Serine proteases and their serpin inhibitors in the nervous system : regulation in development and in degenerative and malignant disease
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書誌事項
Serine proteases and their serpin inhibitors in the nervous system : regulation in development and in degenerative and malignant disease
（NATO ASI series, ser. A . Life sciences ; v. 191）
Plenum Press, c1990
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注記
"Proceedings of a NATO Advanced Research Workshop on Regulation of Extravascular Fibrinolysis in Nervous System Development and Disease, held July 2-8, 1989, in Maratea, Italy"--T.p. verso
"Published in cooperation with NATO Scientific Affairs Division."
Includes bibliographical references and index
内容説明・目次
内容説明
Proceedings of a NATO ARW held in Maratea, Italy, July 2-8, 1989
目次
Section I: Biochemistry and Cell Biology of Serine Proteases and Serpins.- 1: Thrombin Structural Regions in Determining Bioregutatory Functions.- Acknowledgments.- References.- 2: Regulation and Control of the Fibrinolytic System.- Main Components of the Fibrinolytic System.- Plasminogen.- Physiological Plasminogen Activators.- Tissue-type plasminogen activator (tPA).- Urokinase-type plasminogen activator (uPA).- Inhibitors of the I1brinolytic System.- Alpha2-Antiplasmin.- Plasminogen Activator Inhibitor-1 (PAL-1).- Regulation and Control of Physiological Fibrinolysis.- Molecular Interactions Between the Components of the Fibrinolytic System.- Mechanism of Action of tPA.- Mechanism of Action of uPA.- Pathophysiological Aspects of Fibrinolysis.- Excessive Fibrinolysis.- Alpha2-Antiplasmin Deficiency and Bleeding.- Excess tPA Levels and Bleeding.- Impairment of Fibrinolysis.- PAI Activity and Thrombosis.- Plasminogen Deficiency and Thrombosis.- Plasminogen Activator Deficiency and Thrombosis.- Conclusion.- References.- 3: A Key Molecule Dictating and Regulating Surface Plasmin Formation: The Receptor for Urokinase Plasminogen Activator.- Physiologically Invasive Processes.- Plasmin Formation.- The uPA Receptor.- Receptor-binding region in uPA.- Structure of the uPA receptor.- uPA Receptors and the Focal Adhesion Sites.- Plasminogen Activation with Surface-Bound Reactants.- Regulation of the uPA-uPA Receptor Interaction.- Conclusions.- References.- 4: Regulation of Tissue Plasminogen Activator Secretion from Human Endothelial Cells.- Results.- Discussion.- References.- 5: Thrombin Disintegrates Cell Surface Urokinase Focal Adhesion Plaques and Decreases Cell Extension: Implications for Axonal Growth.- Materials and Methods.- Materials.- Methods.- Cell culture.- Interference reflection microscopy.- Immunofluorescence labeling of urokinase and vinculin.- Assay of the Growth Factors.- Results.- Discussion.- Acknowledgments.- References.- 6: Structure and Function of Tissue-Type Plasminogen Activator.- Biology of tPA.- tPA is a Mosaic Protein.- Interaction with plasminogen.- Interaction with PAI-1.- Interaction with fibrin.- Interaction with receptors in the liver.- Extravascular Cofactors.- Heparin.- Fibronectin.- Thrombospondin and Histidine-Rich Glycoprotein.- Miscellaneous.- References.- 7: The Heparin Binding Site and Activation of Protease Nexin I.- Protease Nexin I.- Antithrombin III.- Heparin Cofactor II.- Methods.- Results and Discussion.- Heparin Binding Serpins: Structure and Reactive Centre.- Protease Nexin I: Identification of the Heparin Binding Site.- Evidence From Antithrombin mutants....- Modelling of the Site.- Conclusion.- Acknowledgments.- References.- 8: Polypeptide Chain Structure of Inter-?-Trypsin Inhibitor and Pre-?-Trypsin Inhibttor: Evidence for Chain Assembly by Glycan and Comparison with Other "Kunin"-Containing Proteins.- Experimental Procedures.- Materials.- Polyacrylamide Gel Electrophoresis.- Trypsin Inhibitor Counterstained Gels.- Protein Purification.- Protein Fragmentation.- Amino Acid Sequence Analysis.- Chemical Deglycosylation.- Enzymatic Deglycosylation.- Zone Electrophoresis of I?I and P?I kDa.- Results.- Purification of SDS-Stable Trypsin Inhibitors from Human Plasma.- Identity of the Inhibitors.- Chain Composition.- Chain Stoichiometry.- Composition of the Crosslinks(s).- Location of the Crosslink.- Multiple Forms of Kunin-Containing Proteins.- Summary.- Acknowledgments.- References.- 9: Regulation of Protease Nexin I Activity and Target Protease Specificity by the Extracellular Matrix.- Results.- Fibroblasts Accelerate the Inactivation of Thrombin by PNI.- Fibroblasts Block the Ability of PNI to Inactivate Urokinase and Plasmin.- Discussion.- Summary.- Acknowledgments.- References.- Section II: Molecular Biology of Serine Proteases and Serpins.- 10: Induction of the Urokinase-Type Plasminogen Activator Gene by Cytoskeeton-Disrupting Agents.- Materials and Methods.- Materials.- Cell Culture.- cDNA Probes.- RNA Analysis.- Nuclear run on-transcription.- CAMP-dependent Protein Kinase Assay.- DNA Transfection and CAT Assay.- Transgenic Mice.- Results.- Colchicine Induces uPA mRNA and Gene Transcription.- Cytochalasin B Also Induces uPA Gene Expression.- Induction of uPA mRNA by Colchicine or Cytochalasin B Treatment Involves Protein kinase C.- Induction of uPA Gene Expression is Mediated by Cis-Acting Element.- Expression of uPA LacZ Chimeric Gene in Transgenic Mice.- Discussion.- References.- 11: Use of Protein Chemistry and Molecular Biology to Determine Interaction Areas Between Proteases and Their Inhibitors: The Thrombin-Hirudin Interaction as an Example.- Properties of Thrombin and Hirudin.- Thrombin.- Hirudin.- Kinetic Mechanism of the Inhibition of Thrombin by Hirudin.- Identification of Interaction Areas on Thrombin.- Derivatives of ?-thrombin With Modified Active Sites.- Proteolysed Forms of Thrombin and Peptide-Specific Antibodies.- Protection Against Chemical Modification and Proteolysis.- Identification of Interaction Areas on Hirudin.- Importance of Basic Amino Acid Residues.- Ionic Interactions Involving the C-terminal Region.- Interaction With the N-terminus.- Conclusions.- References.- 12: Signal Transduction Chains Involved in the Control of the Fibrinolytic Enzyme Cascade.- Hormonal Modulation of the Fibrinolytic System.- Protein Kinase C-dependent Pathway.- Tyrosine Specific Protein Kinase Dependent Pathway.- Regulation by Steroid Hormones.- Regulation by Cyclic AMP.- Regulation Via the Hypothalamic-Gonadal Axis.- Regulation by Cytokines.- Summary.- References.- 13: Rodent Serpins: Accelerated Evolution and Novel Specificities.- Materials and Methods.- Genetic Analysis.- Cosmid Clone Analysis.- Sequence Analysis of Exon 5.- Results and Discussion.- Serpin Genes and Genetics.- Structure of the Spi-2 Locus.- Evolution of the Reactive Centre Region of the Serpins.- Accelerated Evolution in the Reactive Centre Domain.- Reactive Centre Regions Within the Spi-2 Gene Cluster.- Expression of the Spi-2 Genes in Mouse.- References.- 14: Structure of the Human Protease Nexin Gene and Expression of Recombinant forms of PNI.- Materials and Methods.- Tissue Culture.- Preparation of mRNA and Northern Blot Analysis.- Construction of Human Genomic Library.- Hybridization Procedures.- DNA Manipulations.- DNA Sequencing and Analysis.- Expression of PNI in CHO Cells.- Expression of Recombinant PNI in Insect Cells.- Thrombin Inhibition Assay of PNI.- PNI/Protease Complex Formation.- Results.- Identification of Two Different Forms of PNI.- Analysis of PNI mRNA Expression.- Differential Expression of PNI and Plasminogen Activator.- Structure of the PNI Gene.- Comparison of the PNI Gene and the PAI-1 Gene.- Expression of Recombinant PNI in Mammalian and Insect Cells.- Characterization of CHO Recombinant Alpha PNI.- Discussion.- Summary.- References.- 15: Evolutionary Adaptations of Serpins and Their Use in Designing New Proteinase Inhibitors.- How Do Serpins Function as Inhibitors?.- Is Serpin Complex Formation Reversible?.- How are Serpins Regulated?.- Is Carbohydrate Required for Inhibitory Activity?.- Are all Elastase Specific Serpins Oxidative sensitive?.- What are the P1 Residues in Naturally Occurring Oxidation Resistant Elastase Inhibitors?.- How Have Elastase Inhibitors Evolved?.- Can We Change Inhibitor Specificity?.- Summary.- References.- Section III: Serine Proteases in the Nervous System.- 16: Plasminogen Activator in the Developing Nervous System.- Methods.- Cell Cultures.- Plasminogen Activator Assays.- 125I-tPA Binding Assay.- Proteolysis of Fibronectin.- tPA mRNA.- Results.- Discussion.- Acknowledgments.- References.- 17: Multiple Roles for Plasminogen Activator System in Nervous System Development.- Neuronal Migration.- Glial Proliferation.- Neuritic Fasciculation.- Neuritogenesis.- Conclusions.- References.- 18: Interaction of Plasminogen Activators with the Neuronal Surface.- Neuronal uPA.- Neuronal Inhibitor of uPA.- Neuronal tPA.- References.- 19: Glial Plasminogen Activators in Developing and Regenerating Neural Tissue.- Results and Discussion.- Modulation of Neural Cytoarchitecture by PA/Plasmin In Vitro.- PAs in Schwann Cells.- PAs in Differentiating Astroglia.- Role of Plasmin/PA Activities in PNS Regeneration.- Concluding Remarks.- Acknowledgment.- References.- 20: Plasminogen Activators in Development, Injury and Pathology of the Neuromuscular System.- Release of PAs from Muscle after Axotomy or Nerve Crush.- Muscle PAs Increase After Muscle Axotomy.- The Nerve Crush Paradigm.- Degradation of Muscle Adhesive Macromolecules by PAs.- Muscle PAs Decline During Synapse Elimination.- PAs in Lower Motor Neuron Diseases.- The Mutant Wobbler Mouse.- Study of PA and Inhibitors in ALS.- Conclusion.- Acknowledgments.- References.- 21: Relationship Between Plasminogen Activators and Regeneration Capacities of Rat Skeletal Muscle.- Materials and Methods.- Chemicals and Reagents.- Preparation of Muscle Extracts.- Cell Cultures.- Electron Microscopy.- Regeneration Studies.- Assay of PAs.- Miscellaneous.- Results.- In Vivo Activities.- In Vitro Activities.- Regeneration Studies.- tPA.- uPA.- Discussion.- Conclusion.- Acknowledgments.- References.- Section IV: Balance of Proteases and Serpins in the Nervous System.- 22: A Cascade Approach to Synapse Formation Based on Thrombogenic and Fibrinolytic Models.- Proteases at the Neuromuscular Junction.- Inhibitors of Serine Proteases.- Kunitz-Type Inhibitors (Kunins).- Serpins.- Protease nexin I.- Plasminogen activator inhibitors 1,2 and 3.- Protease nexin II (PNII).- Serpins in yhe Nervous System.- Serpins in the Central Nervous System.- Neurite Outgrowth Promotion.- Neuronal Survival.- Distribution of Serpins in the CNS.- Serpins in the Peripheral Nervous System.- Thrombogenic and Fibrinolytic Cascade Models of Synapse Formation and Plasticity.- Summary.- References.- 23: Localized Extracellular Proteolysis May Convey Inductive Signals Between Nerve and Muscle Cells During Synaptogenesis.- Short-Range Cellular Interactions.- Neural Regulation of Muscle Basal Lamina Proteoglycan.- Neural Remodeling of the Muscle Basal Lamina.- Desorptive Actions of Inductive Polymer Microbeads.- Alternative Modes of Inductive Cell Communication.- Possible Transduction of Pericellular Proteolysis by Ecm Receptors.- Indirect Proteolytic Regulation of Growth Factor Receptors.- Regulation of Cellular Adhesion, Proliferation and Differentiation.- Summary.- References.- 24: Steps in Establishing a Biological Relevance for Gliaderived Nexin.- Neurite Outgrowth Due to Serine Protease Inhibition.- Characterization of The Primary Sequence.- GDN Biological Effects in Vitro.- Localization of GDN.- Up-Regulation of GDN Following Rat Sciatic Nerve Lesion.- Conclusion.- References.- Section V: Serpins in Degenerative and Malignant Neurologic Diseases.- 25: Protease Inhibitors in Neurologic Diseases.- Protease Inhibitors in Amyotrophic Lateral Sclerosis.- Protease Inhibitors in Familial Amyloidotic Polyneuropathy.- Direct measurement of inhibitors in sera.- Indirect assumption of the state of protease and protease inhibitors from the clinical symptoms of FAP.- Possible Application of Proteases to the Management of FAP.- Protease Inhibitors and Other Neurologic Diseases.- Concluding Comments.- Acknowledgments.- References.- 26: Presence and Significance of ?1-Antitrypsin in Human Brain Tumors.- Material and Methods.- Biochemical Studies.- Immunohistochemical Methods.- Results.- Biochemical Results.- Immunohistochemical Results.- Discussion.- Summary.- Acknowledgment.- References.- 27: Serpins and Brain Tumors: Roles in Pathogenesis.- Experimental Procedures.- Materials.- Methods.- Cell culture.- Preparation of conditioned media from 9L cells.- Tissue processing.- Concanavalin-A chromatography.- Inhibition or release of labeled extracellular matrix.- Fibrin zymography.- Reverse fibrin zymography.- Radioiodination of proteins.- Complex formation studies.- Extraction and purification of RNA.- Northern hybridization.- Results.- Inhibition of Matrix Degradation by 9L Conditioned Medium.- Fibrin Zymography.- Reverse Fibrin Zymography.- Complex Formation Studies with Labeled Urokinase or Thrombin.- Northern Hybridization with Protease Nexin I cDNA.- Discussion.- Summary.- Acknowledgments.- References.- 28: A Serine Protease Inhibitor Domain Encoded Within the Alzheimer Disease Associated Amyloid ?-Protein Precursor Gene.- The Relationship Between the APP Gene and Familial Alzheimer's Disease.- A Kunitz-Type Serine Protease Inhibitor Domain within APP.- Expression of Alternate Transcipts for the APP Gene.- Final Considerations.- References.- 29: The Serpin, al-Antichymotrypsin, in Brain Aging and Diseases of The Nervous System.- ?1-Antichymotrypsin in Alzheimer Amyloid Deposits 321.- Amyloid Deposition During Normal Aging.- The Origin of Amyloid Proteins in Alzheimer's Disease.- Role of Proteases and Inhibitors in Amyloid Formation.- Special Association Between ?1-Antichymotrypsin and ?-Protein in Amyloid.- Is ?1-Antichymotrypsin Part of a Brain 'Acute Phase Response'?.- Summary.- References.- 30: Protease Nexin I Immunostaining in Alzheimer's Disease.- Materials and Methods.- Results.- Discussion.- References.- Section VI: The Maratea Conference.- Photo Layout.- Participants.
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