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Volumn 24, Issue 22, 2015, Pages 6374-6389

Common and specific effects of TIE2 mutations causing venous malformations

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOPOIETIN RECEPTOR; APROTININ; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PLASMIN; PLASMINOGEN; TISSUE PLASMINOGEN ACTIVATOR; UROKINASE; FIBRIN DEGRADATION PRODUCT; FIBRIN FRAGMENT D; LIGAND;

EID: 84949057867     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddv349     Document Type: Article
Times cited : (76)

References (54)
  • 1
    • 77958017956 scopus 로고    scopus 로고
    • Venous malformation: update on aetiopathogenesis, diagnosis and management
    • Dompmartin, A., Vikkula, M. and Boon, L.M. (2010) Venous malformation: update on aetiopathogenesis, diagnosis and management. Phlebology, 25, 224-235.
    • (2010) Phlebology. , vol.25 , pp. 224-235
    • Dompmartin, A.1    Vikkula, M.2    Boon, L.M.3
  • 2
    • 84948977608 scopus 로고    scopus 로고
    • Vascular malformations Fitzpatrick's Dermatology in General Medicine.
    • In Lowell, A., Goldsmith, S.I., Katz, B.A., Gilchrest, A.S., Paller, D.J. and Leffell, K.W.(eds),Mcgraw-Hill Professional Publishing, New York, NY, USA
    • Boon, L.M. and Vikkula, M. (2012) Vascular malformations. In Lowell, A., Goldsmith, S.I., Katz, B.A., Gilchrest, A. S., Paller, D.J. and Leffell, K.W.(eds), Fitzpatrick's Dermatology in General Medicine. Mcgraw-Hill Professional Publishing,New York, NY, USA.
    • (2012)
    • Boon, L.M.1    Vikkula, M.2
  • 3
    • 84877293027 scopus 로고    scopus 로고
    • Variable somatic TIE2 mutations in half of sporadic venous malformations
    • Soblet, J., Limaye, N., Uebelhoer, M., Boon, L.M. and Vikkula, M. (2013) Variable somatic TIE2 mutations in half of sporadic venous malformations. Mol. Syndromol., 4, 179-183.
    • (2013) Mol. Syndromol. , vol.4 , pp. 179-183
    • Soblet, J.1    Limaye, N.2    Uebelhoer, M.3    Boon, L.M.4    Vikkula, M.5
  • 11
    • 74349107185 scopus 로고    scopus 로고
    • Angiogenic and prothrombotic markers in extensive 4slow-flow vascular malformations: implications for antiangiogenic/antithrombotic strategies
    • Redondo, P., Aguado, L., Marquina, M., Paramo, J., Sierra, A.,Sánchez-Ibarrola, A., Martínez-Cuesta, A. and Cabrera,J.(2010) Angiogenic and prothrombotic markers in extensive 4slow-flow vascular malformations: implications for antiangiogenic/antithrombotic strategies. Br. J. Dermatol.,162, 350-356.
    • (2010) Br. J. Dermatol. , vol.162 , pp. 350-356
    • Redondo, P.1    Aguado, L.2    Marquina, M.3    Paramo, J.4    Sierra, A.5    Sánchez-Ibarrola, A.6    Martínez-Cuesta, A.7    Cabrera, J.8
  • 12
    • 47849114345 scopus 로고    scopus 로고
    • Coagulation disorders in patients with venous malformation of the limbs and trunk: a case series of 118 patients
    • Mazoyer, E., Enjolras, O., Bisdorff, A., Perdu, J.,Wassef, M. and Drouet, L. (2008) Coagulation disorders in patients with venous malformation of the limbs and trunk: a case series of 118 patients. Arch. Dermatol., 144, 861-867.
    • (2008) Arch. Dermatol. , vol.144 , pp. 861-867
    • Mazoyer, E.1    Enjolras, O.2    Bisdorff, A.3    Perdu, J.4    Wassef, M.5    Drouet, L.6
  • 16
    • 0006677050 scopus 로고    scopus 로고
    • Angiopoietin-1 regulates endothelial cell survival through the phosphatidylinositol 3'-kinase/Akt signal transduction pathway
    • Kim, I., Kim, H.G., So, J.N., Kim, J.H., Kwak, H.J. and Koh, G.Y. (2000) Angiopoietin-1 regulates endothelial cell survival through the phosphatidylinositol 3'-kinase/Akt signal transduction pathway. Circ. Res., 86, 24-29.
    • (2000) Circ. Res. , vol.86 , pp. 24-29
    • Kim, I.1    Kim, H.G.2    So, J.N.3    Kim, J.H.4    Kwak, H.J.5    Koh, G.Y.6
  • 17
    • 0042850313 scopus 로고    scopus 로고
    • Localization of Tie2 and phospholipase D in endothelial caveolae is involved in angiopoietin-1-induced MEK/ ERK phosphorylation and migration in endothelial cells
    • Yoon, M.J., Cho, C.H., Lee, C.S., Jang, I.H., Ryu, S.H. and Koh, G.Y. (2003) Localization of Tie2 and phospholipase D in endothelial caveolae is involved in angiopoietin-1-induced MEK/ ERK phosphorylation and migration in endothelial cells. Biochem. Biophys. Res. Commun., 308, 101-105.
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 101-105
    • Yoon, M.J.1    Cho, C.H.2    Lee, C.S.3    Jang, I.H.4    Ryu, S.H.5    Koh, G.Y.6
  • 18
    • 0031834338 scopus 로고    scopus 로고
    • Tyrosine 1101 of Tie2 is the major site of association of p85 and is required for activation of phosphatidylinositol3-kinase and Akt
    • Kontos, C.D., Stauffer, T.P., Yang, W.P., York, J.D., Huang, Li., Blanar, M.A., Meyer, T. and Peters, K.G. (1998) Tyrosine 1101 of Tie2 is the major site of association of p85 and is required for activation of phosphatidylinositol 3-kinase and Akt. Mol. Cell. Biol., 18, 4131-4140.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4131-4140
    • Kontos, C.D.1    Stauffer, T.P.2    Yang, W.P.3    York, J.D.4    Huang, Li.5    Blanar, M.A.6    Meyer, T.7    Peters, K.G.8
  • 19
    • 0032695794 scopus 로고    scopus 로고
    • Identification of Tek/Tie2 binding partners: binding to a multifunctional docking site mediates cell survival and migration
    • Jones, N., Master, Z., Jones, J., Bouchard, D., Gunji, Y., Sasaki, H., Daly, R., Alitalo, K. and Dumont, D.J. (1999) Identification of Tek/Tie2 binding partners: binding to a multifunctional docking site mediates cell survival and migration. J. Biol. Chem., 274, 30896-30905.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30896-30905
    • Jones, N.1    Master, Z.2    Jones, J.3    Bouchard, D.4    Gunji, Y.5    Sasaki, H.6    Daly, R.7    Alitalo, K.8    Dumont, D.J.9
  • 20
    • 5644241730 scopus 로고    scopus 로고
    • The kinase activity of fibroblast growth factor receptor 3 with activation loop mutations affects receptor trafficking and signaling
    • Lievens, P.M.J., Mutinelli, C., Baynes, D. and Liboi, E. (2004) The kinase activity of fibroblast growth factor receptor 3 with activation loop mutations affects receptor trafficking and signaling. J. Biol. Chem., 279, 43254-43260.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43254-43260
    • Lievens, P.M.J.1    Mutinelli, C.2    Baynes, D.3    Liboi, E.4
  • 22
    • 33748740798 scopus 로고    scopus 로고
    • Intracellular retention, degradation, and signaling of glycosylation-deficient FGFR2 and craniosynostosis syndrome-associated FGFR2C278F
    • Hatch, N.E., Hudson, M., Seto, M.L., Cunningham, M.L. and Bothwell, M. (2006) Intracellular retention, degradation, and signaling of glycosylation-deficient FGFR2 and craniosynostosis syndrome-associated FGFR2C278F. J. Biol. Chem., 281, 27292-27305.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27292-27305
    • Hatch, N.E.1    Hudson, M.2    Seto, M.L.3    Cunningham, M.L.4    Bothwell, M.5
  • 23
    • 45549099309 scopus 로고    scopus 로고
    • Inhibition of N-linked glycosylation disrupts receptor tyrosine kinase signaling in tumor cells
    • Contessa, J.N., Bhojani, M.S., Freeze, H.H., Rehemtulla, A. and Lawrence, T.S. (2008) Inhibition of N-linked glycosylation disrupts receptor tyrosine kinase signaling in tumor cells. Cancer. Res., 68, 3803-3809.
    • (2008) Cancer. Res. , vol.68 , pp. 3803-3809
    • Contessa, J.N.1    Bhojani, M.S.2    Freeze, H.H.3    Rehemtulla, A.4    Lawrence, T.S.5
  • 24
    • 0032482220 scopus 로고    scopus 로고
    • Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization
    • Bass, J., Chiu, G., Argon, Y. and Steiner, D.F. (1998) Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization. J. Cell. Biol., 141, 637-646.
    • (1998) J. Cell. Biol. , vol.141 , pp. 637-646
    • Bass, J.1    Chiu, G.2    Argon, Y.3    Steiner, D.F.4
  • 26
    • 0028973594 scopus 로고
    • GRB2 and SH-PTP2: potentially important endothelial signaling molecules downstream of the TEK/TIE2 receptor tyrosinekinase
    • Huang, L., Turck, C.W., Rao, P. and Peters, K.G. (1995) GRB2 and SH-PTP2: potentially important endothelial signaling molecules downstream of the TEK/TIE2 receptor tyrosine kinase. Oncogene., 11, 2097-2103.
    • (1995) Oncogene. , vol.11 , pp. 2097-2103
    • Huang, L.1    Turck, C.W.2    Rao, P.3    Peters, K.G.4
  • 27
    • 84873036563 scopus 로고    scopus 로고
    • Systematic and quantitative analysis of G protein-coupled receptor trafficking motifs
    • Hurt, C.M., Ho, V.K. and Angelotti, T. (2013) Systematic and quantitative analysis of G protein-coupled receptor trafficking motifs. Methods Enzymol., 521, 171-187.
    • (2013) Methods Enzymol. , vol.521 , pp. 171-187
    • Hurt, C.M.1    Ho, V.K.2    Angelotti, T.3
  • 28
    • 84877154358 scopus 로고    scopus 로고
    • Ligand-independent Tie2 dimers mediate kinase activity stimulated by high dose angiopoietin-1
    • Yamakawa, D., Kidoya, H., Sakimoto, S., Jia,W., Naito, H. and Takakura, N. (2013) Ligand-independent Tie2 dimers mediate kinase activity stimulated by high dose angiopoietin-1. J. Biol. Chem., 288, 12469-12477.
    • (2013) J. Biol. Chem. , vol.288 , pp. 12469-12477
    • Yamakawa, D.1    Kidoya, H.2    Sakimoto, S.3    Jia, W.4    Naito, H.5    Takakura, N.6
  • 29
    • 33749414768 scopus 로고    scopus 로고
    • Activation of Tie2 by angiopoietin-1 and angiopoietin-2 results in their release and receptor internalization
    • Bogdanovic, E., Nguyen, V.P.K.H. and Dumont, D.J. (2006) Activation of Tie2 by angiopoietin-1 and angiopoietin-2 results in their release and receptor internalization. J. Cell. Sci., 119, 3551-3560.
    • (2006) J. Cell. Sci. , vol.119 , pp. 3551-3560
    • Bogdanovic, E.1    Nguyen, V.P.K.H.2    Dumont, D.J.3
  • 30
    • 0035678581 scopus 로고    scopus 로고
    • Identification of a soluble form of the angiopoietin receptor TIE-2 released from endothelial cells and present in human blood
    • Reusch, P., Barleon, B.,Weindel, K., Martiny-Baron, G., Gödde, A., Siemeister, G. and Marmé, D. (2001) Identification of a soluble form of the angiopoietin receptor TIE-2 released from endothelial cells and present in human blood. Angiogenesis, 4, 123-131.
    • (2001) Angiogenesis. , vol.4 , pp. 123-131
    • Reusch, P.1    Barleon, B.2    Weindel, K.3    Martiny-Baron, G.4    Gödde, A.5    Siemeister, G.6    Marmé, D.7
  • 31
    • 36348946298 scopus 로고    scopus 로고
    • VEGF induces Tie2 shedding via a phosphoinositide 3-kinase/Akt dependent pathway to modulate Tie2 signaling
    • Findley, C.M., Cudmore, M.J., Ahmed, A. and Kontos, C.D. (2007) VEGF induces Tie2 shedding via a phosphoinositide 3-kinase/Akt dependent pathway to modulate Tie2 signaling. Arterioscler. Thromb. Vasc. Biol., 27, 2619-2626.
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 2619-2626
    • Findley, C.M.1    Cudmore, M.J.2    Ahmed, A.3    Kontos, C.D.4
  • 34
    • 78649728329 scopus 로고    scopus 로고
    • Autocrine fibronectin directs matrix assembly and crosstalk between cell-matrix and cell-cell adhesion in vascular endothelial cells
    • Cseh, B., Fernandez-Sauze, S., Grall, D., Schaub, S., Doma, E. and Van Obberghen-Schilling, E. (2010) Autocrine fibronectin directs matrix assembly and crosstalk between cell-matrix and cell-cell adhesion in vascular endothelial cells. J. Cell Sci., 123, 3989-3999.
    • (2010) J. Cell Sci. , vol.123 , pp. 3989-3999
    • Cseh, B.1    Fernandez-Sauze, S.2    Grall, D.3    Schaub, S.4    Doma, E.5    Van Obberghen-Schilling, E.6
  • 35
    • 0018102645 scopus 로고
    • Identification, localization, and role of fibronectin in cultured bovine endothelial cells
    • Birdwell, C.R., Gospodarowicz, D. and Nicolson, G.L. (1978) Identification, localization, and role of fibronectin in cultured bovine endothelial cells. Proc. Natl. Acad. Sci. USA, 75, 3273-3277.
    • (1978) Proc. Natl. Acad. Sci. USA. , vol.75 , pp. 3273-3277
    • Birdwell, C.R.1    Gospodarowicz, D.2    Nicolson, G.L.3
  • 36
    • 0017148395 scopus 로고
    • Correlation between tumor induction and the large external transformation sensitive protein on the cell surface
    • Chen, L.B., Gallimore, P.H. and Mcdougall, J.K. (1976) Correlation between tumor induction and the large external transformation sensitive protein on the cell surface. Proc. Natl. Acad. Sci. USA, 73, 3570-3574.
    • (1976) Proc. Natl. Acad. Sci. USA. , vol.73 , pp. 3570-3574
    • Chen, L.B.1    Gallimore, P.H.2    Mcdougall, J.K.3
  • 37
    • 0032748089 scopus 로고    scopus 로고
    • Tensional forces in fibrillar extracellular matrices control directional capillary sprouting
    • Korff, T. and Augustin, H.G. (1999) Tensional forces in fibrillar extracellular matrices control directional capillary sprouting. J. Cell. Sci., 112, 3249-3258.
    • (1999) J. Cell. Sci. , vol.112 , pp. 3249-3258
    • Korff, T.1    Augustin, H.G.2
  • 40
    • 84903377262 scopus 로고    scopus 로고
    • Non-collagenous ECM proteins in blood vessel morphogenesis and cancer
    • Kostourou, V. and Papalazarou, V. (2014) Non-collagenous ECM proteins in blood vessel morphogenesis and cancer. Biochim. Biophys. Acta Gen. Subj., 1840, 2403-2413.
    • (2014) Biochim. Biophys. Acta Gen. Subj. , vol.1840 , pp. 2403-2413
    • Kostourou, V.1    Papalazarou, V.2
  • 41
    • 24944468632 scopus 로고    scopus 로고
    • Stable interaction between alpha5beta1 integrin and Tie2 tyrosine kinase receptor regulates endothelial cell response to Ang-1
    • Cascone, I., Napione, L., Maniero, F., Serini, G. and Bussolino, F. (2005) Stable interaction between alpha5beta1 integrin and Tie2 tyrosine kinase receptor regulates endothelial cell response to Ang-1. J. Cell Biol., 170, 993-1004.
    • (2005) J. Cell Biol. , vol.170 , pp. 993-1004
    • Cascone, I.1    Napione, L.2    Maniero, F.3    Serini, G.4    Bussolino, F.5
  • 42
    • 0030818072 scopus 로고    scopus 로고
    • Fibronectins are essential for heart and blood vessel morphogenesis but are dispensable for initial specification of precursor cells
    • George, B.E.L., Baldwin, H.S., Hynes, R.O. and George, E.L. (1997) Fibronectins are essential for heart and blood vessel morphogenesis but are dispensable for initial specification of precursor cells. Blood, 90, 3073-3081.
    • (1997) Blood. , vol.90 , pp. 3073-3081
    • George, B.E.L.1    Baldwin, H.S.2    Hynes, R.O.3    George, E.L.4
  • 43
    • 0019850184 scopus 로고
    • Effect of plasminogen activator (urokinase), plasmin, and thrombin on glycoprotein and collagenous components of basement membrane
    • Liotta, L.A.,Goldfarb, R.H., Brundage, R., Siegal,G.P., Terranova,V. andGarbisa, S. (1981) Effect of plasminogen activator (urokinase), plasmin, and thrombin on glycoprotein and collagenous components of basement membrane. Cancer Res., 41,4629-4636.
    • (1981) Cancer Res. , vol.41 , pp. 4629-4636
    • Liotta, L.A.1    Goldfarb, R.H.2    Brundage, R.3    Siegal, G.P.4    Terranova, V.5    Garbisa, S.6
  • 44
    • 0030907299 scopus 로고    scopus 로고
    • Involvement of PA/plasmin system in the processing of pro-MMP-9 and in the second step of pro-MMP-2 activation
    • Baramova, E.N., Bajou, K., Remacle, A., L'Hoir, C., Krell, H.W., Weidle, U.K., Noel, A. and Foidart, J.M. (1997) Involvement of PA/plasmin system in the processing of pro-MMP-9 and in the second step of pro-MMP-2 activation. FEBS Lett., 405, 157-162.
    • (1997) FEBS Lett. , vol.405 , pp. 157-162
    • Baramova, E.N.1    Bajou, K.2    Remacle, A.3    L'Hoir, C.4    Krell, H.W.5    Weidle, U.K.6    Noel, A.7    Foidart, J.M.8
  • 46
    • 0037446064 scopus 로고    scopus 로고
    • Vascular smooth muscle cells efficiently activate a newproteinase cascade involving plasminogen and fibronectin
    • Houard, X., Monnot, C., Dive, V., Corvol, P. and Pagano, M. (2003) Vascular smooth muscle cells efficiently activate a newproteinase cascade involving plasminogen and fibronectin. J. Cell Biochem., 88, 1188-1201.
    • (2003) J. Cell Biochem. , vol.88 , pp. 1188-1201
    • Houard, X.1    Monnot, C.2    Dive, V.3    Corvol, P.4    Pagano, M.5
  • 47
    • 0034657657 scopus 로고    scopus 로고
    • Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase
    • Bonnefoy, A. and Legrand, C. (2000) Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase. Thromb. Res., 98, 323-332.
    • (2000) Thromb. Res. , vol.98 , pp. 323-332
    • Bonnefoy, A.1    Legrand, C.2
  • 48
    • 0025063772 scopus 로고
    • Increased proteolytic activity is responsible for the aberrant morphogenetic behavior of endothelial cells expressing the middle Toncogene
    • Montesano, R., Pepper, M.S., Möhle-Steinlein, U., Risau, W., Wagner, E.F. and Orci, L. (1990) Increased proteolytic activity is responsible for the aberrant morphogenetic behavior of endothelial cells expressing the middle Toncogene. Cell, 62, 435-445.
    • (1990) Cell. , vol.62 , pp. 435-445
    • Montesano, R.1    Pepper, M.S.2    Möhle-Steinlein, U.3    Risau, W.4    Wagner, E.F.5    Orci, L.6
  • 51
    • 33846446433 scopus 로고    scopus 로고
    • Antiproliferative agents alter vascular plasminogen activator inhibitor-1 expression: A potential prothrombotic mechanism of drugeluting stents
    • Muldowney, J.A.S., Stringham, J.R., Levy, S.E., Gleaves, L.A., Eren, M., Piana, R.N. and Vaughan, D.E. (2007) Antiproliferative agents alter vascular plasminogen activator inhibitor-1 expression: a potential prothrombotic mechanism of drugeluting stents. Arterioscler. Thromb. Vasc. Biol., 27, 400-406.
    • (2007) Arterioscler. Thromb. Vasc. Biol. , vol.27 , pp. 400-406
    • Muldowney, J.A.S.1    Stringham, J.R.2    Levy, S.E.3    Gleaves, L.A.4    Eren, M.5    Piana, R.N.6    Vaughan, D.E.7
  • 52
    • 0029862497 scopus 로고    scopus 로고
    • A stable human-derived packaging cell line for production of high titer retrovirus/vesicular stomatitis virus G pseudotypes
    • Ory, D.S., Neugeboren, B.A. and Mulligan, R.C. (1996) A stable human-derived packaging cell line for production of high titer retrovirus/vesicular stomatitis virus G pseudotypes. Proc. Natl. Acad. Sci. USA, 93, 11400-11406.
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 11400-11406
    • Ory, D.S.1    Neugeboren, B.A.2    Mulligan, R.C.3
  • 53
    • 0142227052 scopus 로고    scopus 로고
    • Retrovirus-mediated gene transfer and expression cloning: powerful tools in functional genomics
    • Kitamura, T., Koshino, Y., Shibata, F., Oki, T., Nakajima, H., Nosaka, T. and Kumagai, H. (2003) Retrovirus-mediated gene transfer and expression cloning: powerful tools in functional genomics. Exp. Hematol., 31, 1007-1014.
    • (2003) Exp. Hematol. , vol.31 , pp. 1007-1014
    • Kitamura, T.1    Koshino, Y.2    Shibata, F.3    Oki, T.4    Nakajima, H.5    Nosaka, T.6    Kumagai, H.7
  • 54


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