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Matrix proteases in health and disease / edited by Niels Behrendt. -- Weinheim : Wiley-VCH, c2012. -- (58.174355 /M433m)

Contents

    CONTENTS
    
    List of Contributors XV
    Introduction 1
    Niels Behrendt
    1 Matrix Proteases and the Degradome 5
    Clara Soria-Valles, Carlos L'opez-Ot'yn, and Ana Guti'errez-Fern'andez
    1.1 Introduction 5
    1.2 Bioinformatic Tools for the Analysis of Complex Degradomes 6
    1.3 Evolution of Mammalian Degradomes 8
    1.3.1 Human Degradome 8
    1.3.2 Rodent Degradomes 10
    1.3.3 Chimpanzee Degradome 10
    1.3.4 Duck-Billed Platypus Degradome 11
    1.3.5 Other Degradomes 12
    1.4 Human Diseases of Proteolysis 13
    1.5 Matrix Proteases and Their Inhibitors 14
    Acknowledgments 17
    References 17
    2 The Plasminogen Activation System in Normal Tissue Remodeling 25
    Vincent Ellis
    2.1 Introduction 25
    2.2 Biochemical and Enzymological Fundamentals 26
    2.2.1 Plasminogen 27
    2.2.2 Regulation of the Plasminogen Activation System 28
    2.3 Biological Roles of the Plasminogen Activation System 30
    2.3.1 Congenital Plasminogen Deficiencies 31
    2.3.2 Intravascular Fibrinolysis 32
    2.3.3 Extravascular Fibrinolysis -- Ligneous Conjunctivitis 32
    2.3.4 Congenital Inhibitor Deficiencies 33
    2.4 Tissue Remodeling Processes 34
    2.4.1 Wound Healing 34
    2.4.2 Vascular Remodeling 35
    2.4.3 Fibrosis 36
    2.4.4 Nerve Injury 38
    2.4.5 Rheumatoid Arthritis 38
    2.4.6 Complex Tissue Remodeling 40
    2.4.7 Angiogenesis 40
    2.4.8 uPAR -- Cinderella Finds Her Shoe 42
    2.5 Conclusions 44
    References 45
    3 Physiological Functions of Membrane-Type Metalloproteases 57
    Kenn Holmbeck
    3.1 Introduction 57
    3.2 Historical Perspective 57
    3.3 Activation of the Activator 59
    3.4 Potential Roles of MT-MMPs and Discovery of a Human MMP Mutation 59
    3.5 MT-MMP Function? 60
    3.6 Physiological Roles of MT1-MMP in the Mouse 61
    3.7 MT1-MMP Function in Lung Development 63
    3.8 MT1-MMP Is Required for Root Formation and Molar Eruption 64
    3.9 Identification of Cooperative Pathways for Collagen Metabolism 64
    3.10 MT-MMP Activity in the Hematopoietic Environment 65
    3.11 Physiological Role of MT2-MMP 66
    3.12 MT-Type MMPs Work in Concert to Execute Matrix Remodeling 67
    3.13 MT4-MMP -- an MT-MMP with Elusive Function 69
    3.14 MT5-MMP Modulates Neuronal Growth and Nociception 69
    3.15 Summary and Concluding Remarks 70
    Acknowledgment 71
    References 71
    4 Bone Remodeling: Cathepsin K in Collagen Turnover 79
    Dieter Br¨omme
    4.1 Introduction 79
    4.2 Proteolytic Machinery of Bone Resorption and Cathepsin K 80
    4.3 Specificity and Mechanism of Collagenase Activity of Cathepsin K 82
    4.4 Role of Glycosaminoglycans in Bone Diseases 86
    4.5 Development of Specific Cathepsin K Inhibitors and Clinical Trials 87
    4.6 Off-Target and Off-Site Inhibition 89
    4.7 Conclusion 91
    Acknowledgments 91
    References 91
    5 Type-II Transmembrane Serine Proteases: Physiological Functions and Pathological Aspects 99
    Gregory S. Miller, Gina L. Zoratti, and Karin List
    5.1 Introduction 99
    5.2 Functional/Structural Properties of TTSPs 99
    5.3 Physiology and Pathobiology 104
    5.3.1 Hepsin/TMPRSS Subfamily 104
    5.3.2 Corin Subfamily 105
    5.3.3 Matriptase Subfamily 106
    5.3.4 HAT/DESC1 Subfamily 110
    5.3.5 TTSPs in Cancer 111
    References 114
    6 Plasminogen Activators in Ischemic Stroke 127
    Gerald Schielke and Daniel A. Lawrence
    6.1 Introduction 127
    6.2 Rationale for Thrombolysis after Stroke 128
    6.2.1 Clinical Trials: Overview 129
    6.3 Preclinical Studies 131
    6.3.1 Localization of PAs, Neuroserpin, and Plasminogen in the Brain 131
    6.4 The Association of Endogenous tPA with Excitotoxic and Ischemic Brain Injury 134
    6.4.1 Excitotoxicity 134
    6.4.2 Focal Ischemia 135
    6.4.3 Global Ischemia 137
    6.5 Mechanistic Studies of tPA in Excitotoxic and Ischemic Brain Injury 137
    6.5.1 tPA and the NMDA Receptor 137
    6.5.2 tPA and the Blood--Brain Barrier 138
    6.5.3 tPA and the Blood--Brain Barrier -- MMPs 139
    6.5.4 tPA and the Blood--Brain Barrier -- LRP 140
    6.6 tPA and the Blood--Brain Barrier--PDGF-CC 141
    6.7 Summary 143
    Acknowledgments 144
    References 145
    7 Bacterial Abuse of Mammalian Extracellular Proteases during Tissue Invasion and Infection 157
    Claudia Weber, Heiko Herwald, and Sven Hammerschmidt
    7.1 Introduction 157
    7.2 Tissue and Cell Surface Remodeling Proteases 158
    7.2.1 Matrix Metalloproteinases (MMPs) 158
    7.2.2 A Disintegrin and Metalloproteinases (ADAMs) 160
    7.2.3 A Disintegrin and Metalloproteinase with Thrombospondin Motif (ADAMTS) 161
    7.3 Proteases of the Blood Coagulation and the Fibrinolytic System 162
    7.3.1 Proteases of the Blood Coagulation System 162
    7.3.2 Proteases of the Fibrinolytic System 164
    7.4 Contact System 168
    7.4.1 Mechanisms of Bacteria-Induced Contact Activation 169
    7.5 Conclusion and Future Prospectives 170
    Acknowledgments 172
    References 172
    8 Experimental Approaches for Understanding the Role of Matrix Metalloproteinases in Cancer Invasion 181
    Elena Deryugina
    8.1 Introduction: Functional Roles of MMPs in Physiological Processes Involving the Induction and Sustaining of Cancer Invasion 181
    8.2 EMT: a Prerequisite of MMP-Mediated Cancer Invasion or a Coordinated Response to Growth-Factor-Induced MMPs? 182
    8.2.1 MMP-Induced EMT 183
    8.2.2 EMT-Induced MMPs 185
    8.3 Escape from the Primary Tumor: MMP-Mediated Invasion of Basement Membranes 186
    8.3.1 In vitro Models of BM Invasion: Matrigel Invasion in Transwells 186
    8.3.2 Ex Vivo Models of BM Invasion: Transmigration through the Intact BM 188
    8.3.3 In Vivo Models of BM Invasion: Invasion of the CAM in Live Chick Embryos 189
    8.4 Invasive Front Formation: Evidence for MMP Involvement In Vivo 189
    8.4.1 MMP-Dependent Invasion in Spontaneous Tumors Developing in Transgenic Mice 190
    8.4.2 MMP-Dependent Invasion of Tumor Grafts in MMP-Competent Mice 191
    8.4.3 Invasion of MMP-Competent Tumor Grafts in MMP-Deficient Mice 192
    8.5 Invasion at the Leading Edge: MMP-Mediated Proteolysis of Collagenous Stroma 193
    8.5.1 Collagen Invasion in Transwells 193
    8.5.2 Invasion of Collagen Matrices by Overlaid Tumor Cells 194
    8.5.3 Models of 3D Collagen Invasion 195
    8.5.4 Invasion of Collagenous Stroma In Vivo 196
    8.5.5 Dynamic Imaging of ECM Proteolysis during Path-Making In vitro and In Vivo 197
    8.6 Tumor Angiogenesis and Cancer Invasion: MMP-Mediated Interrelationships 197
    8.6.1 Angiogenic Switch: MMP-9-Induced Neovascularization as a Prerequisite for Blood-Vessel-Dependent Cancer Invasion 198
    8.6.2 Mutual Reliance of MMP-Mediated Angiogenesis and Cancer Invasion 200
    8.6.3 Apparent Distinction between MMP-Mediated Tumor Angiogenesis and Cancer Invasion 201
    8.7 Cancer Cell Intravasation: MMP-Dependent Vascular Invasion 202
    8.8 Cancer Cell Extravasation: MMP-Dependent Invasion of the Endothelial Barrier and Subendothelial Stroma 204
    8.8.1 Transmigration across Endothelial Monolayers In Vitro 204
    8.8.2 Tumor Cell Extravasation In Vivo 205
    8.9 Metastatic Site: Involvement of MMPs in the Preparation, Colonization, and Invasion of Distal Organ Stroma 206
    8.9.1 MMPs as Determinants of Organ-Specific Metastases 207
    8.9.2 MMP-Dependent Preparation of the PreMetastatic Microenvironment 208
    8.9.3 Invasive Expansion of Cancer Cells at the Metastatic Site 210
    8.10 Perspectives: MMPs in the Early Metastatic Dissemination and Awakening of Dormant Metastases 211
    References 212
    9 Plasminogen Activators and Their Inhibitors in Cancer 227
    Joerg Hendrik Leupold and Heike Allgayer
    9.1 Introduction 227
    9.2 The Plasminogen Activator System 228
    9.2.1 Molecular Characteristics and Physiological Functions of the u-PA System 228
    9.2.2 Expression in Cancer 230
    9.2.3 Regulation of Expression of the u-PA System in Cancer 231
    9.2.4 Regulation of Cell Signaling by the u-PA System 235
    9.2.5 Conclusion 238
    References 238
    10 Protease Nexin-1 -- a Serpin with a Possible Proinvasive Role in Cancer 251
    Tina M. Kousted, Jan K. Jensen, Shan Gao, and Peter A. Andreasen
    10.1 Introduction -- Serpins and Cancer 251
    10.2 History of PN-1 252
    10.3 General Biochemistry of PN-1 253
    10.4 Inhibitory Properties of PN-1 254
    10.5 Binding of PN-1 and PN-1-Protease Complexes to Endocytosis Receptors of the Low-Density Lipoprotein Receptor Family 257
    10.6 Pericellular Functions of PN-1 in Cell Cultures 260
    10.7 PN-1 Expression Patterns 261
    10.7.1 Expression of PN-1 in Cultured Cells 261
    10.7.2 Mechanisms of Transcriptional Regulation of PN-1 Expression 262
    10.7.3 Expression of PN-1 in the Intact Organism 263
    10.8 Functions of PN-1 in Normal Physiology 263
    10.8.1 Reproductive Organs 263
    10.8.2 Neurobiological Functions 264
    10.8.3 Vascular Functions 265
    10.9 Functions of PN-1 in Cancer 266
    10.9.1 PN-1 Expression is Upregulated in Human Cancers, and a High Expression Is a Marker for a Poor Prognosis 266
    10.9.2 Studies with Cell Cultures and Animal Tumor Models Indicate a Proinvasive Role of PN-1 267
    10.10 Conclusions 270
    References 271
    11 Secreted Cysteine Cathepsins --Versatile Players in Extracellular Proteolysis 283
    Fee Werner, Kathrin Sachse, and Thomas Reinheckel
    11.1 Introduction 283
    11.2 Structure and Function of Cysteine Cathepsins 283
    11.3 Synthesis, Processing, and Sorting of Cysteine Cathepsins 284
    11.4 Extracellular Enzymatic Activity of Lysosomal Cathepsins 286
    11.5 Endogenous Cathepsin Inhibitors as Regulators of Extracellular Cathepsins 286
    11.6 Extracellular Substrates of Cysteine Cathepsins 287
    11.7 Cysteine Cathepsins in Cancer: Clinical Associations 287
    11.8 Cysteine Cathepsins in Cancer: Evidence from Animal Models 288
    11.9 Molecular Dysregulation of Cathepsins in Cancer Progression 289
    11.10 Extracellular Cathepsins in Cancer 289
    11.11 Conclusions and Further Directions 290
    Acknowledgments 291
    References 291
    12 ADAMs in Cancer 299
    Dorte Stautz, Sarah Louise Dombernowsky, and Marie Kveiborg
    12.1 ADAMs--Multifunctional Proteins 299
    12.1.1 Structure and Biochemistry 299
    12.1.2 Biological Functions 300
    12.1.3 Pathological Functions 301
    12.2 ADAMs in Tumors and Cancer Progression 301
    12.2.1 Self-Sufficiency in Growth Signals 303
    12.2.2 Evasion of Apoptosis 303
    12.2.3 Sustained Angiogenesis 304
    12.2.4 Tissue Invasion and Metastasis 305
    12.2.5 Cancer-Related Inflammation 306
    12.2.6 Tumor--Stroma Interactions 307
    12.3 ADAMs in Cancer--Key Questions Yet to Be Answered 307