Antibody glycosylation / / edited by Marija Pezer

• Record Nr.: UNINA9910506382203321
• Pubbl/distr/stampa: Cham, Switzerland : , : Springer, , [2021]; ©2021
• ISBN: 3-030-76912-7
• Descrizione fisica: 1 online resource (585 pages)
• Collana: Experientia Supplementum Ser ; ; v.112
• Disciplina: 571.967
• Soggetti: Biochemical markers; Pharmacology; Immunology; Enginyeria de proteïnes; Enginyeria bioquímica; Llibres electrònics
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Nota di bibliografia: Includes bibliographical references and index.
• Nota di contenuto: Intro -- Foreword -- Contents -- Editor and Contributors -- Chapter 1: Micro-Heterogeneity of Antibody Molecules -- 1.1 Introduction -- 1.2 Disulfide Bond-Related Modifications -- 1.3 N- and C-Terminal Modifications -- 1.3.1 N-Terminal Modifications -- 1.3.2 C-Terminal Modifications -- 1.4 Chemical Modifications of Main-Chain Amino Acid Residues -- 1.4.1 Deamidation -- 1.4.2 Glycation -- 1.4.3 Oxidation -- 1.5 Aggregation -- 1.6 Glycosylation -- 1.6.1 IgG-Fc Oligosaccharide Chain -- 1.6.2 Fab Oligosaccharide Chain -- 1.7 Conclusion -- References -- Part I: Analytical Methods -- Chapter 2: Lectin and Liquid Chromatography-Based Methods for Immunoglobulin (G) Glycosylation Analysis -- 2.1 Introduction -- 2.1.1 Glycosylation -- 2.1.2 Immunoglobulins -- 2.2 Liquid Chromatography -- 2.2.1 Immunoglobulin Purification by Liquid Chromatography -- 2.2.1.1 Affinity Chromatography -- 2.2.1.2 Melon Gel Chromatography -- 2.2.1.3 Size-Exclusion Chromatography (SEC) -- 2.2.1.4 Ion-Exchange Chromatography (IEX) -- 2.2.2 N-Glycan Analysis by Liquid Chromatography -- 2.2.2.1 Glycan Release -- 2.2.2.2 Fluorescent Labeling Methods -- 2.2.2.3 Reducing Agent -- 2.2.2.4 Clean-Up ; Strategies -- 2.2.2.5 Detection of Labeled Glycans with (U)HPLC -- 2.2.2.6 N-Glycan Sequencing by Exoglycosidases -- 2.2.3 O-Glycan Analysis by Liquid Chromatography -- 2.2.4 Liquid Chromatography Coupled to Mass Spectrometry -- 2.2.4.1 Proteolytic Cleavage -- 2.2.4.2 Glycopeptide and Glycan Enrichment -- 2.2.4.3 Glycopeptide and Glycan Analysis by LC-MS -- 2.2.4.4 Analysis of Ig Glycosylation on the Subunit and Whole Protein Level -- 2.3 Lectin Techniques -- 2.3.1 Lectin Chromatography -- 2.3.2 Lectin Microarrays -- 2.4 Perspectives -- References -- Chapter 3: Mass Spectrometry-Based Methods for Immunoglobulin G N-Glycosylation Analysis -- 3.1 Basic Principles of Mass Spectrometry.; 3.1.1 Ionization -- 3.1.2 Gas-Phase Separation and Detection -- 3.1.3 Tandem MS -- 3.2 Levels of IgG N-Glycosylation Analysis -- 3.3 Sample Preparation for IgG Glycosylation Analysis -- 3.3.1 Protein A, G, and L Affinity Chromatography for IgG Enrichment from Biological Samples -- 3.3.1.1 Protein A -- 3.3.1.2 Protein G -- 3.3.1.3 Protein L -- 3.3.1.4 Recombinant Fusion Proteins and Alternative Scaffolds -- 3.3.2 Sample Preparation for Released IgG Glycan Analysis -- 3.3.2.1 Chemical and Enzymatic Glycan Release -- 3.3.3 Fluorescent and Isotopic Glycan Labeling -- 3.3.4 Sample Preparation for Glycopeptide Mapping and Subclass-Specific IgG Fc Glycosylation Analysis -- 3.3.4.1 Enzymatic Digestion -- 3.3.4.2 Stable Isotope Glycopeptide Labeling -- 3.3.4.3 Glycan and Glycopeptide Enrichment and Purification Strategies -- 3.4 Deciphering the IgG Glycan Structure -- 3.4.1 Fragmentation -- 3.4.2 Fragmentation Nomenclature -- 3.4.3 Fragmentation Candidates -- 3.4.3.1 Fragmentation of Glycopeptides -- 3.4.3.2 Fragmentation of Released Glycans -- 3.4.4 Ionization Polarity of MS Analysis -- 3.4.4.1 Example of Positive Ion Mode Fragmentation -- 3.4.4.2 Example of Negative Ion Mode Fragmentation -- 3.4.5 Exoglycosidase Digestion Monitored by MS -- 3.5 Selected Approaches for IgG Glycosylation Analysis -- 3.5.1 MALDI-MS -- 3.5.1.1 Intact Proteins and Glycopeptides -- 3.5.1.2 Released N-Glycans -- 3.5.1.3 Sialic Acid Stability -- 3.5.1.4 Matrix Substances for MALDI-MS -- 3.5.1.5 MALDI-MS for High-Throughput and Quantitative Analysis -- 3.5.2 LC-MS for IgG Glycosylation Analysis -- 3.5.2.1 Coupling LC to MS for Enhanced Separation and Structural Characterization -- 3.5.2.2 HILIC-UHPLC-MS -- 3.5.2.3 RP-LC-MS -- 3.5.2.4 PGC for Enhanced Isomeric Glycan Separation -- 3.5.2.5 Anion Exchange LC-MS -- 3.5.2.6 Challenges of Miniaturization.; 3.5.3 Capillary Electrophoresis-Mass Spectrometry -- 3.6 Perspectives -- References -- Chapter 4: Capillary (Gel) Electrophoresis-Based Methods for Immunoglobulin (G) Glycosylation Analysis -- 4.1 Historical Background -- 4.2 Background: Principles of Capillary (Gel) Electrophoresis (C(G)E) -- 4.3 Performance, Benefits, and Potentials of Capillary (Gel) Electrophoresis C(G)E -- 4.4 Data Analysis and Interpretation -- 4.5 Exoglycosidase Sequencing of Glycans -- 4.6 Coupling Capillary Electrophoresis with Mass Spectrometry -- 4.7 Latest Developments: Miniaturization of CE Systems-Microchip CE -- 4.8 Application of C(G)E for Immunoglobulin Analysis -- 4.9 Conclusion -- References -- Chapter 5: Automation of Immunoglobulin Glycosylation Analysis -- 5.1 Introduction -- 5.1.1 Biopharmaceutical Glycomics -- 5.1.2 Clinical Glycomics -- 5.1.3 Towards High-Throughput Glycomics -- 5.1.4 Robotics: The Ultimate High-Throughput Solution? -- 5.2 Automation of Glycomics Sample Preparation -- 5.2.1 Sample Origins and Protein Purification -- 5.2.1.1 Serum and Plasma -- 5.2.1.2 Therapeutic Antibody Glycoproteins -- 5.2.2 Preparing Glycans for Analysis: Glycan Release, Derivatization and Clean-Up -- 5.2.2.1 Plasma and Serum -- Automated Methods for N-; Glycan Preparation Employing Anomeric Fluorescent Labeling Strategies -- Automated Methods for N-Glycan Preparation Employing Permethylation Derivatization Strategies -- 5.2.2.2 Therapeutic Antibody Glycoproteins -- Automated Methods for N-Glycan Preparation Employing Anomeric Fluorescent Labeling Strategies -- Automated Methods for N-Glycan Preparation Employing Permethylation Derivatization Strategies -- 5.2.3 Automated Methods for Glycopeptide Preparation -- 5.3 Commentary -- 5.4 Future Perspectives -- 5.5 Conclusions -- References -- Chapter 6: Bioinformatics in Immunoglobulin Glycosylation Analysis -- 6.1 Introduction.; 6.2 Glycomic Data Collection and Processing -- 6.2.1 Reference Databases -- 6.2.2 Identification and Quantification Software Tools -- 6.3 Glycoproteomics Data Collection and Processing -- 6.3.1 Reference Databases -- 6.3.2 Identification Software Tools -- 6.3.3 Quantification Software Tools -- 6.4 Data Integration with Other Omics -- 6.5 Practical Examples -- 6.5.1 Glycomic Data Processing -- 6.5.1.1 Software Required -- 6.5.1.2 Glycan Composition Determination -- 6.5.1.3 Annotation of MS and MS/MS Glycomics Spectra -- 6.5.1.4 Convert Raw Mass Spectrometry Data to mzXML -- 6.5.1.5 Skyline for Glycomics Quantitation -- 6.5.1.6 Setting Up Transition List -- 6.5.2 Glycopeptide Data Processing for Enriched Immunoglobulins -- 6.5.2.1 Software Required -- 6.5.2.2 Glycosylation Site Identification Based on MS2 -- 6.5.2.3 Glycoform Identification Based on MS1 -- 6.5.2.4 Targeted Glycopeptide Quantification -- 6.5.3 Visualizing Profiles -- 6.5.3.1 Structural Dependencies Brought Out by GlyConnect Compozitor -- 6.5.3.2 Comparing Profiles with Glynsight -- 6.6 Conclusion -- References -- Part II: Biosynthesis and Regulation -- Chapter 7: N-Glycan Biosynthesis: Basic Principles and Factors Affecting Its Outcome -- 7.1 Introduction -- 7.2 Biosynthesis of N-Glycans in the Endoplasmic Reticulum -- 7.2.1 Building Blocks for N-Glycan Synthesis -- 7.2.2 Precursor Synthesis and Its Attachment to Nascent Polypeptide Chains -- 7.2.3 N-Glycan Processing in the ER and Quality Control -- 7.3 N-Glycan Processing in the Golgi Apparatus -- 7.3.1 N-Glycosylation of Immunoglobulins -- 7.4 Golgi Microenvironment Is Important for Normal Processing and Maturation of N-Glycans -- 7.4.1 Golgi pH Homeostasis -- 7.4.2 Golgi Ion Homeostasis -- 7.4.3 Golgi Redox State -- 7.5 Concluding Remarks -- References -- Chapter 8: Genetic Regulation of Immunoglobulin G Glycosylation.; 8.1 Introduction -- 8.2 Heritability of the Human IgG N-Glycome -- 8.3 Linkage Studies of Mouse N-glycome -- 8.4 Genome-Wide Association Studies of Human N-Glycome -- 8.4.1 Genomic Loci Associated with IgG N-Glycosylation -- 8.4.1.1 Chromosome 1 -- 8.4.1.2 Chromosome 3 -- 8.4.1.3 Chromosome 5 -- 8.4.1.4 Chromosome 6 -- 8.4.1.5 Chromosome 7 -- 8.4.1.6 Chromosome 9 -- 8.4.1.7 Chromosome 11 -- 8.4.1.8 Chromosome 14 -- 8.4.1.9 Chromosome 17 -- 8.4.1.10 Chromosome 21 -- 8.4.1.11 Chromosome 22 -- 8.4.2 Suggestive Associations -- 8.4.3 Functional Network of Loci Associated with IgG Glycosylation -- 8.5 Pleiotropy with Complex Traits and Diseases -- 8.6 Conclusions -- References -- Chapter 9: Epigenetics of Immunoglobulin G Glycosylation -- 9.1 Introduction -- 9.2 Regulation of Glycosyltransferases by Transcription Factors -- 9.3 Epigenetic Regulation of IgG Glycosylation -- 9.4 The Role of miRNAs in Protein N-Glycosylation -- 9.5 Conclusions -- References -- Chapter 10: Immunoglobulin G Glycosylation Changes in Aging and Other Inflammatory Conditions -- 10.1 Premise -- 10.2 IgG Glycosylation -- 10.3 Changes in IgG Asn297 Glycans Associated with Inflammatory Diseases -- 10.4 IgG Glycosylation as a Predictor of Disease Onset, ; Progression, and Therapy Response -- 10.4.1 Prediction of Disease Onset -- 10.4.2 Prediction of Progression and Therapy Response -- 10.5 IgG Glycosylation in Aging -- 10.6 The Inflammaging Is a Link Between Aging and Inflammation -- 10.7 How Altered IgG Glycosylation Drives Inflammation -- 10.7.1 Activation of Complement Through the Lectin or the Classical Pathways -- 10.7.2 Binding to Fcγ Receptors -- 10.7.3 Binding on Lectin Receptors of Antigen-Presenting Cells: Role in the Intravenous Administration of High Doses IgG (IVIG) -- 10.7.4 Anti IgG Autoantibodies -- 10.8 Molecular Bases of N-Glycosylation Changes -- 10.9 Conclusions.; References.

Trauma and Orthopaedic Classifications : A Comprehensive Overview / / edited by Nick G. Lasanianos, Nikolaos K. Kanakaris, Peter V. Giannoudis

• Record Nr.: UNINA9910300202903321
• Pubbl/distr/stampa: London : , : Springer London : , : Imprint : Springer, , 2015
• ISBN: 1-4471-6572-1
• Edizione: [1st ed. 2015.]
• Descrizione fisica: 1 online resource (492 p.)
• Disciplina: 610; 616.7; 617.1; 617.1027
• Soggetti: Orthopedics; Sports medicine; Surgery; Orthopedic surgery; Orthopaedics; Sports Medicine; General Surgery; Surgical Orthopedics
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Note generali: Description based upon print version of record.
• Nota di bibliografia: Includes bibliographical references and index.
• Nota di contenuto: Upper limb trauma -- Upper limb pathology -- Spine trauma -- Spine orthopaedic pathology -- Lower limb trauma -- Lower limb pathology -- General trauma -- Orthopaedic pathology – Oncology.
• Sommario/riassunto: Reporting on classification systems which are currently utilised in the clinical setting, this illustrated guide is an essential resource for all young clinicians and researchers of Trauma and Orthopaedics. Each chapter of the different anatomical sites and pathologies is designed to assist the decision making of the readers regarding treatment strategy as well as informed consent of their patients. Trauma and Orthopaedic Classifications: A Comprehensive Overview includes classifications relevant to both Elective Orthopaedic Practice and Orthopaedic Trauma. Clear graphic illustrations accompany the description of all different classification schemes in a comprehensive manner, together with a structured presentation of existing clinical evidence. Surgeons in training right through to senior surgeons and academic clinicians will find this book to be a key reference to formulate the right decisions in their clinical practice. .