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Volumn 77, Issue , 2016, Pages 130-138

Corrigendum to “Selective binding of C-6OH sulfated hyaluronic acid to the angiogenic isoform of VEGF165” [Biomaterials 77(2016) 130–138, (S0142961215008844), (10.1016/j.biomaterials.2015.10.074)];Selective binding of C-6 OH sulfated hyaluronic acid to the angiogenic isoform of VEGF165

Author keywords

Angiogenesis; Selective binding property; Sulfated sodium hyaluronate; Vascular endothelial growth factor 165; VEGF165a; VEGF165b

Indexed keywords

ANTIBODIES; BINDING ENERGY; CELL ENGINEERING; COST EFFECTIVENESS; DISEASES; DISSOCIATION; DRUG DELIVERY; ENDOTHELIAL CELLS; ORGANIC ACIDS; SULFUR COMPOUNDS; SYNTHESIS (CHEMICAL);

EID: 84949256478     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2024.122501     Document Type: Erratum
Times cited : (47)

References (36)
  • 1
    • 77957764473 scopus 로고    scopus 로고
    • Vascular endothelial growth factor and age-related macular degeneration: from basic science to therapy
    • Ferrara N. Vascular endothelial growth factor and age-related macular degeneration: from basic science to therapy. Nat. Med. 2010, 16:1107-1111.
    • (2010) Nat. Med. , vol.16 , pp. 1107-1111
    • Ferrara, N.1
  • 3
    • 0020572581 scopus 로고
    • Angiogenesis inhibition and tumor-regression caused by heparin or a heparin fragment in the presence of cortisone
    • Folkman J., Langer R., Linhardt R.J., Haudenschild C., Taylor S. Angiogenesis inhibition and tumor-regression caused by heparin or a heparin fragment in the presence of cortisone. Science 1983, 221:719-725.
    • (1983) Science , vol.221 , pp. 719-725
    • Folkman, J.1    Langer, R.2    Linhardt, R.J.3    Haudenschild, C.4    Taylor, S.5
  • 5
    • 38449100932 scopus 로고    scopus 로고
    • Anti-vascular endothelial growth factor therapy for ocular neovascular disease
    • Andreoli C.M., Miller J.W. Anti-vascular endothelial growth factor therapy for ocular neovascular disease. Curr. Opin. Ophthalmol. 2007, 18:502-508.
    • (2007) Curr. Opin. Ophthalmol. , vol.18 , pp. 502-508
    • Andreoli, C.M.1    Miller, J.W.2
  • 7
    • 27944490875 scopus 로고    scopus 로고
    • VEGF as a therapeutic target in cancer
    • Ferrara N. VEGF as a therapeutic target in cancer. Oncology 2005, 69:11-16.
    • (2005) Oncology , vol.69 , pp. 11-16
    • Ferrara, N.1
  • 8
    • 0037098860 scopus 로고    scopus 로고
    • VEGF(165)b, an inhibitory splice variant of vascular endothelial growth factor, is down-regulated in renal cell carcinoma
    • Bates D.O., Cui T.G., Doughty J.M., Winkler M., Sugiono M., Shields J.D., et al. VEGF(165)b, an inhibitory splice variant of vascular endothelial growth factor, is down-regulated in renal cell carcinoma. Cancer Res. 2002, 62:4123-4131.
    • (2002) Cancer Res. , vol.62 , pp. 4123-4131
    • Bates, D.O.1    Cui, T.G.2    Doughty, J.M.3    Winkler, M.4    Sugiono, M.5    Shields, J.D.6
  • 9
    • 56349136033 scopus 로고    scopus 로고
    • Expression of pro- and anti-angiogenic isoforms of VEGF is differentially regulated by splicing and growth factors
    • Nowak D.G., Woolard J., Amin E.M., Konopatskaya O., Saleem M.A., Churchill A.J., et al. Expression of pro- and anti-angiogenic isoforms of VEGF is differentially regulated by splicing and growth factors. J. Cell Sci. 2008, 121:3487-3495.
    • (2008) J. Cell Sci. , vol.121 , pp. 3487-3495
    • Nowak, D.G.1    Woolard, J.2    Amin, E.M.3    Konopatskaya, O.4    Saleem, M.A.5    Churchill, A.J.6
  • 10
    • 7444240909 scopus 로고    scopus 로고
    • VEGF(165)b, an inhibitory vascular endothelial growth factor splice variant: Mechanism of action, in vivo effect on angiogenesis and endogenous protein expression
    • Woolard J., Wang W.Y., Bevan H.S., Qiu Y., Morbidelli L., Pritchard-Jones R.O., et al. VEGF(165)b, an inhibitory vascular endothelial growth factor splice variant: Mechanism of action, in vivo effect on angiogenesis and endogenous protein expression. Cancer Res. 2004, 64:7822-7835.
    • (2004) Cancer Res. , vol.64 , pp. 7822-7835
    • Woolard, J.1    Wang, W.Y.2    Bevan, H.S.3    Qiu, Y.4    Morbidelli, L.5    Pritchard-Jones, R.O.6
  • 12
    • 27744448867 scopus 로고    scopus 로고
    • Prospective incidence study of diabetes mellitus in New Zealand children aged 0 to 14 years. Diabetologia 48: 643-648
    • on behalf of the New Zealand Children's Diabetes Working Group
    • Willis J., Scott R., Darlow B., Campbell-Stokes P.L., Taylor B.J. Prospective incidence study of diabetes mellitus in New Zealand children aged 0 to 14 years. Diabetologia 48: 643-648. Diabetologia 2005, 2005(48):2442-2443. on behalf of the New Zealand Children's Diabetes Working Group.
    • (2005) Diabetologia , vol.2005 , Issue.48 , pp. 2442-2443
    • Willis, J.1    Scott, R.2    Darlow, B.3    Campbell-Stokes, P.L.4    Taylor, B.J.5
  • 13
    • 42149152015 scopus 로고    scopus 로고
    • VEGF165b, an antiangiogenic VEGF-A isoform, binds and inhibits bevacizumab treatment in experimental colorectal carcinoma: balance of pro-and antiangiogenic VEGF-A isoforms has implications for therapy
    • Varey A., Rennel E., Qiu Y., Bevan H., Perrin R., Raffy S., et al. VEGF165b, an antiangiogenic VEGF-A isoform, binds and inhibits bevacizumab treatment in experimental colorectal carcinoma: balance of pro-and antiangiogenic VEGF-A isoforms has implications for therapy. Br. J. cancer 2008, 98:1366-1379.
    • (2008) Br. J. cancer , vol.98 , pp. 1366-1379
    • Varey, A.1    Rennel, E.2    Qiu, Y.3    Bevan, H.4    Perrin, R.5    Raffy, S.6
  • 14
    • 33644977975 scopus 로고    scopus 로고
    • VEGF(165)-binding sites within heparan sulfate encompass two highly sulfated domains and can be liberated by K5 lyase
    • Robinson C.J., Mulloy B., Gallagher J.T., Stringer S.E. VEGF(165)-binding sites within heparan sulfate encompass two highly sulfated domains and can be liberated by K5 lyase. J. Biol. Chem. 2006, 281:1731-1740.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1731-1740
    • Robinson, C.J.1    Mulloy, B.2    Gallagher, J.T.3    Stringer, S.E.4
  • 15
    • 54549123309 scopus 로고    scopus 로고
    • VEGF-A splicing: the key to anti-angiogenic therapeutics?
    • Harper S.J., Bates D.O. VEGF-A splicing: the key to anti-angiogenic therapeutics?. Nat. Rev. Cancer 2008, 8:880-887.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 880-887
    • Harper, S.J.1    Bates, D.O.2
  • 16
    • 75349091269 scopus 로고    scopus 로고
    • Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling
    • Grunewald F.S., Prota A.E., Giese A., Ballmer-Hofer K. Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling. BBA Proteins Proteom. 2010, 1804:567-580.
    • (2010) BBA Proteins Proteom. , vol.1804 , pp. 567-580
    • Grunewald, F.S.1    Prota, A.E.2    Giese, A.3    Ballmer-Hofer, K.4
  • 19
    • 79958816088 scopus 로고    scopus 로고
    • Targeting hyaluronidase for cancer therapy: Antitumor activity of sulfated hyaluronic acid in prostate cancer cells
    • Benitez A., Yates T.J., Lopez L.E., Cerwinka W.H., Bakkar A., Lokeshwar V.B. Targeting hyaluronidase for cancer therapy: Antitumor activity of sulfated hyaluronic acid in prostate cancer cells. Cancer Res. 2011, 71:4085-4095.
    • (2011) Cancer Res. , vol.71 , pp. 4085-4095
    • Benitez, A.1    Yates, T.J.2    Lopez, L.E.3    Cerwinka, W.H.4    Bakkar, A.5    Lokeshwar, V.B.6
  • 20
    • 77955347373 scopus 로고    scopus 로고
    • Synthetic heparan sulfate oligosaccharides inhibit endothelial cell functions essential for angiogenesis
    • Cole C.L., Hansen S.U., Barath M., Rushton G., Gardiner J.M., Avizienyte E., et al. Synthetic heparan sulfate oligosaccharides inhibit endothelial cell functions essential for angiogenesis. PLoS One 2010, 5.
    • (2010) PLoS One , vol.5
    • Cole, C.L.1    Hansen, S.U.2    Barath, M.3    Rushton, G.4    Gardiner, J.M.5    Avizienyte, E.6
  • 21
    • 21744450786 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans: the sweet side of development
    • Hacker U., Nybakken K., Perrimon N. Heparan sulphate proteoglycans: the sweet side of development. Nat. Rev. Mol. Cell Biol. 2005, 6:530-541.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 530-541
    • Hacker, U.1    Nybakken, K.2    Perrimon, N.3
  • 22
    • 72449141752 scopus 로고    scopus 로고
    • Modifications of hyaluronan influence the interaction with human bone morphogenetic protein-4 (hBMP-4)
    • Hintze V., Moeller S., Schnabelrauch M., Bierbaum S., Viola M., Worch H., et al. Modifications of hyaluronan influence the interaction with human bone morphogenetic protein-4 (hBMP-4). Biomacromolecules 2009, 10:3290-3297.
    • (2009) Biomacromolecules , vol.10 , pp. 3290-3297
    • Hintze, V.1    Moeller, S.2    Schnabelrauch, M.3    Bierbaum, S.4    Viola, M.5    Worch, H.6
  • 23
    • 0028228672 scopus 로고
    • Synthetic polysulfated hyaluronic acid is a potent inhibitor for tumor necrosis factor production
    • Chang N.S., Intrieri C., Mattison J., Armand G. Synthetic polysulfated hyaluronic acid is a potent inhibitor for tumor necrosis factor production. J. Leukoc. Biol. 1994, 55:778-784.
    • (1994) J. Leukoc. Biol. , vol.55 , pp. 778-784
    • Chang, N.S.1    Intrieri, C.2    Mattison, J.3    Armand, G.4
  • 24
    • 0001385243 scopus 로고
    • Hyaluronidase induces murine L929 fibrosarcoma cells resistant to tumor necrosis factor and fas cytotoxicity in the presence of actinomycin D
    • Chang N.-S. Hyaluronidase induces murine L929 fibrosarcoma cells resistant to tumor necrosis factor and fas cytotoxicity in the presence of actinomycin D. Cell Biochem. Biophys. 1995, 27:109-132.
    • (1995) Cell Biochem. Biophys. , vol.27 , pp. 109-132
    • Chang, N.-S.1
  • 25
    • 0032118794 scopus 로고    scopus 로고
    • Sulphated hyaluronic acids: a chemical and biological characterisation
    • Magnani A., Lamponi S., Rappuoli R., Barbucci R. Sulphated hyaluronic acids: a chemical and biological characterisation. Polym. Int. 1998, 46:225-240.
    • (1998) Polym. Int. , vol.46 , pp. 225-240
    • Magnani, A.1    Lamponi, S.2    Rappuoli, R.3    Barbucci, R.4
  • 27
    • 33644804663 scopus 로고    scopus 로고
    • Discovery of a sulfated tetrapeptide that binds to vascular endothelial growth factor
    • Maynard H.D., Hubbell J.A. Discovery of a sulfated tetrapeptide that binds to vascular endothelial growth factor. Acta Biomater. 2005, 1:451-459.
    • (2005) Acta Biomater. , vol.1 , pp. 451-459
    • Maynard, H.D.1    Hubbell, J.A.2
  • 28
    • 84866522723 scopus 로고    scopus 로고
    • Control of protein-binding kinetics on synthetic polymer nanoparticles by tuning flexibility and inducing conformation changes of polymer chains
    • Hoshino Y., Nakamoto M., Miura Y. Control of protein-binding kinetics on synthetic polymer nanoparticles by tuning flexibility and inducing conformation changes of polymer chains. J. Am. Chem. Soc. 2012, 134:15209-15212.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15209-15212
    • Hoshino, Y.1    Nakamoto, M.2    Miura, Y.3
  • 29
    • 78149441693 scopus 로고    scopus 로고
    • Regulation of pathologic retinal angiogenesis in mice and inhibition of VEGF-VEGFR2 binding by soluble heparan sulfate
    • Nishiguchi K.M., Kataoka K., Kachi S., Komeima K., Terasaki H. Regulation of pathologic retinal angiogenesis in mice and inhibition of VEGF-VEGFR2 binding by soluble heparan sulfate. PLoS One 2010, 5:e13493.
    • (2010) PLoS One , vol.5 , pp. e13493
    • Nishiguchi, K.M.1    Kataoka, K.2    Kachi, S.3    Komeima, K.4    Terasaki, H.5
  • 30
    • 0032530717 scopus 로고    scopus 로고
    • VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 Å resolution and mutational analysis of the interface
    • Muller Y.A., Chen Y., Christinger H.W., Li B., Cunningham B.C., Lowman H.B., et al. VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 Å resolution and mutational analysis of the interface. Structure 1998, 6:1153-1167.
    • (1998) Structure , vol.6 , pp. 1153-1167
    • Muller, Y.A.1    Chen, Y.2    Christinger, H.W.3    Li, B.4    Cunningham, B.C.5    Lowman, H.B.6
  • 31
    • 30044436689 scopus 로고    scopus 로고
    • A therapeutic aptamer inhibits angiogenesis by specifically targeting the heparin binding domain of VEGF165
    • Lee J.-H., Canny M.D., De Erkenez A., Krilleke D., Ng Y.-S., Shima D.T., et al. A therapeutic aptamer inhibits angiogenesis by specifically targeting the heparin binding domain of VEGF165. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:18902-18907.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18902-18907
    • Lee, J.-H.1    Canny, M.D.2    De Erkenez, A.3    Krilleke, D.4    Ng, Y.-S.5    Shima, D.T.6
  • 32
    • 0030801996 scopus 로고    scopus 로고
    • Expression of basic fibroblast growth factor (FGF-2)-associated with tumour proliferation in human pancreatic carcinoma
    • Yamazaki K., Nagao T., Yamaguchi T., Saisho H., Kondo Y. Expression of basic fibroblast growth factor (FGF-2)-associated with tumour proliferation in human pancreatic carcinoma. Virchows Arch. 1997, 431:95-101.
    • (1997) Virchows Arch. , vol.431 , pp. 95-101
    • Yamazaki, K.1    Nagao, T.2    Yamaguchi, T.3    Saisho, H.4    Kondo, Y.5
  • 33
    • 53449095951 scopus 로고    scopus 로고
    • Comparison of bevacizumab, ranibizumab, and pegaptanib in vitro: efficiency and possible additional pathways
    • Klettner A., Roider J. Comparison of bevacizumab, ranibizumab, and pegaptanib in vitro: efficiency and possible additional pathways. Investiga. Ophthalmol. Vis. Sci. 2008, 49:4523.
    • (2008) Investiga. Ophthalmol. Vis. Sci. , vol.49 , pp. 4523
    • Klettner, A.1    Roider, J.2
  • 34
    • 78149441693 scopus 로고    scopus 로고
    • Regulation of pathologic retinal angiogenesis in mice and inhibition of VEGF-VEGFR2 binding by soluble heparan sulfate
    • Nishiguchi K.M., Kataoka K., Kachi S., Komeima K., Terasaki H. Regulation of pathologic retinal angiogenesis in mice and inhibition of VEGF-VEGFR2 binding by soluble heparan sulfate. PLoS One 2010, 5.
    • (2010) PLoS One , vol.5
    • Nishiguchi, K.M.1    Kataoka, K.2    Kachi, S.3    Komeima, K.4    Terasaki, H.5
  • 35
    • 0031046646 scopus 로고    scopus 로고
    • Growth factors in the extracellular matrix
    • Taipale J., Keski-Oja J. Growth factors in the extracellular matrix. FASEB J. 1997, 11:51-59.
    • (1997) FASEB J. , vol.11 , pp. 51-59
    • Taipale, J.1    Keski-Oja, J.2
  • 36
    • 20544455330 scopus 로고    scopus 로고
    • Bevacizumab (Avastin), a humanized anti-VEGF monoclonal antibody for cancer therapy
    • Ferrara N., Hillan K.J., Novotny W. Bevacizumab (Avastin), a humanized anti-VEGF monoclonal antibody for cancer therapy. Biochem. biophys. Res. Commun. 2005, 333:328-335.
    • (2005) Biochem. biophys. Res. Commun. , vol.333 , pp. 328-335
    • Ferrara, N.1    Hillan, K.J.2    Novotny, W.3


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