Cellular Peptidases in Immune Functions and Diseases 2

2002
ISBN: 978-1-4757-8649-1
Verlag: Springer US

Buch, Englisch, Band 477, 522 Seiten, Paperback, Format (B × H): 178 mm x 254 mm, Gewicht: 1003 g

Reihe: Advances in Experimental Medicine and Biology

Of the many special roles played by proteolytic enzymes in immune reactions, this book addresses different aspects of membrane peptidases, signal transduction via ligation of membrane peptidases (especially of dipeptidyl peptidase IV/CD26 and aminopeptidase N/CD13), and regulation of membrane peptidases in vivo and in vitro. A number of newly discovered peptidases (including cathepsin F, W and X, carboxypeptidase X, attractin) are described, with special emphasis given to the role of peptidases in immune and defense reactions and in the pathogenesis of inflammatory and other diseases, including rheumatoid arthritis, pancreatitis, multiple sclerosis, Alzheimer's disease and tumours of various origins. The focus on the involvement of a selection of proteolytic enzymes in immune reactions and diseases is a unique feature of this multifaceted work, which combines biochemical, immunological and clinical research reports with literary reviews of the field.

Zielgruppe

Research

Autoren/Hrsg.

Ansorge, Siegfried

Langner, Jürgen

Fachgebiete

• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Klinische und Innere Medizin Immunologie
• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Klinische und Innere Medizin Rheumatologie, Muskelerkrankungen
• Naturwissenschaften Chemie Chemie Allgemein Pharmazeutische Chemie, Medizinische Chemie
• Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)
• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Klinische und Innere Medizin Onkologie, Krebsforschung

Inhaltsverzeichnis

Membrane Ectopeptidases with Influence on Immune Functions.- Review: The Role of Membrane Peptidase in Immune Functions.- Structure and Function of Aminopeptidase N.- Modulation of WNT-5At Eexpression by Actinonin: Linkage of APN to the WNT-Pathway?.- Enzymatic Activity Is Not A Precondition For The Intracellular Calcium Increase Mediated By mAbs Specific For Aminopeptidase N/CD13.- Transforming Growth Factor-? Increases the Expression of Aminopeptidase N/CD13 mRNA and Protein in Monocytes and Monocytic Cell Lines.- Cell-Cell Contact Between Lymphocytes and Fibroblast-Like Synovioctyes Induces Lymphocytic Expression of Aminopeptidase n/cd13 and Results in Lymphocytic Activation.- Natural Substrates of Dipeptidyl Peptidase IV.- Relating Structure to Function in the Beta-Propeller Domain of Dipeptidyl Peptidase IV.- Development of a Tertiary-Structure Model of the C-Terminal Domain of DPP IV.- Post Proline Cleaving Peptidases Having DP IV Like Enzyme Activity.- A New Type of Fluorogenic Substrates for Determination of Cellular Dipeptidyl Peptidese IV (DP IV/CD26) Activity.- Potent Inhibitors of Dipeptidyl Peptidase iv and Their Mechanisms of Inhibition.- N-Terminal HIV-1 Tat Nonapeptides as Inhibitors of Dipeptidyl Peptidase IV. Conformational Characterization.- Signal Transduction Events Induced or Affected by Inhibition of the Catalytic Activity of Dipeptidyl Peptidase IV (DP IV, CD26).- Specific Inhibitors of Dipeptidyl Peptidase IV Suppress mRNA Expression of DP IV/CD26 and Cytokines.- Dipeptidyl Peptidase IV in Inflammatory CNS Disease.- Dipeptidyl Peptidase IV (CD26): Role in T Cell Activation and Autoimmune Disease.- Effects of Nonapeptides Derived From the N-terminal Structure of Human Immunodeficiency Virus-1 (HIV-1) Tat on Suppression of CD26-Dependent T CellGrowth.- DNA Synthesis in Cultured Human Keratinocytes and Hacat Kerationcytes is Reduced by Specific Inhibition of Dipeptidyl Peptidase IV (CD26) Enzymatic Activity.- Attractin: A Cub-Family Protease Involved in T Cell-Monocyte/Macrophage Interactions.- Analogs of Glucose-Dependent Insulinotropic Polypeptide With Increased Dipeptidyl Peptidase IV Resistance.- Dipeptidyl Peptidase IV (DPP IV, CD26) In Patients With Mental Eating Disorders.- The Membrane-Bound Ectopeptidase CPM as a Marker Of Macrophage Maturation in vitro And in vivo.- Matrix Metalloproteinases (MMP-8, -13 and -14) Interact with the Clotting System and Degrade Fibrinogen and Factor XII (Hagemann Factor).- The Neprilysin Family in Health and Disease.- Cellular Endopeptidases: New Cathepsins; Results from Knock-out-mice; Regulatory Aspects.- Review: Novel Cysteine Proteases of the Papain Family.- Development and Validation of Homology Models of Human Cathepsins K, S, H, and F.- The Function of Propeptide Domains of Cysteine Proteinases.- Human Cathepsins W and F form A New Subgroup of Cathepsins that is Evolutionary Separated from the Cathepsin B- and L-Like Cysteine Proteases.- Cathepsin K Expression in Human Lung.- Expression of Cathepsins B and L in Human Lung Epithelial Cells is Regulated by Cytokines.- Functions of Cathepsin K in Bone Resorption.- Ceramide as an Activator Lipid of Cathepsin D.- Human Cathepsin X.- A Novel Proteolytic Mechanism for Termination of the Ca2+ Signalling Evoked by Proteinase-Activated Receptor-1 (PAR-1) in Rat Astrocytes.- Natural and Synthetic Inhibitors of The Tumor-Associated Serine Protease Urokinase-Type Plasminogen Activator.- Processing of Interleukin-18 by Human Vascular Smooth Muscle Cells.- Peptidases and Peptidase Inhibitors in Pathogensis of Diseases.- Review:Peptidases and Peptidase Inhibitors in the Pathogenesis of Diseases.- The Role of Proteolysis in Alzheimer’s Disease.- Observing Proteases in Living Cells.- The Role of Cysteine Proteases in Intracellular Pancreatic Serine Protease Activation.- Peptidases in the Asthmatic Airways.- Inactivation of Interleukin-6 by Neutrophil Proteases at Sites of Inflammation.- Antisense Inhibition of Cathepsin Bina Human Osteosarcoma Cell Line.- Protease-Protease Inhibitor Balance in the Gastric Mucosa.- The Role of Bacterial and Host Proteinases in Periodontal Disease.- Multifunctional Role of Proteases in Rhumatic Diseases.- Evidence of Proteolytic Activation of Transforming Growth Factor ? in Synovial Fluid.- Matrix Metalloproteinases and Tace Play A Role in The Pathogenesis of Endometriosis.- Influence of Proliferation, Differentiation and Dedifferentiation Factors on the Expression of the Lysosomal Cysteine Proteinase Cathepsin L (CL) in Thyroid Cancer Cell Lines.