IgM and its receptors and binding proteins

This volume reviews the current state of research on the IgM antibody and its multiple receptors and binding proteins. Interactions of the IgM ligands with these molecules are important for protection against infections as a first line of defense, as well as for regulation of immune responses to pat...

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Bibliographic Details
Other Authors: Kubagawa, Hiromi, (Editor), Burrows, Peter D., (Editor)
Format: eBook
Language: English
Published: Cham, Switzerland : Springer, [2017]
Series: Current topics in microbiology and immunology ; v. 408.
Subjects:
ISBN: 9783319645261
9783319645247
Physical Description: 1 online resource : illustrations

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245 0 0 |a IgM and its receptors and binding proteins /  |c Hiromi Kubagawa, Peter D. Burrows, editors. 
264 1 |a Cham, Switzerland :  |b Springer,  |c [2017] 
264 4 |c ©2017 
300 |a 1 online resource :  |b illustrations 
336 |a text  |b txt  |2 rdacontent 
337 |a počítač  |b c  |2 rdamedia 
338 |a online zdroj  |b cr  |2 rdacarrier 
490 1 |a Current topics in microbiology and immunology ;  |v v. 408 
504 |a Includes bibliographical references. 
505 0 |6 880-01  |a Preface -- References -- Contents -- 22 The Appearance and Diversification of Receptors for IgM During Vertebrate Evolution -- Abstract -- 1 The Adaptive Immune System of Vertebrates -- 2 The Appearance of Receptors Interacting with the Constant Domain of Igs -- 3 The Polymeric Ig Receptorâ#x80;#x94;PIGR -- 4 The FcαÂæR -- 5 The FcÂæR -- 6 Concluding Remarks -- Acknowledgements -- References -- 23 Authentic IgM Fc Receptor (FcÎơR) -- Abstract -- 1 Introduction -- 2 Lymphocyte-Restricted Expression of FcÂæR -- 3 Unique Ligand-Binding Activity 
505 8 |a 3.1 FcÂæ-Specificity, Ligand-Binding Avidity, and Glycosylation3.2 Cis Engagement -- 3.3 Modulatory Effect of FcÂæR by Cis Engagement -- 3.4 Key Residues in the Transmembrane and Cytoplasmic Tail for FcÂæR Function -- 4 FcÂæR Deficiency in Mice -- 5 Epilogue -- Acknowledgements -- References -- 40 FCRLAâ#x80;#x94;A Resident Endoplasmic Reticulum Protein that Associates with Multiple Immunoglobulin Isotypes in B Lineage Cells -- Abstract -- 1 Introductionâ#x80;#x94;Fc Receptors and Their Relatives -- 2 The Identification of FCRLA and FCRLB -- 3 The FCRLA Genome Landscape 
505 8 |a 4 Features of the FCRLA Protein5 FCRLAâ#x80;#x94;Phylogeny and Disease Association -- 6 FCRLAâ#x80;#x94;Expression Pattern and Regulation -- 7 FCRLA is a Soluble Resident ER Protein -- 8 FCRLA is Retained in the ER via its N-terminal Disordered Domain -- 9 FCRLA Associates with Multiple Ig Isotypes in the ER -- 10 TRIM21â#x80;#x94;One Other Intracellular Fc Receptor that Binds Multiple Ig Isotypes -- 11 FCRLA Functionâ#x80;#x94;Facts and Speculations -- 11.1 Facts -- 11.2 Speculations -- Acknowledgements -- References -- 24 Specific IgM and Regulation of Antibody Responses -- Abstract 
505 8 |a 1 Introduction1.1 IgG-Mediated Feedback Suppression -- 1.2 IgG-Mediated Feedback Enhancement -- 1.3 IgE-Mediated Feedback Enhancement -- 1.4 IgM-Mediated Feedback Enhancement -- 2 Basic Parameters of IgM-Mediated Enhancement -- 2.1 Antigens -- 2.2 The IgM Molecule and Mode of Administration -- 2.3 Primary Antibody Responses -- 2.4 Priming for Memory Responses -- 2.5 Avidity of the Enhanced Response -- 2.6 Germinal Center Responses -- 2.7 Specificity of the Enhanced Antibody Response -- 2.8 T Cells and IgM-Mediated Enhancement 
505 8 |a 3 Complement in Antibody Responses to Uncomplexed Antigen4 Complement in Antibody Responses to IgM-Antigen Complexes -- 4.1 Complement Activation by IgM -- 4.2 Complement Receptors 1 and 2, CR1/2, in Antibody Responses to IgM-Antigen Complexes -- 4.3 CÎơ13 Knock-in Mice with a Point Mutation in the IgM Heavy Chain Abolishing C1q-Binding -- 4.4 FcÎơR (Toso/Faim3) and IgM-Mediated Enhancement -- 4.5 Other IgM-Binding Receptors and IgM-Mediated Enhancement -- 4.6 Specific IgM from Wildtype but not CÎơ13 Mice, Causes Rapid Deposition of C3 on SRBC in Vivo 
506 |a Plný text je dostupný pouze z IP adres počítačů Univerzity Tomáše Bati ve Zlíně nebo vzdáleným přístupem pro zaměstnance a studenty 
520 |a This volume reviews the current state of research on the IgM antibody and its multiple receptors and binding proteins. Interactions of the IgM ligands with these molecules are important for protection against infections as a first line of defense, as well as for regulation of immune responses to pathogens and self-antigens. The book includes up-to-date information on: (i) the phylogeny of three IgM-binding receptors [polymeric Ig receptor (pIgR), Fc receptor for both IgA and IgM (Fc?/æR), and Fc receptor for IgM only (FcæR)]; (ii) the lymphocyte-restricted distribution and unique ligand-binding activity of FcæR; (iii) the definition and potential function of Fc receptor-like molecule A (FCRLA) as a resident endoplasmic reticulum protein that binds IgM, but also IgG and IgA; (iv) IgM antibody-mediated enhancement of humoral immune responses, highlighting the importance of complement and its receptors, (v) the numerous important roles of IgM natural antibodies in regulation of inflammation. It is an invaluable resource for researchers and clinicians alike. 
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700 1 |a Kubagawa, Hiromi,  |e editor. 
700 1 |a Burrows, Peter D.,  |e editor. 
776 0 8 |i Printed edition:  |z 9783319645247 
830 0 |a Current topics in microbiology and immunology ;  |v v. 408. 
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