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Автор: Grafiati

Опубліковано: 20 квітня 2024

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1

Fridén, Barbro E., Ricardo Makiya, Berith M. Nilsson, Stig Holm, and Torgny I. Stigbrand. "The human placental immunoglobulin G receptor and immunoglobulin G transport." American Journal of Obstetrics and Gynecology 171, no. 1 (July 1994): 258–63. http://dx.doi.org/10.1016/0002-9378(94)90479-0.

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2

Campos-Neto, Antonio, Isabelle Suffia, Karen A. Cavassani, Shyian Jen, Kay Greeson, Pamela Ovendale, João S. Silva, Steven G. Reed, and Yasir A. W. Skeiky. "Cloning and Characterization of a Gene Encoding an Immunoglobulin-Binding Receptor on the Cell Surface of Some Members of the Family Trypanosomatidae." Infection and Immunity 71, no. 9 (September 2003): 5065–76. http://dx.doi.org/10.1128/iai.71.9.5065-5076.2003.

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ABSTRACT Several members of the Trypanosomatidae family, when freshly isolated from their mammalian hosts, have immunoglobulins adsorbed to their cell surfaces. However, a significant portion of these antibody molecules is not parasite specific, i.e., the immunoglobulins are bound to the parasite's cell surface molecules via noncognitive interactions. It has been proposed that this noncognitive adsorption of immunoglobulins to the parasite is mediated by an Fc-like receptor present in several members of the Trypanosomatidae family. However, the molecular identification of this receptor has never been defined. Here, we describe the cloning of a gene encoding a protein that might represent this molecule. The gene, named Lmsp1, was cloned by screening a Leishmania major cDNA expression library using a rabbit antiserum. Lmsp1 is present in both Leishmania and Trypanosoma and is expressed in all developmental stages of these parasites. The predicted protein has a molecular mass of 16.6 kDa and contains an RGD sequence starting at residue 104 and three cysteine residues at positions 55, 74, and 116. The purified recombinant protein strongly binds to normal immunoglobulins of various animal species (humans, rabbits, sheep, goats, guinea pigs, donkeys, rats, and mice) and the binding to human immunoglobulins appears to be immunoglobulin G (IgG) and IgM isotype specific. Moreover, Lmsp1 binds to both purified Fc and Fab fragments of IgG from both humans and rabbits. The mapping of the Lmsp1 epitopes that bind human IgG revealed that different sequences of the molecule bind to Fc or Fab. In addition, fluorescence-activated cell sorter analyses with a specific rabbit anti-Lmsp1 antiserum showed that Lmsp1 is associated with the parasite's cell surface. Finally, inhibition experiments point to an active role of this molecule in the immunoglobulin-mediated attachment and penetration of Trypanosoma cruzi in its macrophage host cells, thus suggesting that Lmsp1 is a putative Trypanosomatidae immunoglobulin receptor.

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3

Hansen, Gert H., Lise-Lotte Niels-Christiansen, Lissi Immerdal, and E. Michael Danielsen. "Antibodies in the small intestine: mucosal synthesis and deposition of anti-glycosyl IgA, IgM, and IgG in the enterocyte brush border." American Journal of Physiology-Gastrointestinal and Liver Physiology 291, no. 1 (July 2006): G82—G90. http://dx.doi.org/10.1152/ajpgi.00021.2006.

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Synthesis and deposition of immunoglobulins in the brush border was studied in organ-cultured pig small intestinal mucosal explants. Surprisingly, comparable amounts of IgM and IgA were synthesized during a 6-h pulse, and also newly made IgG was detected in media and explants, including the microvillar fraction. For IgA and IgM, this subcellular distribution is consistent with basolateral-to-apical transcytosis, mediated by the polymeric immunoglobulin receptor. IgG is a ligand for the Fc receptor FcRn, and β2-microglobulin, the light chain of FcRn, coclustered in immunogold double labeling with IgG in subapical endosomes and in the basolateral membrane of enterocytes. In addition, β2-microglobulin was copurified with IgG on protein G-Sepharose. Apical endocytosis of IgG, as judged by internalization of fluorescent protein G, was not detectable except in a few isolated cells. This suggests that IgG in the adult small intestine is transported across the enterocyte mainly in the basolateral to apical direction. Significant fractions of all immunoglobulins bound to lactoseagarose, indicating that “anti-glycosyl” antibodies, raised against commensal gut bacteria, are synthesized locally in the small intestine. By partial deposition in the brush border, these antibodies therefore may have a protective function by preventing lectin-like pathogens from gaining access to the brush border surface.

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4

Peng, Xu, Xiao-Bi Xie, Hong Tan, Dan Zhang, Bo-Tao Jiang, Jie Liu, Shuang Li, Ya-Rui Chen, and Tao-Yang Xie. "Effects of Plasma Exchange Combined with Immunoglobulin Therapy on Consciousness, Immune Function, and Prognosis in Patients with Myasthenia Gravis Crisis: A Prospective Randomized Test." Computational and Mathematical Methods in Medicine 2022 (June 30, 2022): 1–7. http://dx.doi.org/10.1155/2022/7796833.

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Background. Myasthenia gravis (MG) is an acquired autoimmune disease. The main clinical features of MG are skeletal muscle fatigue and pathological fatigue, which worsen at night or after fatigue, such as dyspnea, dysphagia, and systemic weakness. Plasma exchange (PE) is often used in patients with acute exacerbation of MG. Intravenous immunoglobulin (IVIG) is a collection of immunoglobulins from thousands of donors. IVIG can replace a variety of immunosuppressants or PE. However, the effect of PE or IVIG on patients’ consciousness, immune function, and prognosis is not clear. Objective. A prospective randomized test of the effects of PE combined with immunoglobulin on consciousness, immune function, and prognosis in patients with myasthenia gravis crisis (MGC). Methods. Sixty patients with MGC treated from February 2019 to April 2021 were enrolled in our hospital. The cases who received PE were set as the PE group, and those who received PE combined with immunoglobulin were set as the PE+immunoglobulin group. The efficacy, clinical score, state of consciousness, immune function, acetylcholine receptor antibody (AChR-Ab), lymphocyte (LYM), albumin (ALB) levels, and the incidence of adverse reactions were compared. Results. The improvement rate was 100.005% in the treatment group and 83.33% in the PE group. After treatment, the clinical score of the PE+immunoglobulin group was lower than that of the PE group, and the clinical relative score of the PE+immunoglobulin group was higher than that of the PE group ( P < 0.05 ). The number of conscious people in the PE+immunoglobulin group was more than that in the PE group ( P < 0.05 ). Immunoglobulin A, immunoglobulin M, immunoglobulin G, and immunoglobulin G in the PE+immunoglobulin group were higher than those in the PE group ( P < 0.05 ). The levels of AChR-Ab and ALB in the PE+immunoglobulin group were higher than those in the PE group, while the level of LYM in the PE+immunoglobulin group was lower than that in the PE group. The incidence of skin system, gastrointestinal system, nervous system, and systemic damage in the PE+immunoglobulin group was lower than that in the PE group ( P < 0.05 ). Conclusion. The treatment of MGC with PE combined with immunoglobulin can not only effectively enhance the consciousness and immune function of patients but also effectively promote the prognosis, and the safety of treatment can be guaranteed.

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5

Steiner, M., and E. F. Lüscher. "Identification of the immunoglobulin G receptor of human platelets." Journal of Biological Chemistry 261, no. 16 (June 1986): 7230–35. http://dx.doi.org/10.1016/s0021-9258(17)38379-5.

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6

Nakamura, Kazuhiro, Hirokazu Hirai, Takashi Torashima, Taisuke Miyazaki, Hiromichi Tsurui, Yan Xiu, Mareki Ohtsuji, et al. "CD3 and Immunoglobulin G Fc Receptor Regulate Cerebellar Functions." Molecular and Cellular Biology 27, no. 14 (May 14, 2007): 5128–34. http://dx.doi.org/10.1128/mcb.01072-06.

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ABSTRACT The immune and nervous systems display considerable overlap in their molecular repertoire. Molecules originally shown to be critical for immune responses also serve neuronal functions that include normal brain development, neuronal differentiation, synaptic plasticity, and behavior. We show here that FcγRIIB, a low-affinity immunoglobulin G Fc receptor, and CD3 are involved in cerebellar functions. Although membranous CD3 and FcγRIIB are crucial regulators on different cells in the immune system, both CD3ε and FcγRIIB are expressed on Purkinje cells in the cerebellum. Both CD3ε-deficient mice and FcγRIIB-deficient mice showed an impaired development of Purkinje neurons. In the adult, rotarod performance of these mutant mice was impaired at high speed. In the two knockout mice, enhanced paired-pulse facilitation of parallel fiber-Purkinje cell synapses was shared. These results indicate that diverse immune molecules play critical roles in the functional establishment in the cerebellum.

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7

Hibbs, M. L., L. Bonadonna, B. M. Scott, I. F. McKenzie, and P. M. Hogarth. "Molecular cloning of a human immunoglobulin G Fc receptor." Proceedings of the National Academy of Sciences 85, no. 7 (April 1, 1988): 2240–44. http://dx.doi.org/10.1073/pnas.85.7.2240.

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8

Luzi, G., and R. Ferrara. "Immunoregulation of Autoimmune Disorders: The Role of Intravenous Immunoglobulins." International Journal of Artificial Organs 16, no. 5_suppl (May 1993): 189–95. http://dx.doi.org/10.1177/039139889301605s43.

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Modified and intact immunoglobulin preparations are available for therapeutic use. The administration of intravenous immunoglobulins (IVI G) gave positive results in Primary Immunodeficiency Syndromes (PIS) (prophylaxis of viral and bacterial diseases), in treatment of secondary immunodeficiencies (hematologic malignancies, bone marrow transplantation), and in some infections. Adverse reactions have been reported during IVIG infusions, but they are rarely serious and do not represent limiting conditions for a short or long term therapy. After the original observation in thrombocytopenic purpura, IVIG have been used as immune modulators in various autoimmune related disorders. Various mechanisms of action are proposed: blockade and down regulation of phagocytic function via Fc receptor, regulation of idiotype-anti idiotype network, suppression of idiotype synthesis, T-B cell interference towards antigen presentation, increase in suppressor lymphocytes, IVIG-cytokine interaction.

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9

Lindroos, Jenny Linnea Victoria, Marte-Helene Bjørk, and Nils Erik Gilhus. "Transient Neonatal Myasthenia Gravis as a Common Complication of a Rare Disease: A Systematic Review." Journal of Clinical Medicine 13, no. 4 (February 17, 2024): 1136. http://dx.doi.org/10.3390/jcm13041136.

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Myasthenia gravis (MG) is a rare autoimmune disease. Transient neonatal myasthenia gravis (TNMG) is caused by pathogenic maternal autoantibodies that cross the placenta and disrupt signaling at the neuromuscular junction. This is a systematic review of this transient immunoglobulin G (IgG)-mediated disease. TNMG affects 10–20% of children born to mothers with MG. The severity of symptoms ranges from minor feeding difficulties to life-threatening respiratory weakness. Minor symptoms might go unnoticed but can still interfere with breastfeeding. Acetylcholine-esterase inhibitors and antibody-clearing therapies such as immunoglobulins can be used to treat TNMG, but most children do well with observation only. TNMG is self-limiting within weeks as circulating antibodies are naturally cleared from the blood. In rare cases, TNMG is associated with permanent skeletal malformations or permanent myopathy. The mother’s antibodies can also lead to spontaneous abortions. All healthcare professionals meeting pregnant or birthing women with MG or their neonates should be aware of TNMG. TNMG is hard to predict. Reoccurrence is common among siblings. Pre-pregnancy thymectomy and intravenous immunoglobulins during pregnancy reduce the risk. Neonatal fragment crystallizable receptor (FcRn) blocking drugs for MG might reduce TNMG risk.

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10

Ramos-Martínez, Ivan, Edgar Ramos-Martínez, Marco Cerbón, Armando Pérez-Torres, Laura Pérez-Campos Mayoral, María Teresa Hernández-Huerta, Margarito Martínez-Cruz, et al. "The Role of B Cell and T Cell Glycosylation in Systemic Lupus Erythematosus." International Journal of Molecular Sciences 24, no. 1 (January 3, 2023): 863. http://dx.doi.org/10.3390/ijms24010863.

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Glycosylation is a post-translational modification that affects the stability, structure, antigenicity and charge of proteins. In the immune system, glycosylation is involved in the regulation of ligand–receptor interactions, such as in B-cell and T-cell activating receptors. Alterations in glycosylation have been described in several autoimmune diseases, such as systemic lupus erythematosus (SLE), in which alterations have been found mainly in the glycosylation of B lymphocytes, T lymphocytes and immunoglobulins. In immunoglobulin G of lupus patients, a decrease in galactosylation, sialylation, and nucleotide fucose, as well as an increase in the N-acetylglucosamine bisector, are observed. These changes in glycoisolation affect the interactions of immunoglobulins with Fc receptors and are associated with pericarditis, proteinuria, nephritis, and the presence of antinuclear antibodies. In T cells, alterations have been described in the glycosylation of receptors involved in activation, such as the T cell receptor; these changes affect the affinity with their ligands and modulate the binding to endogenous lectins such as galectins. In T cells from lupus patients, a decrease in galectin 1 binding is observed, which could favor activation and reduce apoptosis. Furthermore, these alterations in glycosylation correlate with disease activity and clinical manifestations, and thus have potential use as biomarkers. In this review, we summarize findings on glycosylation alterations in SLE and how they relate to immune system defects and their clinical manifestations.

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11

HIRAYAMA, Kazuo. "Structural Characterization of Immune Components; Immunoglobulin G and Its Receptor." Journal of the Mass Spectrometry Society of Japan 48, no. 2 (2000): 101–7. http://dx.doi.org/10.5702/massspec.48.101.

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12

Nimmerjahn, F. "Divergent Immunoglobulin G Subclass Activity Through Selective Fc Receptor Binding." Science 310, no. 5753 (December 2, 2005): 1510–12. http://dx.doi.org/10.1126/science.1118948.

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13

Anderson, Clark, George Chacko, Jeanne Osborne та John Brandt. "The Fc Receptor for Immunoglobulin G (FcγRII) on Human Platelets". Seminars in Thrombosis and Hemostasis 21, № 01 (січень 1995): 1–9. http://dx.doi.org/10.1055/s-2007-1000374.

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14

Tonacchera, Massimo, Sabine Costagliola, Filomena Cetani, Jean Ducobu, Patrick Stordeur, Gilbert Vassart, and Marian Ludgate. "Patient with monoclonal gammopathy, thyrotoxicosis, pretibial myxedema and thyroid-associated ophthalmopathy; demonstration of direct binding of autoantibodies to the thyrotropin receptor." European Journal of Endocrinology 134, no. 1 (January 1996): 97–103. http://dx.doi.org/10.1530/eje.0.1340097.

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Tonacchera M. Costagliola S, Cetani F, Ducobu J. Stordeur P. Vassart G. Ludgate M. Patient with monoclonal gammopathy, thyrotoxicosis, pretibial myxedema and thyroid-associated ophthalmopathy: demonstration of direct binding of autoantibodies to the thyrotropin receptor. Eur J Endocrinol 1996:134:97–103. ISSN 0804–4643 We describe a patient with monoclonal gammopathy who subsequently developed thyrotoxicosis, pretibial myxedema and thyroid-associated ophthalmopathy. The pathogenesis of thyrotoxicosis in Graves' disease is due to the presence of autoantibodies that mimic the action of thyrotropin (TSH). called thyroid-stimulating antibodies (TS-ab): these antibodies may or may not inhibit the binding of TSH to the receptor (thyroid-binding inhibiting immunoglobulin, TBII). The patient's immunoglobulins were TS-ab positive and TBII negative when measured on CHO cells expressing the human TSH receptor. The pathogenetic link between the thyroid, orbit and skin is yet to be established but several candidate shared antigens have been proposed, including the TSH receptor itself. The monoclonal immunoglobulins were in evidence before the symptoms of pretibial myxedema, thyrotoxicosis and ophthalmopathy, In addition, the patient had no autoantibodies to thyroglobulin or thyroperoxidase, which are classic markers of thyroid autoimmunity. This combination led us to postulate that the monoclonal gammopathy could be the cause of all the observed pathology. One method to test this hypothesis would be to show that the monoclonal immunoglobulin is a TS-ab. Various methods were used to separate the monoclonal from the polyclonal components of the patient's serum. Preparative isoelectric focusing enabled us to obtain fractions containing only the monoclonal (as revealed by polyacrylamide gel electrophoresis), which were devoid of TS-ab activity (measured as cAMP accumulation in CHO cells expressing the human TSH receptor in a hypotonic bioassay). Subsequently, different oligoclonal fractions were shown to have varying degrees of TS-ab activity, with one fraction having faint biological activity and able to recognize a recombinant TSH receptor preparation in a Western blot. In conclusion, the monoclonal antibody does not seem to be responsible for the thyrotoxicosis, pretibial myxedema and ophthalmopathy. We confirm previous data showing that TSH receptor antibodies in patients with Graves' disease are heterogeneous in nature and we present the first demonstration of autoantibodies capable of binding the TSH receptor but devoid of TBII activity. Massimo Tonacchera, Institut de Recherche Interdisciplinaire, Université Libre de Bruxelles, Campus Erasme, 808 Route de Lennik, 1070 Bruxelles

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15

Lancaster, Eric, Frank Leypoldt, Maarten J. Titulaer, Jérôme Honnorat, Patrick J. Waters, Markus Reindl, and Romana Höftberger. "Immunoglobulin G antibodies to the N-Methyl-D-aspartate receptor are distinct from immunoglobulin A and immunoglobulin M responses." Annals of Neurology 77, no. 1 (December 4, 2014): 183. http://dx.doi.org/10.1002/ana.24233.

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16

Yang, Tan, Ling Xu, Bin Li, Weijie Li, Xiang Ma, Lingling Fan, Robert Lee, Chuanrui Xu, and Guangya Xiang. "Antitumor activity of a folate receptor-targeted immunoglobulin G-doxorubicin conjugate." International Journal of Nanomedicine Volume 12 (March 2017): 2505–15. http://dx.doi.org/10.2147/ijn.s125591.

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17

Huang, Tao, Xueling Chen, Conghui Zhao, Xingmu Liu, Zaiping Zhang, Tongfei Li, Ruiman Sun, Huan Gu, and Jiang Gu. "Sialylated immunoglobulin G can neutralize influenza virus infection through receptor mimicry." Oncotarget 7, no. 13 (February 8, 2016): 15606–17. http://dx.doi.org/10.18632/oncotarget.7244.

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18

Ruttens, D., S. E. Verleden, P. C. Goeminne, E. Vandermeulen, E. Wauters, B. Cox, R. Vos, et al. "Genetic Variation in Immunoglobulin G Receptor Affects Survival After Lung Transplantation." American Journal of Transplantation 14, no. 7 (May 6, 2014): 1672–77. http://dx.doi.org/10.1111/ajt.12745.

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19

Spiekermann, Gerburg M., Patricia W. Finn, E. Sally Ward, Jennifer Dumont, Bonny L. Dickinson, Richard S. Blumberg, and Wayne I. Lencer. "Receptor-mediated Immunoglobulin G Transport Across Mucosal Barriers in Adult Life." Journal of Experimental Medicine 196, no. 3 (July 29, 2002): 303–10. http://dx.doi.org/10.1084/jem.20020400.

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Mucosal secretions of the human gastrointestinal, respiratory, and genital tracts contain the immunoglobulins (Ig)G and secretory IgA (sIgA) that function together in host defense. Exactly how IgG crosses epithelial barriers to function in mucosal immunity remains unknown. Here, we test the idea that the MHC class I–related Fc-receptor, FcRn, transports IgG across the mucosal surface of the human and mouse lung from lumen to serosa. We find that bronchial epithelial cells of the human, nonhuman primate, and mouse, express FcRn in adult-life, and demonstrate FcRn-dependent absorption of a bioactive Fc-fusion protein across the respiratory epithelium of the mouse in vivo. Thus, IgG, like dimeric IgA, can cross epithelial barriers by receptor-mediated transcytosis in adult animals. These data show that mucosal surfaces that express FcRn reabsorb IgG and explain a mechanism by which IgG may act in immune surveillance to retrieve lumenal antigens for processing in the lamina propria or systemically.

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20

Liu, Yunchao, Aiping Wang, Songlin Qiao, Gaiping Zhang, Jun Xi, Leiming You, Xiaohui Tian, Qiaomu Li, Lina Zhang та Junqing Guo. "Cloning and characterization of ovine immunoglobulin G Fc receptor II (FcγRII)". Veterinary Immunology and Immunopathology 133, № 2-4 (лютий 2010): 243–49. http://dx.doi.org/10.1016/j.vetimm.2009.07.020.

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21

Liu, Yunchao, Songlin Qiao, Aiping Wang, Junbiao Chang, Yumei Chen, Suzhen Yang, Ruiguang Deng та Gaiping Zhang. "Cloning and characterization of ovine immunoglobulin G Fc receptor III (FcγRIII)". Veterinary Immunology and Immunopathology 139, № 2-4 (лютий 2011): 282–88. http://dx.doi.org/10.1016/j.vetimm.2010.10.002.

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22

Tesar, Devin B., and Pamela J. Björkman. "An intracellular traffic jam: Fc receptor-mediated transport of immunoglobulin G." Current Opinion in Structural Biology 20, no. 2 (April 2010): 226–33. http://dx.doi.org/10.1016/j.sbi.2010.01.010.

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23

Honma, Y., N. Sugita, T. Kobayashi, Y. Abiko та H. Yoshie. "Lower antibody response toPorphyromonas gingivalisassociated with immunoglobulin G Fcγ receptor IIBpolymorphism". Journal of Periodontal Research 43, № 6 (грудень 2008): 706–11. http://dx.doi.org/10.1111/j.1600-0765.2007.01078.x.

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24

Chaikin, Margery A., Raymond W. Sweet, Daniel R. Sylvester та Derk J. Bergsma. "Variants of the human high-affinity receptor (FcγRI) for immunoglobulin G". Gene 104, № 2 (серпень 1991): 285–86. http://dx.doi.org/10.1016/0378-1119(91)90264-c.

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25

Ruttens, D., S. E. Verleden, P. C. Goeminne, E. Vandermeulen, E. Wauters, R. Vos, D. E. Van Raemdonck, D. Lambrechts, B. M. Vanaudenaerde, and G. M. Verleden. "Genetic Variation in Immunoglobulin G Receptor Affects Survival After Lung Transplantation." Journal of Heart and Lung Transplantation 33, no. 4 (April 2014): S30. http://dx.doi.org/10.1016/j.healun.2014.01.110.

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26

Cho, B. Y., Y. K. Shong, H. K. Lee, C. S. Koh, and H. K. Min. "Inhibition of thyrotropin-stimulated adenylate cyclase activation and growth of rat thyroid cells, FRTL-5, by immunoglobulin G from patients with primary myxedema: comparison with activities of thyrotropin-binding inhibitor immunoglobulins." Acta Endocrinologica 120, no. 1 (January 1989): 99–106. http://dx.doi.org/10.1530/acta.0.1200099.

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Abstract. We studied the blocking type TSH receptor antibodies in 28 patients with primary myxedema and 21 patients with goitrous Hashimoto's thyroiditis by measuring the ability of their IgGs to inhibit TSH binding to its receptor, and to inhibit TSH-stimulated cAMP increase and [3H] thymidine incorporation in a rat thyroid cell line, FRTL-5. The incidences of TSH binding inhibitor immunoglobulin, thyroid stimulation inhibiting immunoglobulin and thyroid growth inhibiting immunoglobulin in patients with primary myxedema were 54.6, 75 and 65.2%, respectively, against 14.3,0 and 17.7%, respectively, in goitrous Hashimoto's thyroiditis. The antibodies inhibited dose-dependently not only TSH stimulated but also Graves' IgG-stimulated cAMP increase and [3H] thymidine incorporation. The TSH binding inhibitor immunoglobulin activities in patients with primary myxedema were significantly correlated with both the thyroid stimulation inhibiting immunoglobulin (r = 0.665; P<0.01) and the thyroid growth inhibiting immunoglobulin (r = 0.618; P<0.01) activity. Thirteen patients whose TSH binding inhibitor immunoglobulin activities were more than 50% had both strong thyroid stimulation inhibiting immunoglobulin (75.1–100%) and thyroid growth inhibiting immunoglobulin (57.4–100%) activities. These data suggest that the vast majority of patients with primary myxedema have potent blocking type TSH receptor antibodies. These might play a role in primary myxedema causing hypothyroidism and thyroid atrophy through inhibiting TSH-stimulated cAMP generation.

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27

Teeling, Jessica L., Theo Jansen-Hendriks, Taco W. Kuijpers, Masja de Haas, Jan G. J. van de Winkel, C. Erik Hack, and Wim K. Bleeker. "Therapeutic efficacy of intravenous immunoglobulin preparations depends on the immunoglobulin G dimers: studies in experimental immune thrombocytopenia." Blood 98, no. 4 (August 15, 2001): 1095–99. http://dx.doi.org/10.1182/blood.v98.4.1095.

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The clinical benefit of intravenous immunoglobulin (IVIG) preparations in the treatment of immune thrombocytopenic purpura (ITP) is supposed to be mediated by blockade of Fcγ receptor–bearing phagocytes. In 2 experimental models for ITP, it is shown that the therapeutic efficacy of IVIG preparations is related to the IgG dimer content present in these preparations. A rat monoclonal antibody (mAb; MWReg30) directed to the murine platelet-specific integrin αIIbβ3 (gpIIb/IIIa) was administered intraperitoneally either as bolus injection or continuous infusion. With bolus injection, the circulating platelet count dropped to almost zero within 3 hours. Pretreatment with cobra venom factor did not affect platelet depletion, whereas pretreatment with anti-FcγRII/III mAb 2.4G2 or IVIG greatly reduced platelet clearance. With continuous infusion, platelet numbers reached a steady state after 4 days, at approximately 25% of control. This reduction in platelets was, however, not observed in mice deficient for the FcRγ-chain, lacking FcγRI, FcγRIII, and FcγRIII−/− mice. Infusion of a single dose of IVIG with a high IgG dimer content on the 4th day—ie, mimicking therapeutic administration—resulted in a platelet increase for several days. IVIG predominantly consisting of monomeric IgG had no effect on platelet numbers. In conclusion, continuous infusion of MWReg30 induces thrombocytopenia in mice by enhancing Fcγ receptor–mediated clearance of platelets. In this model, it is shown that IgG dimers present in IVIG preparations are responsible for the increase in platelet counts.

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28

Verbeet, Martin Ph, Hendrika Vermeer, Gertrüd C. M. Warmerdam, Herman A. de Boer, and Sang He Lee. "Cloning and characterization of the bovine polymeric immunoglobulin receptor-encoding cDNA." Gene 164, no. 2 (October 1995): 329–33. http://dx.doi.org/10.1016/0378-1119(95)00520-g.

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29

Rivera, J., J. M. Mullins, K. Furuichi, and C. Isersky. "Endocytosis of aggregated immunoglobulin G by rat basophilic leukemia cells; rate, extent, and effects on the endocytosis of immunoglobulin E." Journal of Immunology 136, no. 2 (January 15, 1986): 623–27. http://dx.doi.org/10.4049/jimmunol.136.2.623.

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Abstract Rat basophilic leukemia (RBL) cells have distinct receptors for IgE and IgG. We assessed the endocytosis of chemically and immunochemically cross-linked mouse-IgG and its influence on the simultaneous endocytosis of IgE. We found that at 37 degrees C, aggregates of IgG and IgE were endocytosed at about the same rate with one-half of the maximal endocytosis occurring in 5 to 13 min, and the efficiency of endocytosis for both ligands ranging from 40 to 70%. We also found that endocytosis of cross-linked IgE and IgG occurred simultaneously and neither ligand significantly affected the rate or extent of endocytosis of the other. The cells accumulated the cross-linked IgG, and then released it to the extracellular environment, at a rate (less than 3%/hr) slower than the released endocytosed IgE (greater than 10%/hr). Using an assay that discriminates between unbound and receptor-bound oligomeric IgG, we found that oligomeric IgG is endocytosed with its receptor, and that the bulk of the ligand remains bound to its receptor for greater than 120 min after endocytosis. The differences in the rate of release of endocytosed IgG vs IgE suggests that the intracellular fate or pathway of these two oligomeric ligands may differ.

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30

Crisp, Sarah J., Christine L. Dixon, Leslie Jacobson, Elodie Chabrol, Sarosh R. Irani, M. Isabel Leite, Guy Leschziner, Sean J. Slaght, Angela Vincent, and Dimitri M. Kullmann. "Glycine receptor autoantibodies disrupt inhibitory neurotransmission." Brain 142, no. 11 (October 8, 2019): 3398–410. http://dx.doi.org/10.1093/brain/awz297.

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Immunoglobulin G autoantibodies to glycine receptors are found in many patients with progressive encephalomyelitis with rigidity and myoclonus (PERM). Crisp et al. show that purified patient IgGs disrupt inhibitory neurotransmission in cultured motoneurons, and provide evidence for direct antagonistic actions on glycine receptors.

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31

Rosselli, Jennifer L., Stacey M. Thacker, Julie P. Karpinski, and Katherine A. Petkewicz. "Treatment of IgA Nephropathy: An Update." Annals of Pharmacotherapy 45, no. 10 (September 27, 2011): 1284–96. http://dx.doi.org/10.1345/aph.1q122.

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Objective: To review current literature regarding treatment options for immunoglobulin A nephropathy (IgAN). Data Sources: A MEDLINE search was performed using the terms IgA nephropathy, Berger's disease, immunoglobulin A nephropathy, angiotensin converting enzyme inhibitors, angiotensin II receptor blockers, fish oil, omega-3 fatty acids, statins. hydroxymethylglutaryl-CoA reductase Inhibitors, immunosuppressive therapy, corticosteroids, mycophenolate mofetil, cyclophosphamide, cyclosporine, azathioprine, leflunomide, antiplatelets, anticoagulants, vitamin E, infliximab, calcitriol, and intravenous immunoglobulins. A date limit was not set; however, focus was on publications from 1999 to June 2011 to review recent literature and therapeutic recommendations. Study Selection and Data Extraction: All articles in English, including studies conducted in humans, meta-analyses, review articles, guidelines, statements, and reference citations, were identified and evaluated. Data Synthesis: IgAN is the most common primary glomerulonephritis worldwide, leading to end-stage renal disease in 20–30% of patients. Evidence guiding management of IgAN has been sparse and clinical trials have not conclusively demonstrated effective treatments, largely due to suboptimal methodologies. Treatment strategies have included management of blood pressure and lipids, improvement or stabilization of kidney function, and reduction of proteinuria. This review of IgAN provides an update regarding standard and nonconventional treatment options based on recently published literature. Conclusions: Supportive therapies, including angiotensin blockade, should be considered as first-line therapy for patients with urine protein >0.5 g/day and/or blood pressure > 140/90 mmHg, Corticosteroids could be considered as add-on or monotherapy for patients with urine protein >1 g/day with preserved renal function. Conclusive data are lacking for general treatment recommendations for the use of other therapies for IgAN.

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32

Weng, Wen-Kai, Abby Rosenberg, and Ronald Levy. "Immunoglobulin G Fc Receptor Polymorphisms and Clinical Course in Follicular Lymphoma Patients." Blood 104, no. 11 (November 16, 2004): 3250. http://dx.doi.org/10.1182/blood.v104.11.3250.3250.

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Abstract Patients with low-grade B cell lymphoma, such as follicular lymphoma usually have an indolent clinical course. In most of the cases, patients do not require therapy at the time of diagnosis. Instead, patients can be monitored from months to years before the need for therapy. However, the time interval from diagnosis to the first therapy in these patients can vary significantly. In addition, the overall clinical course is heterogeneous in these patients with variable length of survival after diagnosis. The pathobiological basis of this hetergenisity is not known. We have recently found that IgG Fc receptor (FcγR) polymorphisms correlated with clinical outcome after immunotherapies in patients with follicular lymphoma. In one case, FcγRIIIa 158 V/F and FcγRIIa 131 H/R polymorphisms predicted the response to anti-CD20 antibody, rituximab therapy probably due to their role in the antibody-dependent cellular cytotoxicity. One question is whether the FcγR polymorphisms are correlated with the general clinical course of follicular lymphoma due toq their role in innate immunity. We therefore tested if FcγRIIIa 158 V/F, FcγRIIa 131 H/R and FcγRIIb 232 I/T polymorphisms predict clinical course of a group of 307 patients with follicular lymphoma. None of the three FcγR polymorphisms tested correlated with the time interval from diagnosis to first therapy, or with overall survival in this group of patients. We then tested whether FcγR polymorphisms have predictive value on clinical response to chemotherapy. Of 307 patients, only 158 patients received chemotherapy alone as first therapy, while the rest of the patients have received additional idiotype vaccination or rituximab. In the analysis of these 158 patients, there was no correlation between the FcγR polymorphisms and response rate to chemotherapy or time to progression after chemotherapy. Our results did not find any association between the three FcγR polymorphisms tested and clinical course of disease or response to chemotherapy in patients with follicular lymphoma, suggesting that the predictive value of FcγR polymorphisms on the clinical responses to rituximab is specific to the monoclonal antibody therapy.

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33

Paetz, Antje, Markus Sack, Theo Thepen, Mehmet K. Tur, Daniela Bruell, Ricarda Finnern, Rainer Fischer та Stefan Barth. "Recombinant soluble human Fcγ receptor I with picomolar affinity for immunoglobulin G". Biochemical and Biophysical Research Communications 338, № 4 (грудень 2005): 1811–17. http://dx.doi.org/10.1016/j.bbrc.2005.10.162.

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34

Viansone, Alessandro Adriano, Daniela Boggiani, and Antonino Musolino. "Prognostic Role of Immunoglobulin G Fragment C Receptor Polymorphisms in Solid Tumors." JAMA Oncology 4, no. 1 (January 1, 2018): 132. http://dx.doi.org/10.1001/jamaoncol.2017.2802.

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35

Morawetz, R. A., L. Gabriele, L. V. Rizzo, N. Noben-Trauth, R. Kühn, K. Rajewsky, W. Müller, et al. "Interleukin (IL)-4-independent immunoglobulin class switch to immunoglobulin (Ig)E in the mouse." Journal of Experimental Medicine 184, no. 5 (November 1, 1996): 1651–61. http://dx.doi.org/10.1084/jem.184.5.1651.

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Immunoglobulin (Ig) class switching in B cells is regulated by stimuli transduced by cytokines and cell-cell contact. Among these stimuli, interleukin (IL)-4 has been considered an absolute prerequisite for class switching to IgE in the mouse. Here we report that IL-4-deficient (IL-4-/-) and wildtype mice had comparably elevated serum IgE levels during the course of a murine retrovirus-induced immunodeficiency syndrome, MAIDS. IgE switching in IL-4-/- mice was also induced by injection of anti-IgD antibody. Treatment with anti-IgD induced germline epsilon (g epsilon) transcripts with comparable efficiency in IL-4-/- mice and controls, but the levels of productive epsilon transcripts (p epsilon) were lower by a factor of 200 and serum IgE levels were lower by a factor of 300 in IL-4-/- mice as compared with controls. Induction of g epsilon after anti-IgD treatment of IL-4-/- mice was unaffected by simultaneous treatment with monoclonal antibodies to IL-4 and IL-4 receptor alpha chain. Infection of IL-4-/- mice with Nippostrongylus brasiliensis, a potent stimulus for IgE production, resulted in induction of g epsilon transcripts; however, p epsilon transcripts were barely detectable and serum IgE was not detected. These findings establish a novel IL-4-independent pathway for IgE switching in the mouse that is strongly activated in retroviral infection but weakly in nematode infection. This pathway appears to be dependent on distinct factors that separately control induction of g epsilon transcription and switch recombination to p epsilon.

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36

Beltrame, S. P., S. R. Auger, C. R. Bilder, C. I. Waldner, and J. C. Goin. "Modulation of M2 muscarinic receptor-receptor interaction by immunoglobulin G antibodies from Chagas' disease patients." Clinical & Experimental Immunology 164, no. 2 (March 10, 2011): 170–79. http://dx.doi.org/10.1111/j.1365-2249.2011.04370.x.

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37

Senécal, Jean-Luc, Sabrina Hoa, Roger Yang, and Martial Koenig. "Pathogenic roles of autoantibodies in systemic sclerosis: Current understandings in pathogenesis." Journal of Scleroderma and Related Disorders 5, no. 2 (September 9, 2019): 103–29. http://dx.doi.org/10.1177/2397198319870667.

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The potential pathogenic role for autoantibodies in systemic sclerosis has captivated researchers for the past 40 years. This review answers the question whether there is yet sufficient knowledge to conclude that certain serum autoantibodies associated with systemic sclerosis contribute to its pathogenesis. Definitions for pathogenic, pathogenetic and functional autoantibodies are formulated, and the need to differentiate these autoantibodies from natural autoantibodies is emphasized. In addition, seven criteria for the identification of pathogenic autoantibodies are proposed. Experimental evidence is reviewed relevant to the classic systemic sclerosis antinuclear autoantibodies, anti-topoisomerase I and anticentromere, and to functional autoantibodies to endothelin 1 type A receptor, angiotensin II type 1 receptor, muscarinic receptor 3, platelet-derived growth factor receptor, chemokine receptors CXCR3 and CXCR4, estrogen receptor α, and CD22. Pathogenic evidence is also reviewed for anti-matrix metalloproteinases 1 and 3, anti-fibrillin 1, anti-IFI16, anti-eIF2B, anti-ICAM-1, and anti-RuvBL1/RuvBL2 autoantibodies. For each autoantibody, objective evidence for a pathogenic role is scored qualitatively according to the seven pathogenicity criteria. It is concluded that anti-topoisomerase I is the single autoantibody specificity with the most evidence in favor of a pathogenic role in systemic sclerosis, followed by anticentromere. However, these autoantibodies have not been demonstrated yet to fulfill completely the seven proposed criteria for pathogenicity. Their contributory roles to the pathogenesis of systemic sclerosis remain possible but not yet conclusively demonstrated. With respect to functional autoantibodies and other autoantibodies, only a few criteria for pathogenicity are fulfilled. Their common presence in healthy and disease controls suggests that major subsets of these immunoglobulins are natural autoantibodies. While some of these autoantibodies may be pathogenetic in systemic sclerosis, establishing that they are truly pathogenic is a work in progress. Experimental data are difficult to interpret because high serum autoantibody levels may be due to polyclonal B-cell activation. Other limitations in experimental design are the use of total serum immunoglobulin G rather than affinity-purified autoantibodies, the confounding effect of other systemic sclerosis autoantibodies present in total immunoglobulin G and the lack of longitudinal studies to determine if autoantibody titers fluctuate with systemic sclerosis activity and severity. These intriguing new specificities expand the spectrum of autoantibodies observed in systemic sclerosis. Continuing elucidation of their potential mechanistic roles raises hope of a better understanding of systemic sclerosis pathogenesis leading to improved therapies.

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38

Kobayashi, Noriyoshi, Yusuke Suzuki, Toshinao Tsuge, Ko Okumura, Chisei Ra, and Yasuhiko Tomino. "FcRn-mediated transcytosis of immunoglobulin G in human renal proximal tubular epithelial cells." American Journal of Physiology-Renal Physiology 282, no. 2 (February 1, 2002): F358—F365. http://dx.doi.org/10.1152/ajprenal.0164.2001.

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In the kidney, proteins filtered through glomeruli are reabsorbed by endocytosis along the proximal tubules to avoid renal loss of large amounts of proteins. Recently, neonatal Fc receptor (FcRn), which is involved in the transport of IgG across several epithelial and endothelial cells, was reported to be expressed in renal proximal tubular epithelial cells (RPTECs). However, there has been no direct evidence for receptor-mediated endocytosis of IgG in human RPTECs. To explore physiological roles of FcRn in the proximal tubules, we used the human RPTECs to examine IgG transport. FcRn was expressed in RPTECs and physically associated with β2-microglobulin, preserving the capacity of specific pH-dependent IgG binding. Human IgG was bound to the cell surface of RPTECs in a pH-dependent manner. The human IgG transport assay revealed that receptor-mediated transepithelial transport of intact IgG in RPTECs is bidirectional and that it requires the formation of acidified intracellular compartments. With the use of double immunofluorescence, the internalized human IgG was marked in cytoplasm of RPTECs and colocalized with FcRn. These data define the mechanisms of FcRn-associated IgG transport in RPTEC monolayers. It was suggested that the intact pathway for human IgG transepithelial transport may avoid lysosomal degradation of IgG.

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39

Duncan, JI, SS Armstrong-Fisher, SJ Urbaniak, DR Abramovich, PH Whiting, and KR Page. "Transfer of immunoglobulin G across the isolated perfused human placental lobule." Reproduction, Fertility and Development 7, no. 6 (1995): 1547. http://dx.doi.org/10.1071/rd9951547.

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This study demonstrates that IgG transfer in vitro across the isolated perfused human placental lobule can be successfully studied by using natural forms of IgG. The transfer of anti-RhD IgG (anti-D) was measured in the presence and absence of intravenous immunoglobulin (IVIgG). When anti-D and IVIgG were present alone each crossed the placenta at about the same rate, but when both forms were present at the same time the movement of one interfered with the movement of the other. This pattern of transfer is consistent with receptor-mediated transcytosis. The interactions of IgG with trophoblastic transporters may therefore be studied without the complications that might arise from the use of conventionally labelled molecules.

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40

Sigitova, O. N., T. Yu Kim, and R. R. Sharipova. "Modern classification, progression factors, treatment and outcomes of primary mesangial proliferative glomerulonephritis." Kazan medical journal 98, no. 5 (October 15, 2017): 784–91. http://dx.doi.org/10.17750/kmj2017-784.

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The choice of treatment of mesangial proliferative glomerulonephritis (post-infection, immunoglobulin A, G and M nephritis) is performed taking into account the remission achievement, slowing of progression and reduction of the risk of recurrences of glomerulonephritis. The efficiency of etiologic factor removing is debatable: glomerulonephritis associated with infections usually resolves after their elimination; individual patients achieve immunoglobulin A nephritis remission with persistent antimicrobial treatment of focal infection, but surgical removal of the focus (tonsillectomy) does not affect the long-term prognosis, therefore it is not recommended. Treatment of immunoglobulin A nephritis with oral prednisone for up to 4 months, sometimes in combination with cyclophosphamide (cyclophosphane), reduces the likelihood of its relapse. At low risk of progression of immunoglobulin A nephritis with proteinuria less than 1 g/day, long-term therapy with angiotensin-converting enzyme inhibitors or angiotensin receptor blockers is indicated with administration of maximum tolerated doses for proteinuria more than 1 g/day. Also fish oil 3 g/day is administered for up to 2 years. If proteinuria more than 1 g/day persists for 3-6 months, corticosteroids are recommended for 6 months. With mild renal dysfunction, corticosteroids are prescribed orally or in pulse-therapy with high doses intravenously and maintenance therapy with low doses orally. Immunosuppressive therapy - cyclophosphamide, cyclosporine, azathioprine, mycophenolate mofetil - in combination with corticosteroids is indicated in rapid loss of renal function or massive/moderate proteinuria. In minimal proteinuria immunosuppressive therapy is considered to be unreasonable. Use of intravenous immunoglobulin for immunoglobulin A nephritis from the point of view of lesser toxic effect is possible only as the induction therapy. Currently, there are no clinical recommendations for the treatment of immunoglobulin M nephritis, in case of nephrotic syndrome, corticosteroids are the drugs of the 1st line. There are isolated studies of the use of cyclophosphamide, mycophenolate mofetil, and cyclosporine, with the achievement of remission in frequent relapses of nephrotic syndrome or steroid drug resistance. The cases of immunoglobulin M nephritis treates with retuximab with a positive effect are described. The effectiveness of immunoglobulin G nephritis treatment is less studied, the choice of treatment is similar to that of immunoglobulin A and M nephritis.

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41

Hansen, Steffen F., Lotte B. Larsen, and Lars Wiking. "Thermal effects on IgM-milk fat globule-mediated agglutination." Journal of Dairy Research 86, no. 1 (December 6, 2018): 108–13. http://dx.doi.org/10.1017/s0022029918000778.

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AbstractThe process of agglutination causes firm cream layers in bovine milk, and a functioning agglutination mechanism is paramount to the quality of non-homogenized milks. The phenomenon is not well-described, but it is believed to occur due to interactions between immunoglobulins (Ig) and milk fat globules. For the first time, this paper demonstrates how the process of agglutination can be visualized using confocal laser scanning microscopy, rhodamine red and a fluoresceinisothiocynat-conjugated immunoglobulin M antibody. The method was used to illustrate the effect on agglutination of storage temperature and pasteurization temperature. Storage at 5 °C resulted in clearly visible agglutination which, however, was markedly reduced at 15 °C. Increasing storage temperature to 20 or 37 °C cancelled any detectable interaction between IgM and milk fat globules, whereby the occurrence of cold agglutination was documented. Increasing 20 s pasteurization temperatures from 69 °C to 71 °C and further to 73 °C lead to progressively higher inactivation of IgM and, hence, reduction of agglutination. Furthermore, 2-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that changes in storage temperature caused a redistribution of Ig-related proteins in milk fat globule membrane isolates. Poly-immunoglobulin G receptor was present in milk fat globule preparations stored at cold (4 °C) conditions, but absent at storage at higher temperature (25 °C). The findings provide valuable knowledge to dairy producers of non-homogenized milk in deciding the right pasteurization temperature to retain the crucial agglutination mechanism.

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42

Sprague, Elizabeth R., Henrike Reinhard, Evelyn J. Cheung, Alexander H. Farley, Robin Deis Trujillo, Hartmut Hengel, and Pamela J. Bjorkman. "The Human Cytomegalovirus Fc Receptor gp68 Binds the Fc CH2-CH3 Interface of Immunoglobulin G." Journal of Virology 82, no. 7 (January 23, 2008): 3490–99. http://dx.doi.org/10.1128/jvi.01476-07.

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ABSTRACT Recognition of immunoglobulin G (IgG) by surface receptors for the Fc domain of immunoglobulin G (Fcγ), FcγRs, can trigger both humoral and cellular immune responses. Two human cytomegalovirus (HCMV)-encoded type I transmembrane receptors with Fcγ-binding properties (vFcγRs), gp34 and gp68, have been identified on the surface of HCMV-infected cells and are assumed to confer protection against IgG-mediated immunity. Here we show that Fcγ recognition by both vFcγRs occurs independently of N-linked glycosylation of Fcγ, in contrast with the properties of host FcγRs. To gain further insight into the interaction with Fcγ, truncation mutants of the vFcγR gp68 ectodomain were probed for Fcγ binding, resulting in localization of the Fcγ binding site on gp68 to residues 71 to 289, a region including an immunoglobulin-like domain. Gel filtration and biosensor binding experiments revealed that, unlike host FcγRs but similar to the herpes simplex virus type 1 (HSV-1) Fc receptor gE-gI, gp68 binds to the CH2-CH3 interdomain interface of the Fcγ dimer with a nanomolar affinity and a 2:1 stoichiometry. Unlike gE-gI, which binds Fcγ at the slightly basic pH of the extracellular milieu but not at the acidic pH of endosomes, the gp68/Fcγ complex is stable at pH values from 5.6 to pH 8.1. These data indicate that the mechanistic details of Fc binding by HCMV gp68 differ from those of host FcγRs and from that of HSV-1 gE-gI, suggesting distinct functional and recognition properties.

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43

Margiloff, Linda, Larissa Chaplia, Andrew Chow, Pravin C. Singhal, and Joseph Mattana. "Metal-catalyzed oxidation of immunoglobulin G impairs Fc receptor-mediated binding to macrophages." Free Radical Biology and Medicine 25, no. 7 (November 1998): 780–85. http://dx.doi.org/10.1016/s0891-5849(98)00130-0.

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44

Hanson, Quinlin M., and Adam W. Barb. "A Perspective on the Structure and Receptor Binding Properties of Immunoglobulin G Fc." Biochemistry 54, no. 19 (May 7, 2015): 2931–42. http://dx.doi.org/10.1021/acs.biochem.5b00299.

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45

Cameron and Allen. "The human high-affinity immunoglobulin G receptor activates SH2-containing inositol phosphatase (SHIP)." Immunology 97, no. 4 (August 1999): 641–47. http://dx.doi.org/10.1046/j.1365-2567.1999.00813.x.

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46

Qiao, Shuo-Wang, Wayne I. Lencer, and Richard S. Blumberg. "How the controller is controlled ? neonatal Fc receptor expression and immunoglobulin G homeostasis." Immunology 120, no. 2 (February 2007): 145–47. http://dx.doi.org/10.1111/j.1365-2567.2006.02507.x.

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47

Kim, S. Rim, Patrick G. Gavin, and Katherine Pogue-Geile. "Prognostic Role of Immunoglobulin G Fragment C Receptor Polymorphisms in Solid Tumors—Reply." JAMA Oncology 4, no. 1 (January 1, 2018): 132. http://dx.doi.org/10.1001/jamaoncol.2017.2813.

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48

Neuberger, Michael S., Michael R. Ehrenstein, Cristina Rada, Julian Sale, Facundo D. Batista, Gareth Williams, and Cesar Milstein. "Memory in the B–cell compartment: antibody affinity maturation." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 355, no. 1395 (March 29, 2000): 357–60. http://dx.doi.org/10.1098/rstb.2000.0573.

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In the humoral arm of the immune system, the memory response is not only more quickly elicited and of greater magnitude than the primary response, but it is also different in quality. In the recall response to antigen, the antibodies produced are of higher affinity and of different isotype (typically immunoglobulin G rather than immunoglobulin M). This maturation rests on the antigen dependence of B–cell maturation and is effected by programmed genetic modifications of the immunoglobulin gene loci. Here we consider how the B–cell response to antigen depends on the affinity of the antigen–receptor interaction. We also compare and draw parallels between the two processes, which underpin the generation of secondaryresponse antibodies: V gene somatic hypermutation and immunoglobulin heavy–chain class switching.

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49

Larsen, A., T. Davis, B. M. Curtis, S. Gimpel, J. E. Sims, D. Cosman, L. Park, E. Sorensen, C. J. March, and C. A. Smith. "Expression cloning of a human granulocyte colony-stimulating factor receptor: a structural mosaic of hematopoietin receptor, immunoglobulin, and fibronectin domains." Journal of Experimental Medicine 172, no. 6 (December 1, 1990): 1559–70. http://dx.doi.org/10.1084/jem.172.6.1559.

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We report the isolation from a placental library, of two cDNAs that can encode high affinity receptors for granulocyte colony-stimulating factor (G-CSF) when expressed in COS-7 cells. The cDNAs are predicted to encode integral membrane proteins of 759 and 812 amino acids in length. The predicted extracellular and membrane spanning sequences of the two clones are identical, as are the first 96 amino acids of their respective cytoplasmic regions. Different COOH termini of 34 or 87 residues are predicted for the two cDNAs, due apparently to alternate splicing. The receptor with the longer cytoplasmic domain is the closest human homologue of the murine G-CSF receptor recently described by Fukunaga et al. (Fukunaga, R., E. Ishizaka-Ikeda, Y. Seto, and S. Nagata. 1990. Cell. 61:341). A hybridization probe derived from the placental G-CSF receptor cDNA detects a approximately 3-kb transcript in RNAs isolated from placenta and a number of lymphoid and myeloid cells. The extracellular region of the G-CSF receptors is composed of four distinct types of structural domains, previously recognized in other cell surface proteins. In addition to the two domains of the HP receptor family-defining region (Patthy, L. 1990. Cell. 61:13) it incorporates one NH2-terminal Ig-like domain, and three additional repeats of fibronectin type III-like domains. The presence of both an NH2-terminal Ig-like domain and multiple membrane-proximal FN3-like domains suggests that the G-CSF receptor may be derived from an ancestral NCAM-like molecule and that the G-CSF receptor may function in some adhesion or recognition events at the cell surface in addition to the binding of G-CSF.

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50

Brown, R. S., L. P. Kertiles, and R. E. Kleinmann. "Choice of immunoglobulin G purification method in assays for antibodies to the thyrotropin receptor." Clinical Chemistry 32, no. 11 (November 1, 1986): 2034–39. http://dx.doi.org/10.1093/clinchem/32.11.2034.

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Abstract Activity of autoantibodies to the thyrotropin receptor in the serum of patients with active Graves's disease was compared when the patients' IgG was purified by three different procedures: ammonium sulfate precipitation (I), a modified batch diethylaminoethyl cellulose method (II), and affinity chromatography on Protein A-Sepharose CL-4B (III). IgG extracted by I was significantly less potent in inhibiting binding of 125I-labeled thyroid membranes than that prepared by either II or III, and was significantly less effective than II in stimulating adenyl cyclase activity in thyroid membrane. Thyroglobulin, a serum protein whose concentration is increased in patients with various thyroid diseases, was coprecipitated in amounts sufficient to significantly inhibit binding only when method I was used, but not with either of the other two procedures. Evidently method I is inferior to either of the other two when used for purification of autoantibodies to the thyrotropin receptor. Method II used in this study, being faster and more economical than I and of equivalent efficacy, is a feasible alternative method for clinical use.

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