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ویرایش:
نویسندگان: Preetham Elumalai (editor). Sreeja Lakshmi (editor)
سری:
ISBN (شابک) : 9811674612, 9789811674617
ناشر: Springer
سال نشر: 2022
تعداد صفحات: 306
زبان: English
فرمت فایل : PDF (درصورت درخواست کاربر به PDF، EPUB یا AZW3 تبدیل می شود)
حجم فایل: 7 مگابایت
در صورت تبدیل فایل کتاب Lectins: Innate immune defense and Therapeutics به فرمت های PDF، EPUB، AZW3، MOBI و یا DJVU می توانید به پشتیبان اطلاع دهید تا فایل مورد نظر را تبدیل نمایند.
توجه داشته باشید کتاب لکتین ها: دفاع و درمان ایمنی ذاتی نسخه زبان اصلی می باشد و کتاب ترجمه شده به فارسی نمی باشد. وبسایت اینترنشنال لایبرری ارائه دهنده کتاب های زبان اصلی می باشد و هیچ گونه کتاب ترجمه شده یا نوشته شده به فارسی را ارائه نمی دهد.
Foreword by Dr. Devaraj & Dr. Niranjali Devaraj Foreword by Prof. Sadasivam J. Kaushik Preface Contents About the Editors Chapter 1: Overview of Lectins 1.1 Introduction 1.2 History 1.3 Definition of Lectins 1.4 Carbohydrate-Binding Specificity of Lectins 1.5 Role of Lectins 1.6 Toxic or Therapeutic? 1.7 Applications of Lectins 1.7.1 Antimicrobial and Antifungal Activity of Lectins 1.7.2 Anti-insect Activity of Lectins 1.7.3 Healing Applications of Lectins 1.7.4 Lectins in Cancer Research 1.8 Conclusion References Chapter 2: Structure, Biosynthesis, and Biological Properties of Lectins 2.1 Introduction 2.2 Role of Lectin in Innate Immunity 2.3 Occurrence of Lectin 2.4 Cellular Location of Lectins 2.5 Structure and Its Biological Properties 2.5.1 C-type Lectin (CTL) 2.5.1.1 MBL 2.5.2 DC-SIGN (Dendritic Cell-Specific ICAM-3-Grabbing Non-integrin) 2.5.3 Galectin 2.6 Biosynthesis and Posttranslational Modifications 2.6.1 MBL Synthesis and Processing 2.6.2 Galectin Synthesis and Processing 2.7 Lectin Gene and Its Transcript 2.7.1 Mannose-Binding Lectin 2.7.2 DC-Sign 2.7.3 Galectin 2.8 Regulation of Gene Expression 2.9 Conclusion References Chapter 3: Classification of Lectins 3.1 Introduction 3.2 Classification of Lectins Based on Molecular Structure 3.2.1 Simple Lectins 3.2.1.1 Legume 3.2.1.2 Amaranthin 3.2.1.3 Cereal-Wheat Germ Agglutinin 3.2.1.4 Moraceae-Jacalin 3.2.1.5 Euphorbiaceae-Chitin-Binding Lectins 3.2.1.6 Galectins 3.2.1.7 Pentraxins 3.2.2 Mosaic Lectin 3.2.2.1 Viral Haemagglutinin 3.2.2.2 C-Lectin 3.2.2.3 P-Lectin 3.2.2.4 I-Lectin 3.2.3 Macromolecular Complex 3.3 Classification of Lectins Based on Glycoconjugate Specificity 3.3.1 Mannose-Specific Lectins 3.3.2 Galactose/N-acetylgalactosamine Specific Lectins 3.3.3 Fucose Specific Lectins 3.3.4 Sialic Acid Specific Lectins 3.4 Classification Based on Source (Plants, Animal, Microbes) 3.4.1 Plant Lectins 3.4.2 Animal Lectins 3.4.3 Microbial Lectins 3.5 Conclusion References Chapter 4: Molecular Basis of Lectin-Carbohydrate Interaction 4.1 Introduction 4.2 Types of Lectin and Its Interaction with Other Molecules 4.2.1 Plant Lectins 4.2.1.1 Legume Lectin 4.2.1.2 Ricin Lectin 4.2.2 Animal Lectin 4.2.2.1 S-Lectins 4.2.2.2 C-Lectin 4.2.3 Bacterial Lectin 4.3 Molecular Basis of Carbohydrate Interaction 4.3.1 Mannose/Glucose-Binding Lectins 4.3.2 N-Acetylglucosamine-Binding Lectins 4.3.3 N-Acetylgalactosamine/Galactose-Binding Lectins 4.4 Importance of Lectin-Carbohydrate Interaction 4.5 Conclusion References Chapter 5: Animal Lectin 5.1 Introduction 5.1.1 Basic Structure of Animal Lectin 5.1.2 Classification of Animal Lectin 5.2 Calnexin and Calreticulin 5.2.1 Structure of Calnexin and Calreticulin 5.2.2 Function of Calnexin and Calreticulin 5.3 M Type Lectin 5.3.1 Structure of M Type Lectins 5.3.2 Classification and Functions of M Type Lectins 5.4 L Type Lectins 5.4.1 ERGIC-53, ERGL, VIP 36, VIPL 5.5 P Type Lectin 5.5.1 Cation-Dependent Mannose-6-Phosphate Receptor (CD-MPR) 5.5.2 Cation-Independent Mannose-6-Phosphate Receptor (CI-MPR) 5.6 C Type Lectin 5.6.1 Structure of C Type Lectin 5.6.2 Classification of C Type Lectins (CLRD/CTLD-Containing Proteins) 5.6.3 Functions of C Type Lectin 5.7 S Type Lectin (Galectins) 5.7.1 Classification and Structure of Galectins 5.7.1.1 Chicken Galectins 5.7.2 Functions of Galectins 5.8 I Type Lectin 5.8.1 Classification and Functions of I Type Lectins 5.9 R Type Lectins 5.9.1 Structure of R Type Lectin 5.9.2 The Mannose Receptor Family 5.10 F Box Lectins 5.10.1 Structure of F Box Lectins 5.10.2 Classification and Function of F Box Lectins 5.11 Ficolins 5.11.1 Classification and Structure of Ficolins 5.11.2 Functions of Ficolins 5.11.3 Tachylectins 5.12 Chi-Lectins 5.13 F Type Lectin 5.13.1 Structure of F Type Lectins 5.13.2 Functions of F Type Lectins 5.13.3 Anguilla anguilla Agglutinin 5.14 Intelectins 5.14.1 Classification of Intelectins 5.14.2 Intelectins in Fish 5.15 Conclusion References Chapter 6: Plant Lectins 6.1 Introduction 6.2 History 6.3 Classification 6.3.1 Based on the Number of Carbohydrate Binding Sites 6.3.1.1 Merolectins 6.3.1.2 Hololectins 6.3.1.3 Chimerolectins 6.3.1.4 Superlectins 6.3.2 Based on Structure and Evolution 6.3.2.1 Amaranthin Family 6.3.2.2 Chitin-Binding Lectin 6.3.2.3 Cucurbitaceae Phloem Lectin 6.3.2.4 Jacalin-Related Lectins 6.3.2.5 Legume Lectins 6.3.2.6 Monocot Mannose-Binding Lectin 6.3.2.7 Type 2 Ribosome Inactivating Lectin (RIP) 6.3.3 Based on Sugar Specificity or Binding Affinity to Carbohydrate Moiety 6.3.3.1 Mannose-Binding Lectins 6.3.3.2 Galactose/N-Acetyl Galactosamine Binding Lectins 6.3.3.3 N-Acetyl Glucosamine Binding Lectins 6.3.3.4 Fucose-Binding Lectins 6.4 Production of Plant Lectins 6.4.1 Recombinant Plant Lectins 6.5 Purification of Plant Lectins or Haemagglutinins 6.6 Functions of Plant Lectins 6.7 Lectin Applications 6.7.1 Pathogen Controlling Strategies 6.7.1.1 Insecticidal 6.7.1.2 Fungicidal 6.7.1.3 Antiviral 6.7.1.4 Anti-Microbial Activity 6.7.1.5 Anti-Parasitic Activity 6.7.1.6 Antibacterial Activity 6.7.2 Medicinal Purposes 6.7.2.1 Cancer Treatment Antitumour Drugs Through Apoptosis Lectin Based Delivery System 6.7.2.2 Clinical Diagnosis 6.7.2.3 Detection Using ELLA 6.7.2.4 Recognition of Different Groups of Blood 6.7.2.5 Biosensors 6.7.2.6 Possible Treatment of Diabetes 6.7.3 Other Applications 6.7.3.1 Chromatographic Type 6.7.3.2 Lectin Microarray 6.7.3.3 Detection of Glycoconjugates in Solution 6.7.3.4 Detection of Glycoconjugates on Cells and Organelles 6.7.3.5 Mapping Neurological Pathways 6.7.3.6 Typing in Bacteria 6.7.3.7 Agricultural Purposes 6.7.3.8 Lectin Blotting 6.7.3.9 Flow Cytometry 6.8 Conclusion References Chapter 7: Microbial Lectins 7.1 Introduction 7.2 Microbial Lectins 7.2.1 Bacterial Lectins 7.2.2 Fungal Lectins 7.2.3 Viral Lectins 7.2.4 Protozoal Lectins 7.3 Roles of Microbial Lectins 7.3.1 Biofilm Formation 7.3.2 Antimicrobial Activity 7.3.3 Antitumor Activity 7.3.4 Mitogenic Activity 7.3.5 Bioflocculation 7.3.6 Bioremediation 7.4 Future Perspectives and Applications 7.5 Conclusion References Chapter 8: Regulation of Immune Responses by Lectins 8.1 Introduction 8.2 Type of Lectins 8.3 Immune Functions 8.3.1 Lectin Mediated Immunity in Plants 8.3.2 Lectin Mediated Immunity in Animals 8.3.3 Lectin Mediated Immunity in Fish 8.3.4 Lectin Mediated Immunity in Shellfish 8.4 Regulation in Plants 8.5 Regulation in Animals 8.6 Prospects of Lectins in Fish Health Management 8.7 Conclusion References Chapter 9: Lectin-Carbohydrate Interactions in Pathogenesis 9.1 Introduction 9.2 Pathogen-Lectin and Host-Glycan Interaction in Pathogenesis 9.2.1 Viral Lectins Versus Host Glycans 9.2.2 Bacterial Lectins Versus Host Glycans 9.2.3 Fungal Lectins Versus Host Glycans 9.3 Host-Lectin and Pathogen-Glycans Interactions in Pathogenesis 9.3.1 Membrane Associated Lectins 9.3.2 Soluble Lectins 9.4 Reverse Lectin Approach Against Pathogen Glycans 9.5 Conclusion References Chapter 10: Lectins in Health and Diseases: Mannan-Binding Lectin and Infectious Diseases 10.1 Introduction 10.2 MBL-Mediated Immune Response 10.3 MBL Structure 10.4 MBL Polymorphic Variants 10.5 MBL in Bacterial Infections 10.6 MBL in Parasitic Infections 10.7 MBL in Viral Infections 10.7.1 MBL in SARS-CoV-2 Infection 10.8 MBL in Fungal Infections 10.9 Pathogens´ Survival Strategies 10.10 Perspectives 10.11 Conclusion References Chapter 11: Lectins in Health and Diseases: Galectins and Cancer 11.1 Introduction 11.2 What Are Galectins? 11.3 Structure, Function and Binding Activity of Galectins 11.4 Subcellular Localization and Unconventional Secretion of Galectins 11.5 Cancer and Its Hallmarks 11.6 The Tumour Microenvironment (TME) 11.6.1 Galectin-1 Within the TME 11.6.2 Galectin-3 Within the TME 11.7 Role of Different Galectins in Cancer 11.7.1 Galectin-1 and Cancer 11.7.1.1 Galectin-1 Structure and Its Binding Activity 11.7.1.2 Intracellular and Extracellular Activities of Galectin-1 11.7.1.3 Galectin-1 in Cellular Transformation 11.7.1.4 Galectin-1 in Mediating Angiogenesis, Cancer Cell Adhesion, and Metastasis 11.7.1.5 Immune Regulation of TME via Galectin-1 11.7.2 Galectin-3 in Cancer 11.7.2.1 Galectin-3 Structure and Binding Activities 11.7.2.2 Intracellular and Extracellular Activities 11.7.2.3 Galectin-3 in Cellular Transformation 11.7.2.4 Galectin-3 Mediating Angiogenesis, Cancer Cell Adhesion, and Metastasis 11.7.2.5 Immune Regulation of TME via Galectin-3 Effect on Lymphocytes Effect on Macrophages 11.7.3 Galectin-9 in Cancer 11.7.3.1 Galectin-9 Structure and Binding Activities 11.7.3.2 Galectin-9 in Tumour Regulation 11.7.3.3 Immune Regulation via Galectin-9 11.7.4 Other Galectins in Cancer 11.7.4.1 Galectin-4 in Cancer 11.7.5 Galectin-7 in Cancer 11.7.6 Galectin-8 in Cancer 11.8 Galectin-Targeted Therapeutic Strategies in Cancer 11.8.1 Carbohydrate-Based Small-Molecule Inhibitors 11.8.2 Natural Polysaccharide-Based Inhibitors 11.8.3 Peptide-Based Inhibitors of Galectins 11.8.4 Neutralizing Antibodies in Galectin Inhibition 11.8.5 SiRNA-Mediated Inhibition of Galectins 11.9 Conclusion and Future Perspective: Galectins in Cancer and the Development of Therapeutics References Chapter 12: Lectins in Diagnostic Tools and Therapeutic Agents 12.1 Introduction 12.2 Lectins in Diagnostic Tools 12.3 Lectins as Therapeutic Agents 12.4 Conclusion References Chapter 13: Modern Approach in Lectin-Based Nanomedicine 13.1 Introduction 13.1.1 Types of Glyconanoparticles 13.2 Gold Glyconanoparticles 13.3 Glyco-Quantum Dots 13.4 Magnetic Glyconanoparticle 13.5 Applications of Glyconanoparticles in Nanomedicine 13.5.1 As Lectin-Based Drug Delivery 13.5.2 As Detection and Imaging Tools 13.6 Conclusion References