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Title: IgG Fc domains that bind C1q but not effector Fcγ receptors delineate the importance of complement-mediated effector functions


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Lee, Chang-Han, Romain, Gabrielle, Yan, Wupeng, Watanabe, Makiko, Charab, Wissam, Todorova, Biliana, Lee, Jiwon, Triplett, Kendra, Donkor, Moses, Lungu, Oana I., Lux, Anja, Marshall, Nicholas, Lindorfer, Margaret A., Goff, Odile Richard-Le, Balbino, Bianca, Kang, Tae Hyun, Tanno, Hidetaka, Delidakis, George, Alford, Corrine, Taylor, Ronald P., Nimmerjahn, Falk, Varadarajan, Navin, Bruhns, Pierre, Zhang, Yan Jessie, and Georgiou, George. IgG Fc domains that bind C1q but not effector Fcγ receptors delineate the importance of complement-mediated effector functions. United States: N. p., 2017. Web. doi:10.1038/ni.3770.
Lee, Chang-Han, Romain, Gabrielle, Yan, Wupeng, Watanabe, Makiko, Charab, Wissam, Todorova, Biliana, Lee, Jiwon, Triplett, Kendra, Donkor, Moses, Lungu, Oana I., Lux, Anja, Marshall, Nicholas, Lindorfer, Margaret A., Goff, Odile Richard-Le, Balbino, Bianca, Kang, Tae Hyun, Tanno, Hidetaka, Delidakis, George, Alford, Corrine, Taylor, Ronald P., Nimmerjahn, Falk, Varadarajan, Navin, Bruhns, Pierre, Zhang, Yan Jessie, & Georgiou, George. IgG Fc domains that bind C1q but not effector Fcγ receptors delineate the importance of complement-mediated effector functions. United States. doi:10.1038/ni.3770.
Lee, Chang-Han, Romain, Gabrielle, Yan, Wupeng, Watanabe, Makiko, Charab, Wissam, Todorova, Biliana, Lee, Jiwon, Triplett, Kendra, Donkor, Moses, Lungu, Oana I., Lux, Anja, Marshall, Nicholas, Lindorfer, Margaret A., Goff, Odile Richard-Le, Balbino, Bianca, Kang, Tae Hyun, Tanno, Hidetaka, Delidakis, George, Alford, Corrine, Taylor, Ronald P., Nimmerjahn, Falk, Varadarajan, Navin, Bruhns, Pierre, Zhang, Yan Jessie, and Georgiou, George. Mon . "IgG Fc domains that bind C1q but not effector Fcγ receptors delineate the importance of complement-mediated effector functions". United States. doi:10.1038/ni.3770.
@article{osti_1433698,
title = {IgG Fc domains that bind C1q but not effector Fcγ receptors delineate the importance of complement-mediated effector functions},
author = {Lee, Chang-Han and Romain, Gabrielle and Yan, Wupeng and Watanabe, Makiko and Charab, Wissam and Todorova, Biliana and Lee, Jiwon and Triplett, Kendra and Donkor, Moses and Lungu, Oana I. and Lux, Anja and Marshall, Nicholas and Lindorfer, Margaret A. and Goff, Odile Richard-Le and Balbino, Bianca and Kang, Tae Hyun and Tanno, Hidetaka and Delidakis, George and Alford, Corrine and Taylor, Ronald P. and Nimmerjahn, Falk and Varadarajan, Navin and Bruhns, Pierre and Zhang, Yan Jessie and Georgiou, George},
abstractNote = {},
doi = {10.1038/ni.3770},
journal = {Nature Immunology},
number = 8,
volume = 18,
place = {United States},
year = {Mon Jun 12 00:00:00 EDT 2017},
month = {Mon Jun 12 00:00:00 EDT 2017}
}
  • Two distinct classes of IgG Fc receptors (FcR) on cells of a human monocytic line (U937) by analyzing the direct binding of murine IgG subclasses in medium of low ionic strength. Four lines of evidence support this contention. (1) The binding of aggregated murine IgB2b (AggmIgG2b) to U937 and Daudi cells was enhanced at low ionic strength, whereas monomeric murine IgG2a (mIgG2a) did not bind to Daudi cells and its high affinity binding to U937 cells was unaffected by changes in ionic strength. (2) Double reciprocal inhibition experiments with U937 cells indicated that the binding of both ligands was inhibitedmore » 30 to 135 times more efficiently by the homologous ligand than by the heterologous one. That is, the binding of /sup 125/I-AggmIgG2b was inhibited 50% by 3.5 ..mu..g/ml of AggmIgG2b and 100 ..mu..g/ml of mIgG2a. Similarly, the binding of /sup 125/I-mIgG2a was inhibited 50% by 2.5 ..mu..g/ml of mIgG2a and only 44% by 243 ..mu..g/ml of AggmIgG2b. (3) A monoclonal antibody of the IgG2b subclass raised against an IgG FcR on K562 cells inhibited binding to U937 cells of AggmIgG2b but not of mIgG2a. (4) Trypsinization of U937 cells abrogated by 32% the binding of mIgG2a but did not affect the binding of AggmIgG2b. Human IgG inhibited binding of both AggmIgG2b and mIgG2a t U937 cells. They propose that the newly recognized FcR that binds AggmIgG2b is the human homologue of the murine macrophage IgG2b/1 FcR (FcRII), and that the previously described 72,000 dalton high-affinity FcR on U937 cells that binds mIgG2a is the human equivalent of the murine macrophage IgG2a FcR (FcRI).« less
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