to increased PDGF signaling. Neuron. 2006;51:187-199
    • (2006) Neuron , vol.51 , pp. 187-199
    • Jackson, E.L.1    Garcia-Verdugo, J.M.2    Gil-Perotin, S.3    Roy, M.4    Quinones-Hinojosa, A.5    VandenBerg, S.6    Alvarez-Buylla, A.7
  • 129
    • 0141645497 scopus 로고    scopus 로고
    • Targeting PDGF receptors in cancer-rationales and proof of concept clinical trials
    • George D. Targeting PDGF receptors in cancer-rationales and proof of concept clinical trials. Adv Exp Med Biol. 2003;532:141-151
    • (2003) Adv Exp Med Biol , vol.532 , pp. 141-151
    • George, D.1
  • 130
    • 23044469458 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor-beta (PDGFR-beta) activation promotes its association with the low density lipoprotein receptor-related protein (LRP). Evidence for coreceptor function
    • Newton CS, Loukinova E, Mikhailenko I, Ranganathan S, Gao Y, Haudenschild C, Strickland DK. Platelet-derived growth factor receptor-beta (PDGFR-beta) activation promotes its association with the low density lipoprotein receptor-related protein (LRP). Evidence for coreceptor function. J Biol Chem. 2005;280:27872-27878
    • (2005) J Biol Chem , vol.280 , pp. 27872-27878
    • Newton, C.S.1    Loukinova, E.2    Mikhailenko, I.3    Ranganathan, S.4    Gao, Y.5    Haudenschild, C.6    Strickland, D.K.7
  • 131
    • 84880804841 scopus 로고    scopus 로고
    • The LDL receptor-related protein 1 (LRP1) regulates the PDGF signaling pathway by binding the protein phosphatase SHP-2 and modulating SHP-2-mediated PDGF signaling events
    • Craig J, Mikhailenko I, Noyes N, Migliorini M, Strickland DK. The LDL receptor-related protein 1 (LRP1) regulates the PDGF signaling pathway by binding the protein phosphatase SHP-2 and modulating SHP-2-mediated PDGF signaling events. PLoS One. 2013;8:e70432
    • (2013) PLoS One , vol.8
    • Craig, J.1    Mikhailenko, I.2    Noyes, N.3    Migliorini, M.4    Strickland, D.K.5
  • 132
    • 0038771965 scopus 로고    scopus 로고
    • The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
    • Neel BG, Gu H, Pao L. The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends Biochem Sci. 2003;28:284-293
    • (2003) Trends Biochem Sci , vol.28 , pp. 284-293
    • Neel, B.G.1    Gu, H.2    Pao, L.3
  • 133
    • 0033604644 scopus 로고    scopus 로고
    • Shp-2 tyrosine phosphatase: Signaling one cell or many
    • Feng GS. Shp-2 tyrosine phosphatase: Signaling one cell or many. Exp Cell Res. 1999;253:47-54
    • (1999) Exp Cell Res , vol.253 , pp. 47-54
    • Feng, G.S.1
  • 134
    • 0035313868 scopus 로고    scopus 로고
    • Combinatorial control of the specificity of protein tyrosine phosphatases
    • Tonks NK, Neel BG. Combinatorial control of the specificity of protein tyrosine phosphatases. Curr Opin Cell Biol. 2001;13:182-195
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 182-195
    • Tonks, N.K.1    Neel, B.G.2
  • 136
    • 0033552883 scopus 로고    scopus 로고
    • Atherosclerosis-An inflammatory disease
    • Ross R. Atherosclerosis-An inflammatory disease. N Engl J Med. 1999;340:115-126
    • (1999) N Engl J Med , vol.340 , pp. 115-126
    • Ross, R.1
  • 138
    • 84890570924 scopus 로고    scopus 로고
    • Low density receptor-related protein 1 (LRP1) promotes anti-inflammatory phenotype in murine macrophages
    • May P, Bock HH, Nofer Jr. Low density receptor-related protein 1 (LRP1) promotes anti-inflammatory phenotype in murine macrophages. Cell Tissue Res. 2013;354:887-889
    • (2013) Cell Tissue Res , vol.354 , pp. 887-889
    • May, P.1    Bock, H.H.2    Nofer, J.R.3
  • 139
    • 69849100882 scopus 로고    scopus 로고
    • Inactivation of the LRP1 intracellular NPxYxxL motif in LDLR-deficient mice enhances postprandial dyslipidemia and atherosclerosis
    • Gordts PL, Reekmans S, Lauwers A, Van Dongen A, Verbeek L, Roebroek AJ. Inactivation of the LRP1 intracellular NPxYxxL motif in LDLR-deficient mice enhances postprandial dyslipidemia and atherosclerosis. Arterioscler Thromb Vasc Biol. 2009;29:1258-1264
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 1258-1264
    • Gordts, P.L.1    Reekmans, S.2    Lauwers, A.3    Van Dongen, A.4    Verbeek, L.5    Roebroek, A.J.6
  • 140
    • 77957866595 scopus 로고    scopus 로고
    • Inflammatory mediators promote production of shed LRP1/CD91, which regulates cell signaling and cytokine expression by macrophages
    • Gorovoy M, Gaultier A, Campana WM, Firestein GS, Gonias SL. Inflammatory mediators promote production of shed LRP1/CD91, which regulates cell signaling and cytokine expression by macrophages. J Leukoc Biol. 2010;88:769-778
    • (2010) J Leukoc Biol , vol.88 , pp. 769-778
    • Gorovoy, M.1    Gaultier, A.2    Campana, W.M.3    Firestein, G.S.4    Gonias, S.L.5
  • 141
    • 1542313954 scopus 로고    scopus 로고
    • Transforming growth factor beta and atherosclerosis: So far, so good for the protective cytokine hypothesis
    • Grainger DJ. Transforming growth factor beta and atherosclerosis: So far, so good for the protective cytokine hypothesis. Arterioscler Thromb Vasc Biol. 2004;24:399-404
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 399-404
    • Grainger, D.J.1
  • 142
    • 33746829275 scopus 로고    scopus 로고
    • Transforming growth factor-betas and vascular disorders
    • Bobik A. Transforming growth factor-betas and vascular disorders. Arterioscler Thromb Vasc Biol. 2006;26:1712-1720
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 1712-1720
    • Bobik, A.1
  • 143
    • 37549065952 scopus 로고    scopus 로고
    • Control of phenotypic plasticity of smooth muscle cells by bone morphogenetic protein signaling through the myocardin-related transcription factors
    • Lagna G, Ku MM, Nguyen PH, Neuman NA, Davis BN, Hata A. Control of phenotypic plasticity of smooth muscle cells by bone morphogenetic protein signaling through the myocardin-related transcription factors. J Biol Chem. 2007;282:37244-37255
    • (2007) J Biol Chem , vol.282 , pp. 37244-37255
    • Lagna, G.1    Ku, M.M.2    Nguyen, P.H.3    Neuman, N.A.4    Davis, B.N.5    Hata, A.6
  • 144
    • 12144274863 scopus 로고    scopus 로고
    • BMP4 inhibits proliferation and promotes myocyte differentiation of lung fibroblasts via Smad1 and JNK pathways
    • Jeffery TK, Upton PD, Trembath RC, Morrell NW. BMP4 inhibits proliferation and promotes myocyte differentiation of lung fibroblasts via Smad1 and JNK pathways. Am J Physiol Lung Cell Mol Physiol. 2005;288:L370-L378
    • (2005) Am J Physiol Lung Cell Mol Physiol , vol.288
    • Jeffery, T.K.1    Upton, P.D.2    Trembath, R.C.3    Morrell, N.W.4
  • 148
    • 0034641666 scopus 로고    scopus 로고
    • Ribozyme oligonucleotides against transforming growth factor-beta inhibited neointimal formation after vascular injury in rat model: Potential application of ribozyme strategy to treat cardiovascular disease
    • Yamamoto K, Morishita R, Tomita N, Shimozato T, Nakagami H, Kikuchi A, Aoki M, Higaki J, Kaneda Y, Ogihara T. Ribozyme oligonucleotides against transforming growth factor-beta inhibited neointimal formation after vascular injury in rat model: Potential application of ribozyme strategy to treat cardiovascular disease. Circulation. 2000;102:1308-1314
    • (2000) Circulation , vol.102 , pp. 1308-1314
    • Yamamoto, K.1    Morishita, R.2    Tomita, N.3    Shimozato, T.4    Nakagami, H.5    Kikuchi, A.6    Aoki, M.7    Higaki, J.8    Kaneda, Y.9    Ogihara, T.10
  • 149
    • 0033612364 scopus 로고    scopus 로고
    • Soluble transforming growth factor-beta type II receptor inhibits negative remodeling, fibroblast transdifferentiation, and intimal lesion formation but not endothelial growth
    • Smith JD, Bryant SR, Couper LL, Vary CP, Gotwals PJ, Koteliansky VE, Lindner V. Soluble transforming growth factor-beta type II receptor inhibits negative remodeling, fibroblast transdifferentiation, and intimal lesion formation but not endothelial growth. Circ Res. 1999;84:1212-1222
    • (1999) Circ Res , vol.84 , pp. 1212-1222
    • Smith, J.D.1    Bryant, S.R.2    Couper, L.L.3    Vary, C.P.4    Gotwals, P.J.5    Koteliansky, V.E.6    Lindner, V.7


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