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Lectin Methods and Protocols: (9 Methods in Molecular Medicine)

Lectin Methods and Protocols: (9 Methods in Molecular Medicine)

          
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About the Book

Lectins have in the past been regarded by many scientists as curious proteins of uncertain structure and specificity that bind to carbohydrates of dubious significance themselves. All this is rapidly changing. The functional importance of glycosylation in cell-cell and cell-pathogen interactions, as well as intracellular events, has been recognized by the explosion of the science of glycobiology. This has been paralleled by the realization that lectins, once they have been well characterized, can be extremely useful tools for exam- ing structural changes in glycosylation and their functional consequences for human pathophysiology. Different lectins vary considerably in their degree of specificity. Some, such as wheatgerm agglutinin, have fairly broad specificity (for glucosamine or sialic acid), whereas others, such as Maackia amurensis, are specific not only for a single carbohydrate, but also for its linkage (2-3 linked sialic acid). Lectins with relatively broad specificity may be very useful as an adjunct to isolation or quantification of soluble glycoproteins, whereas lectins of known, and precise, specificity will be more useful for characterization of carbo- drate structure. We have included an appendix in Lectin Methods and Pro- cols that provides the known specificities of all lectins cited in the text.

Table of Contents:
Lectin Histochemistry and Cytochemistry.- Light Microscopy.- Lectin Histochemistry and Cytochemistry—Light Microscopy.- Lectin—Gold Histochemistry on Paraffin and Lowicryl K4M Sections Using Biotin and Digoxigenin-Conjugated Lectins.- Use of Fluorochrome-Labeled Lectins in Light Microscopy.- The Use of Lectins in Combination with Enzymatic Digestion for the Study of Glycoconjugates in Cartilage.- Applications of Lectin Histochemistry and Cytochemistry in Diagnosis and Prognosis.- Electron Microscopy.- Electron Microscopy.- Amplification of Lectin-Gold Histochemistry.- Electron Microscopic Methods for the Demonstration of Lectin-Binding Sites in Cancer Cell Lines.- Use of Lectins for Structural Analysis of Oligosaccharide Chains.- Application of Sequential Smith Degradation to Lectin Blots.- Blot Analysis with Lectins for the Evaluation of Glycoproteins in Cultured Cells and Tissues.- Characterization of HIV gp120 Envelope Glycoprotein by Lectin Analysis.- Use of Lectins for Characterization of O-Linked Glycans of Herpes Simplex Virus Glycoproteins.- Lectins for Detection of Altered Glycosylation of Circulating Glycoproteins.- Use of Lectin for Detection of Agalactosyl IgG.- Lectins for Detection of Altered Glycosylation of Circulating Glycoproteins.- Detection of Altered Glycosylation of ?-Fetoprotein Using Lectin-Affinity Electrophoresis.- Use of Lectin-Affinity Electrophoresis for Quantification and Characterization of Glycoforms of ?-1 Acid Glycoprotein.- ABO(H) Blood Group Expression on Circulating Glycoproteins.- Use of Lectins in Quantification of Soluble Glycoproteins.- Lectin/Antibody “Sandwich” ELISA for Quantification of Circulating Mucin as a Diagnostic Test for Pancreatic Cancer.- Quantification of Intestinal Mucins.- Lectins in AffinityPurification of Soluable Glycoproteins.- Purification and Characterization of Human Serum and Secretory IgA1 and IgA2 Using Jacalin.- Use of Lectins in Affinity Purification of HIV and SIV Envelope Glycoproteins.- T-Cell Receptor Purification.- Lectins in Flow Cytometry.- Use of Monomeric, Monovalent Lectin Derivatives for Flow Cytometric Analysis of Cell Surface Glycoconjugates.- Analysis of Subcellular Components by Fluorescent-Lectin Binding and Flow Cytometry.- Lectins as Tools for Cell Purification/Purging.- Lectins as Tools for the Purification of Liver Endothelial Cells.- The Use of Soybean Agglutinin (SBA) for Bone Marrow (BM) Purging and Hematopoietic Progenitor Cell Enrichment in Clinical Bone Marrow Transplantation.- Combined Lectin/Monoclonal Antibody Purging of Bone Marrow for Use in Conjunction with Autologous Bone Marrow Transplantation in the Treatment of Multiple Myeloma.- Effects of Lectins on Mammalian Cells.- Mechanisms and Assessment of Mitogenesis.- Mitogenic Effects of Lectins on Epithelial Cells.- Use of Lectins as Mitogens for Lymphocytes.- Effect of Lectins on Uptake of Polyamines.- Effects of Lectins on Cytoskeletal Organization in Mammalian Cells.- Effect of Lectins on Protein Kinase Activity.- Lectin-Induced Calcium Mobilization in Human Platelets.- Lectin-Triggered Superoxide/H2O2 and Granule Enzyme Release from Cells.- Cytotoxic Effects of Lectins.- Application of the Lectin-Dependent Cell-Mediated Cytotoxicity Assay to Bronchoalveolar Lavage Fluid and Venous Blood Samples Collected from Canine Lung Allografts.- Effects of Lectins in Organ Culture.- The Effect of Lectins on Crypt Cell Proliferation in Organ Culture.- Effects of Lectin Ingestion.- Effects of Lectin Ingestion on Animal Growth and Internal Organs.- Lectin Ingestion.- Assessment of Lectin Inactivation by Heat and Digestion.- Lectins in The Investigation of Neuronal Trafficking.- Use of Lectins as Transganglionic Neuronal Tracers in the Study of Unmyelinated Primary Sensory Neurons.- Use of Lectins in The Investigation of Pathogen-Host Interactions.- Lectin Inhibition of Bacterial Adhesion to Animal Cells.- Inhibition of HIV Infection by Lectin Binding to CD4.- Inhibition of HIV Infection by Lectin Binding to gp120.- Use of Lectins for Drug Delivery.- Absorption Enhancement by Lectin-Mediated Endo- and Transcytosis.- The Use of Lectins for Liposome Targeting in Drug Delivery.


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Product Details
  • ISBN-13: 9781617370243
  • Publisher: Humana Press Inc.
  • Publisher Imprint: Humana Press Inc.
  • Edition: Softcover reprint of hardcover 1st ed. 1998
  • Language: English
  • Returnable: Y
  • Spine Width: 36 mm
  • Width: 152 mm
  • ISBN-10: 161737024X
  • Publisher Date: 09 Nov 2010
  • Binding: Paperback
  • Height: 229 mm
  • No of Pages: 616
  • Series Title: 9 Methods in Molecular Medicine
  • Weight: 920 gr


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