Cellular Peptidases in Immune Functions and Diseases 2

ISBN-13: 9780306463839 / Angielski / Twarda / 2000 / 522 str.

Jurgen Langner; Siegfried Ansorge; Jrgen Langner

Opis

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.

Spis treści

Part I: Membrane Ectopeptidases with Influence on Immune Functions. Review: The Role of Membrane Peptidases in Immune Functions; U. Lendeckel, et al. Structure and Function of Aminopeptidase N; H. Sjöström, et al. Modulation of WNT-5a Expression by Actinonin: Linkage of APN to the WNT-Pathway? U. Lendeckel, et al. Enzymatic Activity is not a Precondition for the Intracellular Calcium Increase Mediated by mAbs Specific for Aminopeptidase N/CD13; A. Navarrete Santos, et al. Transforming Growth Factor-b Increases the Expression of Aminopeptidase N/CD13 mRNA and Protein in Monocytes and Monocytic Cell Lines; A. Kehlen, et al. Cell-Cell Contact Between Lymphocytes and Fibroblast-like Synoviocytes Induces Lymphocytic Expression of Aminopeptidase N/CD13 and Results in Lymphocytic Activation; D. Riemann, et al. Natural Substrates of Dipeptidyl Peptidase IV; I. De Meester, et al. Relating Structure to Function in the Beta-Propeller Domain of Dipeptidyl Peptidase IV: Point Mutations that Influence Adenosine Deaminase Binding, Antibody Binding and Enzyme Activity; M. D. Gorrell, et al. Development of a Tertiary-Structure Model of the C-Terminal Domain of DPP IV; W. Brandt. Post Proline Cleaving Peptidases Having DP IV Like Enzyme Activity: Post-Proline Peptidases; C. A. Abbott, et al. A New Type of Fluorogenic Substrates for Determination of Cellular Dipeptidyl Peptidase IV (DP IV/CD26) Activity; S. Lorey, et al. Potent Inhibitors of Dipeptidyl Peptidase IV and their Mechanisms of Inhibition; A. Stöckel-Maschek, et al. N-terminal HIV-1 TAT Nonapeptides as Inhibitors of Dipeptidyl Peptidase IV. Conformational Characterization; C. Mrestani-Klaus, et al. Signal Transduction Events Induced or Affected by Inhibition of the Catalytic Activity of Dipeptidyl Peptidase IV (DP IV,CD26); T. Kähne, et al. Specific Inhibitors of Dipeptidyl Peptidase IV Suppress mRNA Expression of DP IV/CD26 and Cytokines; M. Arndt, et al. Dipeptidyl Peptidase IV in Inflammatory CNS Disease; A. Steinbrecher, et al. Dipeptidyl Peptidase IV (CD26): Role in T Cell Activation and Autoimmune Disease; D. Reinhold, et al. Effects of Nonapeptides Derived from the N-Terminal Structure of Human Immunodeficiency Virus-1 (HIV-1) TAT on Suppression of CD26-Dependent T Cell Growth; S. Wrenger, et al. DNA Synthesis in Cultured Human Keratinocytes and HaCaT Keratinocytes is Reduced by Specific Inhibition of Dipeptidyl Peptidase IV (CD26) Enzymatic Activity; R. Vetter, et al. Attractin: A CUB-Family Protease Involved in T Cell-Monocyte/ Macrophage Interactions; J. S. Duke-Cohan, et al. Analogs of Glucose-Dependent Insulinotropic Polypeptide with Increased Dipeptidyl Peptidase IV Resistance; K. Kühn-Wache, et al. Dipeptidyl Peptidase IV (DPP IV, CD26) in Patients with Mental Eating Disorders; M. Hildebrandt, et al. The Membrane-Bound Ectopeptidase CPM as a Marker of Macrophage Maturation in Vitro and in Vivo; M. Rehli, et al. Matrix Metalloproteinases (MMP-8, -13, and -14) Interact with the Clotting System and Degrade Fibrinogen and Factor XII (Hagemann Factor); H.arald Tschesche, et al. The Neprilysin Family in Health and Disease; A. J. Turner, et al. Part II: Cellular Endopeptidases: New Cathepsins; Results from Knock-out-mice; Regulatory Aspects. Review: Novel Cysteine Proteases of the Papain Family; F. Bühling, et al. Development and Validation of Homology Models of Human Cathepsins K, S, H, and F; A. Fengler, Wolfgang Brandt. The Function of Propeptide Domains of Cysteine Proteinases; B. Wiederanders. Human Cathepsins W and F Form