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Volumn 154, Issue , 2017, Pages 39-46

Neonatal Fc receptor FcRn is involved in intracellular transport of the Fc fusion protein aflibercept and its transition through retinal endothelial cells

Author keywords

Aflibercept; Fc fusion protein; IgG; Internalization; Neonatal Fc receptor; Retinal endothelial cells; Transcytosis; Transport

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; AFLIBERCEPT; FC RECEPTOR; IMMUNOGLOBULIN G; NEONATAL FC RECEPTOR; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN A; PROTEIN G; UNCLASSIFIED DRUG; FC RECEPTOR, NEONATAL; HLA ANTIGEN CLASS 1; HYBRID PROTEIN; RNA; VASCULOTROPIN RECEPTOR;

EID: 84994899510     PISSN: 00144835     EISSN: 10960007     Source Type: Journal    
DOI: 10.1016/j.exer.2016.11.007     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 0035113258 scopus 로고    scopus 로고
    • Expression of functionally active FcRn and the differentiated bidirectional transport of IgG in human placental endothelial cells
    • Antohe, F., Rădulescu, L., Gafencu, A., Gheţie, V., Simionescu, M., Expression of functionally active FcRn and the differentiated bidirectional transport of IgG in human placental endothelial cells. Hum. Immunol. 62 (2001), 93–105, 10.1016/S0198-8859(00)00244-5.
    • (2001) Hum. Immunol. , vol.62 , pp. 93-105
    • Antohe, F.1    Rădulescu, L.2    Gafencu, A.3    Gheţie, V.4    Simionescu, M.5
  • 3
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • Burmeister, W.P., Huber, A.H., Bjorkman, P.J., Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature 372 (1994), 379–383.
    • (1994) Nature , vol.372 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 4
    • 84919935824 scopus 로고    scopus 로고
    • Bovine FcRn-mediated human immunoglobulin G transfer across the milk-blood barrier in transgenic mice
    • Cui, D., Zhang, L., Li, J., Zhao, Y., Hu, X., Dai, Y., Zhang, R., Li, N., Bovine FcRn-mediated human immunoglobulin G transfer across the milk-blood barrier in transgenic mice. PLoS One, 9, 2014, e115972, 10.1371/journal.pone.0115972.
    • (2014) PLoS One , vol.9 , pp. e115972
    • Cui, D.1    Zhang, L.2    Li, J.3    Zhao, Y.4    Hu, X.5    Dai, Y.6    Zhang, R.7    Li, N.8
  • 5
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution
    • Deisenhofer, J., Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution. Biochemistry 20 (1981), 2361–2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 6
    • 33644647358 scopus 로고    scopus 로고
    • Generation and characterization of iBREC: novel hTERT-immortalized bovine retinal endothelial cells
    • Deissler, H., Deissler, H., Lang, G.K., Lang, G.E., Generation and characterization of iBREC: novel hTERT-immortalized bovine retinal endothelial cells. Int. J. Mol. Med. 15 (2005), 65–70, 10.3892/ijmm.16.1.65.
    • (2005) Int. J. Mol. Med. , vol.15 , pp. 65-70
    • Deissler, H.1    Deissler, H.2    Lang, G.K.3    Lang, G.E.4
  • 8
    • 79960620834 scopus 로고    scopus 로고
    • Inhibition of VEGF is sufficient to completely restore barrier malfunction induced by growth factors in microvascular retinal endothelial cells
    • Deissler, H.L., Deissler, H., Lang, G.E., Inhibition of VEGF is sufficient to completely restore barrier malfunction induced by growth factors in microvascular retinal endothelial cells. Br. J. Ophthalmol. 95 (2011), 1151–1156, 10.1136/bjo.2010.192229.
    • (2011) Br. J. Ophthalmol. , vol.95 , pp. 1151-1156
    • Deissler, H.L.1    Deissler, H.2    Lang, G.E.3
  • 9
    • 84862847224 scopus 로고    scopus 로고
    • Actions of bevacizumab and ranibizumab on microvascular retinal endothelial cells: similarities and differences
    • Deissler, H.L., Deissler, H., Lang, G.E., Actions of bevacizumab and ranibizumab on microvascular retinal endothelial cells: similarities and differences. Br. J. Ophthalmol. 96 (2012), 1023–1028, 10.1136/bjophthalmol-2012-301677.
    • (2012) Br. J. Ophthalmol. , vol.96 , pp. 1023-1028
    • Deissler, H.L.1    Deissler, H.2    Lang, G.E.3
  • 10
    • 84882800599 scopus 로고    scopus 로고
    • VEGF but not PlGF disturbs the barrier of retinal endothelial cells
    • Deissler, H.L., Lang, G.K., Lang, G.E., VEGF but not PlGF disturbs the barrier of retinal endothelial cells. Exp. Eye Res. 115 (2013), 162–171, 10.1016/j.exer.2013.07.018.
    • (2013) Exp. Eye Res. , vol.115 , pp. 162-171
    • Deissler, H.L.1    Lang, G.K.2    Lang, G.E.3
  • 11
    • 84896968297 scopus 로고    scopus 로고
    • Capacity of aflibercept to counteract VEGF-stimulated abnormal behavior of retinal microvascular endothelial cells
    • Deissler, H.L., Lang, G.K., Lang, G.E., Capacity of aflibercept to counteract VEGF-stimulated abnormal behavior of retinal microvascular endothelial cells. Exp. Eye Res. 122 (2014), 20–31, 10.1016/j.exer.2014.02.024.
    • (2014) Exp. Eye Res. , vol.122 , pp. 20-31
    • Deissler, H.L.1    Lang, G.K.2    Lang, G.E.3
  • 12
    • 84945300064 scopus 로고    scopus 로고
    • Internalization of bevacizumab by retinal endothelial cells and its intracellular fate: evidence for an involvement of the neonatal Fc receptor
    • Deissler, H.L., Lang, G.K., Lang, G.E., Internalization of bevacizumab by retinal endothelial cells and its intracellular fate: evidence for an involvement of the neonatal Fc receptor. Exp. Eye Res. 143 (2016), 49–59, 10.1016/j.exer.2015.10.007.
    • (2016) Exp. Eye Res. , vol.143 , pp. 49-59
    • Deissler, H.L.1    Lang, G.K.2    Lang, G.E.3
  • 13
    • 84956559152 scopus 로고    scopus 로고
    • The role of Fc-receptors in the uptake and transport of therapeutic antibodies in the retinal pigment epithelium
    • Dithmer, M., Hattermann, K., Pomarius, P., Aboul Naga, S.H., Meyer, T., Mentlein, R., Roider, J., Klettner, A., The role of Fc-receptors in the uptake and transport of therapeutic antibodies in the retinal pigment epithelium. Exp. Eye Res. 145 (2016), 187–205, 10.1016/j.exer.2015.12.013.
    • (2016) Exp. Eye Res. , vol.145 , pp. 187-205
    • Dithmer, M.1    Hattermann, K.2    Pomarius, P.3    Aboul Naga, S.H.4    Meyer, T.5    Mentlein, R.6    Roider, J.7    Klettner, A.8
  • 15
    • 33749632278 scopus 로고    scopus 로고
    • Development of ranibizumab, an anti-vascular endothelial growth factor antigen binding fragment, as therapy for neovascular age-related macular degeneration
    • Ferrara, N., Damico, L., Shams, N., Lowman, H., Kim, R., Development of ranibizumab, an anti-vascular endothelial growth factor antigen binding fragment, as therapy for neovascular age-related macular degeneration. Retina 26 (2006), 859–870, 10.1097/01.iae.0000242842.14624.e7.
    • (2006) Retina , vol.26 , pp. 859-870
    • Ferrara, N.1    Damico, L.2    Shams, N.3    Lowman, H.4    Kim, R.5
  • 16
    • 59449083582 scopus 로고    scopus 로고
    • Neonatal Fc receptor mediates internalization of Fc in transfected human endothelial cells
    • Goebl, N.A., Babbey, C.M., Datta-Mannan, A., Witcher, D.R., Wroblewski, V.J., Dunn, K.W., Neonatal Fc receptor mediates internalization of Fc in transfected human endothelial cells. Mol. Biol. Cell. 19 (2008), 5490–5505, 10.1091/mbc.E07-02-0101.
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 5490-5505
    • Goebl, N.A.1    Babbey, C.M.2    Datta-Mannan, A.3    Witcher, D.R.4    Wroblewski, V.J.5    Dunn, K.W.6
  • 18
    • 0033668064 scopus 로고    scopus 로고
    • VEGF-A induced hyperpermeability of blood-retinal barrier endothelium in vivo is predominantly associated with pinocytotic vesicular transport and not with formation of fenestrations
    • Hofman, P., Blaauwgeers, H.G., Tolentino, M.J., Adamis, A.P., Nunes Cardozo, B.J., Vrensen, G.F., Schlingemann, R.O., VEGF-A induced hyperpermeability of blood-retinal barrier endothelium in vivo is predominantly associated with pinocytotic vesicular transport and not with formation of fenestrations. Curr. Eye Res. 21 (2000), 637–645.
    • (2000) Curr. Eye Res. , vol.21 , pp. 637-645
    • Hofman, P.1    Blaauwgeers, H.G.2    Tolentino, M.J.3    Adamis, A.P.4    Nunes Cardozo, B.J.5    Vrensen, G.F.6    Schlingemann, R.O.7
  • 20
    • 77955259013 scopus 로고    scopus 로고
    • Comparison of FcRn- and pIgR-mediated transport in MDCK cells by fluorescence confocal microscopy
    • Jerdeva, G.V., Tesar, D.B., Huey-Tubman, K.E., Ladinsky, M.S., Fraser, S.E., Bjorkman, P.J., Comparison of FcRn- and pIgR-mediated transport in MDCK cells by fluorescence confocal microscopy. Traffic 11 (2010), 1205–1220, 10.1111/j.1600-0854.2010.01083.x.
    • (2010) Traffic , vol.11 , pp. 1205-1220
    • Jerdeva, G.V.1    Tesar, D.B.2    Huey-Tubman, K.E.3    Ladinsky, M.S.4    Fraser, S.E.5    Bjorkman, P.J.6
  • 21
    • 84901606839 scopus 로고    scopus 로고
    • Different effects of intravitreally injected ranibizumab and aflibercept on retinal and choroidal tissues of monkey eyes
    • Julien, S., Biesemeier, A., Taubitz, T., Schraermeyer, U., Different effects of intravitreally injected ranibizumab and aflibercept on retinal and choroidal tissues of monkey eyes. Br. J. Ophthalmol. 98 (2014), 813–825, 10.1136/bjophthalmol-2013-304019.
    • (2014) Br. J. Ophthalmol. , vol.98 , pp. 813-825
    • Julien, S.1    Biesemeier, A.2    Taubitz, T.3    Schraermeyer, U.4
  • 23
    • 0034651936 scopus 로고    scopus 로고
    • Cloning and characterization of the bovine MHC class I-like Fc receptor
    • Kacskovics, I., Wu, Z., Simister, N.E., Frenyó, L.V., Hammarström, L., Cloning and characterization of the bovine MHC class I-like Fc receptor. J. Immunol. 164 (2000), 1889–1897.
    • (2000) J. Immunol. , vol.164 , pp. 1889-1897
    • Kacskovics, I.1    Wu, Z.2    Simister, N.E.3    Frenyó, L.V.4    Hammarström, L.5
  • 26
    • 77649253359 scopus 로고    scopus 로고
    • FcRn receptor-mediated pharmacokinetics of therapeutic IgG in the eye
    • Kim, H., Robinson, S.B., Csaky, K.G., FcRn receptor-mediated pharmacokinetics of therapeutic IgG in the eye. Mol. Vis. 15 (2009), 2803–2812.
    • (2009) Mol. Vis. , vol.15 , pp. 2803-2812
    • Kim, H.1    Robinson, S.B.2    Csaky, K.G.3
  • 27
    • 84885022310 scopus 로고    scopus 로고
    • Two-year safety and efficacy of ranibizumab 0.5 mg in diabetic macular edema: interim analysis of the RESTORE extension study
    • Lang, G.E., Berta, A., Eldem, B.M., Simader, C., Sharp, D., Holz, F.G., Sutter, F., Gerstner, O., Mitchell, P., RESTORE Extension Study Group. Two-year safety and efficacy of ranibizumab 0.5 mg in diabetic macular edema: interim analysis of the RESTORE extension study. Ophthalmology 120 (2013), 2004–2012, 10.1016/j.ophtha.2013.02.019.
    • (2013) Ophthalmology , vol.120 , pp. 2004-2012
    • Lang, G.E.1    Berta, A.2    Eldem, B.M.3    Simader, C.4    Sharp, D.5    Holz, F.G.6    Sutter, F.7    Gerstner, O.8    Mitchell, P.9
  • 28
    • 0034058526 scopus 로고    scopus 로고
    • Bidirectional transcytosis of IgG by the rat neonatal Fc receptor expressed in a rat kidney cell line: a system to study protein transport across epithelia
    • McCarthy, K.M., Yoong, Y., Simister, N.E., Bidirectional transcytosis of IgG by the rat neonatal Fc receptor expressed in a rat kidney cell line: a system to study protein transport across epithelia. J. Cell Sci. 113 (2000), 1277–1285.
    • (2000) J. Cell Sci. , vol.113 , pp. 1277-1285
    • McCarthy, K.M.1    Yoong, Y.2    Simister, N.E.3
  • 29
    • 0035210960 scopus 로고    scopus 로고
    • Differences in promiscuity for antibody-FcRn interactions across species: implications for therapeutic antibodies
    • Ober, R.J., Radu, C.G., Ghetie, V., Ward, E.S., Differences in promiscuity for antibody-FcRn interactions across species: implications for therapeutic antibodies. Int. Immunol. 13 (2001), 1551–1559, 10.1093/intimm/13.12.1551.
    • (2001) Int. Immunol. , vol.13 , pp. 1551-1559
    • Ober, R.J.1    Radu, C.G.2    Ghetie, V.3    Ward, E.S.4
  • 30
    • 3343010237 scopus 로고    scopus 로고
    • Exocytosis of IgG as mediated by the receptor, FcRn: an analysis at the single-molecule level
    • Ober, R.J., Martinez, C., Lai, X., Zhou, J., Ward, E.S., Exocytosis of IgG as mediated by the receptor, FcRn: an analysis at the single-molecule level. Proc. Natl. Acad. Sci. U. S. A. 101 (2004), 11076–11081, 10.1073/pnas.0402970101.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11076-11081
    • Ober, R.J.1    Martinez, C.2    Lai, X.3    Zhou, J.4    Ward, E.S.5
  • 31
    • 0030856731 scopus 로고    scopus 로고
    • Humanization of an anti-vascular endothelial growth factor monoclonal antibody for the therapy of solid tumors and other disorders
    • Presta, L.G., Chen, H., O'Connor, S.J., Chisholm, V., Meng, Y.G., Krummen, L., Winkler, M., Ferrara, N., Humanization of an anti-vascular endothelial growth factor monoclonal antibody for the therapy of solid tumors and other disorders. Cancer Res. 57 (1997), 4593–4599.
    • (1997) Cancer Res. , vol.57 , pp. 4593-4599
    • Presta, L.G.1    Chen, H.2    O'Connor, S.J.3    Chisholm, V.4    Meng, Y.G.5    Krummen, L.6    Winkler, M.7    Ferrara, N.8
  • 33
    • 0028467948 scopus 로고
    • Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand
    • Raghavan, M., Chen, M.Y., Gastinel, L.N., Bjorkman, P.J., Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand. Immunity 1 (1994), 303–315, 10.1016/1074-7613(94)90082-5.
    • (1994) Immunity , vol.1 , pp. 303-315
    • Raghavan, M.1    Chen, M.Y.2    Gastinel, L.N.3    Bjorkman, P.J.4
  • 34
    • 84926670297 scopus 로고    scopus 로고
    • Unraveling the interaction between FcRn and albumin: opportunities for design of albumin-based therapeutics
    • Sand, K.M., Bern, M., Nilsen, J., Noordzij, H.T., Sandlie, I., Andersen, J.T., Unraveling the interaction between FcRn and albumin: opportunities for design of albumin-based therapeutics. Front. Immunol., 5, 2015, 682, 10.3389/fimmu.2014.00682.
    • (2015) Front. Immunol. , vol.5 , pp. 682
    • Sand, K.M.1    Bern, M.2    Nilsen, J.3    Noordzij, H.T.4    Sandlie, I.5    Andersen, J.T.6
  • 35
    • 0029644247 scopus 로고
    • Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG
    • Sauer-Eriksson, A.E., Kleywegt, G.J., Uhlen, M., Jones, T.A., Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure 3 (1995), 265–278.
    • (1995) Structure , vol.3 , pp. 265-278
    • Sauer-Eriksson, A.E.1    Kleywegt, G.J.2    Uhlen, M.3    Jones, T.A.4
  • 36
    • 84866558151 scopus 로고    scopus 로고
    • Formation of immune complexes and thrombotic microangiopathy after intravitreal injection of bevacizumab in the primate eye
    • Schraermeyer, U., Julien, S., Formation of immune complexes and thrombotic microangiopathy after intravitreal injection of bevacizumab in the primate eye. Graefes Arch. Clin. Exp. Ophthalmol. 250 (2012), 1303–1313, 10.1007/s00417-012-2055-z.
    • (2012) Graefes Arch. Clin. Exp. Ophthalmol. , vol.250 , pp. 1303-1313
    • Schraermeyer, U.1    Julien, S.2
  • 37
    • 81355127555 scopus 로고    scopus 로고
    • Comparison of choroidal and retinal endothelial cells: characteristics and response to VEGF-isoforms and anti-VEGF treatment
    • Stewart, E.A., Samaranayake, G.J., Browning, A.C., Hopkinson, A., Amoaku, W.M., Comparison of choroidal and retinal endothelial cells: characteristics and response to VEGF-isoforms and anti-VEGF treatment. Exp. Eye Res. 93 (2011), 761–766, 10.1016/j.exer.2011.09.010.
    • (2011) Exp. Eye Res. , vol.93 , pp. 761-766
    • Stewart, E.A.1    Samaranayake, G.J.2    Browning, A.C.3    Hopkinson, A.4    Amoaku, W.M.5
  • 38
    • 84859883103 scopus 로고    scopus 로고
    • A dynamic real-time method for monitoring epithelial barrier function in vitro
    • Sun, M., Fu, H., Cheng, H., Cao, Q., Zhao, Y., Mou, X., Zhang, X., Liu, X., Ke, Y., A dynamic real-time method for monitoring epithelial barrier function in vitro. Anal. Biochem. 425 (2012), 96–103, 10.1016/j.ab.2012.03.010.
    • (2012) Anal. Biochem. , vol.425 , pp. 96-103
    • Sun, M.1    Fu, H.2    Cheng, H.3    Cao, Q.4    Zhao, Y.5    Mou, X.6    Zhang, X.7    Liu, X.8    Ke, Y.9
  • 39
    • 0037325779 scopus 로고    scopus 로고
    • Evidence to support the cellular mechanism involved in serum IgG homeostasis in humans
    • Ward, E.S., Zhou, J., Ghetie, V., Ober, R.J., Evidence to support the cellular mechanism involved in serum IgG homeostasis in humans. Int. Immunol. 15 (2003), 187–195.
    • (2003) Int. Immunol. , vol.15 , pp. 187-195
    • Ward, E.S.1    Zhou, J.2    Ghetie, V.3    Ober, R.J.4
  • 40
    • 16344376889 scopus 로고    scopus 로고
    • From sorting endosomes to exocytosis: association of Rab4 and Rab11 GTPases with the Fc receptor, FcRn, during recycling
    • Ward, E.S., Martinez, C., Vaccaro, C., Zhou, J., Tang, Q., Ober, R.J., From sorting endosomes to exocytosis: association of Rab4 and Rab11 GTPases with the Fc receptor, FcRn, during recycling. Mol. Biol. Cell. 16 (2005), 2028–2038, 10.1091/mbc.E04-08-0735.
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 2028-2038
    • Ward, E.S.1    Martinez, C.2    Vaccaro, C.3    Zhou, J.4    Tang, Q.5    Ober, R.J.6
  • 41
    • 0034657794 scopus 로고    scopus 로고
    • The IgG Fc contains distinct Fc receptor (FcR) binding sites: the leukocyte receptors Fc gamma RI and Fc gamma RIIa bind to a region in the Fc distinct from that recognized by neonatal FcR and protein A
    • Wines, B.D., Powell, M.S., Parren, P.W., Barnes, N., Hogarth, P.M., The IgG Fc contains distinct Fc receptor (FcR) binding sites: the leukocyte receptors Fc gamma RI and Fc gamma RIIa bind to a region in the Fc distinct from that recognized by neonatal FcR and protein A. J. Immunol. 164 (2000), 5313–5318, 10.4049/jimmunol.164.10.5313.
    • (2000) J. Immunol. , vol.164 , pp. 5313-5318
    • Wines, B.D.1    Powell, M.S.2    Parren, P.W.3    Barnes, N.4    Hogarth, P.M.5
  • 42
    • 84955214590 scopus 로고    scopus 로고
    • Safety of monoclonal antibodies and related therapeutic proteins for the treatment of neovascular macular degeneration: addressing outstanding issues
    • Ziemssen, F., Sobolewska, B., Deissler, H.L., Deissler, H., Safety of monoclonal antibodies and related therapeutic proteins for the treatment of neovascular macular degeneration: addressing outstanding issues. Exp. Opion. Drug Saf. 15 (2016), 75–87, 10.1517/14740338.2016.1121232.
    • (2016) Exp. Opion. Drug Saf. , vol.15 , pp. 75-87
    • Ziemssen, F.1    Sobolewska, B.2    Deissler, H.L.3    Deissler, H.4


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