Ansorge / Langner | Cellular Peptidases in Immune Functions and Diseases | Buch | 978-0-306-45616-9 | sack.de

Buch, Englisch, Band 421, 338 Seiten, Format (B × H): 178 mm x 254 mm, Gewicht: 1970 g

Reihe: Advances in Experimental Medicine and Biology

Ansorge / Langner

Cellular Peptidases in Immune Functions and Diseases

Buch, Englisch, Band 421, 338 Seiten, Format (B × H): 178 mm x 254 mm, Gewicht: 1970 g

Reihe: Advances in Experimental Medicine and Biology

ISBN: 978-0-306-45616-9
Verlag: Springer


This book stems from a conference held at Magdeburg-Herrenkrug, Germany, in November 1996 on "Cellular Peptidases in Immune Functions and Diseases. " This sympo­ sium was designed to bring together scientists from diverse areas of expertise to discuss issues of newly identified relevance of proteolytic processes and their role as molecular regulators in the immune system and in diseases. The meeting was organized by the Son­ derforschungsbereich 387 of the Deutsche Forschungsgemeinschaft "ZelluHire Proteasen, Bedeutung fiir Immunmechanismen und entziindliche Erkrankungen," which links re­ search groups from the Otto von Guericke University Magdeburg and the Martin Luther University Halle. It has become clear during the last decade that proteolysis, the processing and degrada­ tion of peptides and proteins, has to be considered as a special level of epigenetic control of practically all processes of life and-an understanding dating from the last three years or so--also of cell death or apoptosis. There is also increasing evidence that proteolysis does play a crucial role in all areas of immune functions as well as in inflammatory and neoplastic diseases. Cellular proteases have central functions in natural (nonspecific) as well as acquired in the cognitive phase (antigen processing and presen­ (specific) immunity. They are involved tation), in the activation phase (e. g., generation and processing of cytokines, function of CD26, CD 13, processing of transcription factors) as well as in the effector phase of the im­ mune response (e. g., complement system, granzymes, elastase, proteinase 3.
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I: Membrane Peptidases in Immune Functions and Inflammation.- 1. Membrane Metalloendopeptidases in Immune Function and Disease.- 2. Structural Studies of Aminopeptidase P: A Novel Cellular Peptidase.- 3. Aminopeptidase P: A Cell-Surface Antigen of Endothelial and Lymphoid Cells.- 4. Human Lymphocyte X-Prolyl Aminopeptidase (Aminopeptidase P)-like Protein: A New Member of the Proline Peptidase Family?.- 5. Specific Inhibitors of Aminopeptidase P: Peptides and Pseudopeptides of 2-Hydroxy-3-Amino Acids.- 6. ?-Glutamyl Transpeptidase, a Blood-Brain Barrier Associated Membrane Protein: Splitting Peptides to Transport Amino Acids.- 7. Structure and Expression of Aminopeptidase N.- 8. Activation-Dependent Induction of T Cell Alanyl Aminopeptidase and Its Possible Involvement in T Cell Growth.- 9. Antisense-Mediated Inhibition of Aminopeptidase N (CD13) Markedly Decreases Growth Rates of Hematopoietic Tumour Cells.- 10. Co-Incubation of Lymphocytes with Fibroblast-like Synoviocytes and Other Cell Types Can Induce Lymphocytic Surface Expression of Aminopeptidase N/CD13.- 11. Two Transfected Endothelial Cell Lines Expressing High Levels of Membrane Bound or Soluble Aminopeptidase N.- 12. Aminopeptidase N-Mediated Signal Transduction and Inhibition of Proliferation of Human Myeloid Cells.- 13. Regulation of Thymic Development by Neprilysin Inhibition.- 14. Proteases of Isolated Pancreatic Acinar Cells after Caerulein Hyperstimulation.- II: CD26/Dipeptidylpeptidase IV on Lymphocytes.- 15. Structure of CD26 (Dipeptidyl Peptidase IV) and Function in Human T Cell Activation.- 16. Molecular Associations Required for Signalling via Dipeptidyl Peptidase IV (CD26).- 17. CD26/Dipeptidyl Peptidase IV in Lymphocyte Growth Regulation.- 18. CD26 Is Involved in Regulation of CytokineProduction in Natural Killer Cells.- 19. The Effect of Anti-CD26 Antibodies on DNA Synthesis and Cytokine Production (IL-2, IL-10 and IFN-?) Depends on Enzymatic Activity of DP IV/CD26.- 20. New Fluorogenic Dipeptidyl Peptidase IV/CD26 Substrates and Inhibitors.- 21. Molecular Analyses of Human and Rat Dipeptidyl Peptidase IV.- 22. A Molecular Model of the Active Site of Dipeptidyl Peptidase IV: Explanation of the Substrate Specificity and Interaction with Inhibitors.- 23. The Level of CD26 Determines the Rate of HIV Entry in a CD4+ T-Cell Line.- 24. HIV-1 Envelope gp 120 and Viral Particles Block Adenosine Deaminase Binding to Human CD26.- 25. Further Characterization of DPP IV-?, a Novel Cell Surface Expressed Protein with Dipeptidyl Peptidase Activity.- 26. Expression of Dipeptidylpeptidase IV (DPP IV/CD26) Activity on Human Myeloid and B Lineage Cells, and Cell Growth Suppression by the Inhibition of DPP IV Activity.- 27. CD26 as a Positive Regulator of HIV Envelope-Glycoprotein Induced Apoptosis in CD4+ T Cells.- 28. Comparative Study of CD26 as a Thl-like and CD30 as a Potential Th2-like Operational Marker in Leprosy.- III: Peptidases Involved in Cytokine Actions and in the Pathogenesis of Disease.- 29. Regulation of Neutrophil Activation by Proteolytic Processing of Platelet-Derived a-Chemokines.- 30. Selective Proteolytical Cleavage of the Ligand-Binding Chains of the IL-2-Receptor and IL-6-Receptor by Neutrophil-Derived Proteases.- 31. In Vitro Effects of ?-Glutamyltranspeptidase Inhibitor Acivicin on Human Myeloid and B Lineage Cells.- 32. Expression of Several Matrix Metalloproteinase Genes in Human Monocytic Cells.- 33. Lysosomal Cysteine Peptidases and Malignant Tumours.- 34. Expression of Cysteine Protease Inhibitors Stefin A, Stefin B, and Cystatin Cin Human Lung Tumor Tissue.- 35. Contribution of the Proteasome to the a-Secretase Pathway in Alzheimer’s Disease.- 36. Dipeptidyl Peptidase IV (CD26) and Alzheimer Amyloid Protein Precursor (APP) in Polymyositìs.- 37, The HIV Protease and Therapies for AIDS.- 38. Leukodiapedesis, Function, and Physiological Role of Leucocyte Matrix Metalloproteinases.- 39. Matrix Metalloproteinases in Experimental Autoimmune Encephalomyelitis.- 40. Interaction of Transforming Growth Factor ß (TGFß) with Proteinase 3.- 41. Liver Cysteine Proteinases in Macrophage Depression Induced by Gadolinium Chloride.- Contributors.


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