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E-raamat: Matrix Proteases in Health and Disease [Wiley Online]

Edited by (The Finsen Laboratory, Copenhagen, Denmark)
  • Formaat: 416 pages
  • Ilmumisaeg: 06-Jun-2012
  • Kirjastus: Blackwell Verlag GmbH
  • ISBN-10: 3527649328
  • ISBN-13: 9783527649327
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  • Wiley Online
  • Hind: 206,17 €*
  • * hind, mis tagab piiramatu üheaegsete kasutajate arvuga ligipääsu piiramatuks ajaks
Matrix Proteases in Health and DiseaseSuurem pilt
  • Formaat: 416 pages
  • Ilmumisaeg: 06-Jun-2012
  • Kirjastus: Blackwell Verlag GmbH
  • ISBN-10: 3527649328
  • ISBN-13: 9783527649327
Teised raamatud teemal:
Wiley Online e-raamatudRohkem infot Wiley Online kohta
Raamatu kodulehekülg: https://onlinelibrary.wiley.com/doi/book/10.1002/9783527649327
Presenting a comprehensive overview of the multifaceted field of proteases in the extracellular matrix environment, this reference focuses on the recently elucidated functions of complex proteolytic systems in physiological and pathological tissue remodeling. The proteases treated include both serine proteases such as plasminogen activators and TTSPs, metalloproteases such as MMPs and ADAMS and cysteine protease cathepsins. The text specifically addresses the role of extracellular proteases in cancer cell invasion, stroke and infectious diseases, describing the basic biochemistry behind these disease states, as well as therapeutic strategies based on protease inhibition.

With its trans-disciplinary scope, this reference bridges the gap between fundamental research and biomedical and pharmaceutical application, making this required reading for basic and applied scientists in the molecular life sciences.
Preface xiii
List of Contributors
xv
Introduction 1(4)
Niels Behrendt
1 Matrix Proteases and the Degradome
5(20)
Clara Soria-Valles
Carlos Lopez-Otin
Ana Gutierrez-Fernandez
1.1 Introduction
5(1)
1.2 Bioinformatic Tools for the Analysis of Complex Degradomes
6(2)
1.3 Evolution of Mammalian Degradomes
8(5)
1.3.1 Human Degradome
8(2)
1.3.2 Rodent Degradomes
10(1)
1.3.3 Chimpanzee Degradome
10(1)
1.3.4 Duck-Billed Platypus Degradome
11(1)
1.3.5 Other Degradomes
12(1)
1.4 Human Diseases of Proteolysis
13(1)
1.5 Matrix Proteases and Their Inhibitors
14(11)
Acknowledgments
17(1)
References
17(8)
2 The Plasminogen Activation System in Normal Tissue Remodeling
25(32)
Vincent Ellis
2.1 Introduction
25(1)
2.2 Biochemical and Enzymological Fundamentals
26(4)
2.2.1 Plasminogen
27(1)
2.2.2 Regulation of the Plasminogen Activation System
28(2)
2.3 Biological Roles of the Plasminogen Activation System
30(4)
2.3.1 Congenital Plasminogen Deficiencies
31(1)
2.3.2 Intravascular Fibrinolysis
32(1)
2.3.3 Extravascular Fibrinolysis - Ligneous Conjunctivitis
32(1)
2.3.4 Congenital Inhibitor Deficiencies
33(1)
2.4 Tissue Remodeling Processes
34(10)
2.4.1 Wound Healing
34(1)
2.4.2 Vascular Remodeling
35(1)
2.4.3 Fibrosis
36(2)
2.4.4 Nerve Injury
38(1)
2.4.5 Rheumatoid Arthritis
38(2)
2.4.6 Complex Tissue Remodeling
40(1)
2.4.7 Angiogenesis
40(2)
2.4.8 uPAR - Cinderella Finds Her Shoe
42(2)
2.5 Conclusions
44(13)
References
45(12)
3 Physiological Functions of Membrane-Type Metalloproteases
57(22)
Kenn Holmbeck
3.1 Introduction
57(1)
3.2 Historical Perspective
57(2)
3.3 Activation of the Activator
59(1)
3.4 Potential Roles of MT-MMPs and Discovery of a Human MMP Mutation
59(1)
3.5 MT-MMP Function?
60(1)
3.6 Physiological Roles of MT1-MMP in the Mouse
61(2)
3.7 MT1-MMP Function in Lung Development
63(1)
3.8 MT1-MMP Is Required for Root Formation and Molar Eruption
64(1)
3.9 Identification of Cooperative Pathways for Collagen Metabolism
64(1)
3.10 MT-MMP Activity in the Hematopoietic Environment
65(1)
3.11 Physiological Role of MT2-MMP
66(1)
3.12 MT-Type MMPs Work in Concert to Execute Matrix Remodeling
67(2)
3.13 MT4-MMP - an MT-MMP with Elusive Function
69(1)
3.14 MT5-MMP Modulates Neuronal Growth and Nociception
69(1)
3.15 Summary and Concluding Remarks
70(9)
Acknowledgment
71(1)
References
71(8)
4 Bone Remodeling: Cathepsin K in Collagen Turnover
79(20)
Dieter Bromme
4.1 Introduction
79(1)
4.2 Proteolytic Machinery of Bone Resorption and Cathepsin K
80(2)
4.3 Specificity and Mechanism of Collagenase Activity of Cathepsin K
82(4)
4.4 Role of Glycosaminoglycans in Bone Diseases
86(1)
4.5 Development of Specific Cathepsin K Inhibitors and Clinical Trials
87(2)
4.6 Off-Target and Off-Site Inhibition
89(2)
4.7 Conclusion
91(8)
Acknowledgments
92(5)
References
97(2)
5 Type-II Transmembrane Serine Proteases: Physiological Functions and Pathological Aspects
99(28)
Gregory S. Miller
Gina L. Zoratti
Karin List
5.1 Introduction
99(1)
5.2 Functional/Structural Properties of TTSPs
99(5)
5.3 Physiology and Pathobiology
104(23)
5.3.1 Hepsin/TMPRSS Subfamily
104(1)
5.3.2 Corin Subfamily
105(1)
5.3.3 Matriptase Subfamily
106(4)
5.3.4 HAT/DESC1 Subfamily
110(2)
5.3.5 TTSPs in Cancer
112(2)
References
114(13)
6 Plasminogen Activators in Ischemic Stroke
127(30)
Gerald Schielke
Daniel A. Lawrence
6.1 Introduction
127(1)
6.2 Rationale for Thrombolysis after Stroke
128(3)
6.2.1 Clinical Trials: Overview
129(2)
6.3 Preclinical Studies
131(3)
6.3.1 Localization of PAs, Neuroserpin, and Plasminogen in the Brain
131(3)
6.4 The Association of Endogenous tPA with Excitotoxic and Ischemic Brain Injury
134(3)
6.4.1 Excitotoxicity
134(101)
6.4.2 Focal Ischemia
235
6.4.3 Global Ischemia
137(1)
6.5 Mechanistic Studies of tPA in Excitotoxic and Ischemic Brain Injury
137(105)
6.5.1 tPA and the NMDA Receptor
237
6.5.2 tPA and the Blood-Brain Barrier
138(1)
6.5.3 tPA and the Blood-Brain Barrier - MMPs
139(101)
6.5.4 tPA and the Blood-Brain Barrier - LRP
240(2)
6.6 tPA and the Blood-Brain Barrier-PDGF-CC
242(1)
6.7 Summary
243
Acknowledgments
244(1)
References
245
7 Bacterial Abuse of Mammalian Extracellular Proteases during Tissue Invasion and Infection
157(24)
Claudia Weber
Heiko Herwald
Sven Hammerschmidt
7.1 Introduction
257(1)
7.2 Tissue and Cell Surface Remodeling Proteases
258
7.2.1 Matrix Metalloproteinases (MMPs)
158(2)
7.2.2 A Disintegrin and Metalloproteinases (ADAMs)
160(1)
7.2.3 A Disintegrin and Metalloproteinase with Thrombospondin Motif (ADAMTS)
161(1)
7.3 Proteases of the Blood Coagulation and the Fibrinolytic System
162(6)
7.3.1 Proteases of the Blood Coagulation System
162(2)
7.3.2 Proteases of the Fibrinolytic System
164(4)
7.4 Contact System
168(2)
7.4.1 Mechanisms of Bacteria-Induced Contact Activation
169(1)
7.5 Conclusion and Future Prospectives
170(11)
Acknowledgments
172(1)
References
172(9)
8 Experimental Approaches for Understanding the Role of Matrix Metalloproteinases in Cancer Invasion
181(46)
Elena Deryugina
8.1 Introduction: Functional Roles of MMPs in Physiological Processes Involving the Induction and Sustaining of Cancer Invasion
181(1)
8.2 EMT: a Prerequisite of MMP-Mediated Cancer Invasion or a Coordinated Response to Growth-Factor-Induced MMPs?
182(4)
8.2.1 MMP-Induced EMT
183(2)
8.2.2 EMT-Induced MMPs
185(1)
8.3 Escape from the Primary Tumor: MMP-Mediated Invasion of Basement Membranes
186(3)
8.3.1 In vitro Models of BM Invasion: Matrigel Invasion in Transwells
186(2)
8.3.2 Ex Vivo Models of BM Invasion: Transmigration through the Intact BM
188(1)
8.3.3 In Vivo Models of BM Invasion: Invasion of the CAM in Live Chick Embryos
189(1)
8.4 Invasive Front Formation: Evidence for MMP Involvement In Vivo
189(4)
8.4.1 MMP-Dependent Invasion in Spontaneous Tumors Developing in Transgenic Mice
190(1)
8.4.2 MMP-Dependent Invasion of Tumor Grafts in MMP-Competent Mice
191(1)
8.4.3 Invasion of MMP-Competent Tumor Grafts in MMP-Deficient Mice
192(1)
8.5 Invasion at the Leading Edge: MMP-Mediated Proteolysis of Collagenous Stroma
193(4)
8.5.1 Collagen Invasion in Transwells
193(1)
8.5.2 Invasion of Collagen Matrices by Overlaid Tumor Cells
194(1)
8.5.3 Models of 3D Collagen Invasion
195(1)
8.5.4 Invasion of Collagenous Stroma In Vivo
196(1)
8.5.5 Dynamic Imaging of ECM Proteolysis during Path-Making In vitro and In Vivo
197(1)
8.6 Tumor Angiogenesis and Cancer Invasion: MMP-Mediated Interrelationships
197(5)
8.6.1 Angiogenic Switch: MMP-9-Induced Neovascularization as a Prerequisite for Blood-Vessel-Dependent Cancer Invasion
198(2)
8.6.2 Mutual Reliance of MMP-Mediated Angiogenesis and Cancer Invasion
200(1)
8.6.3 Apparent Distinction between MMP-Mediated Tumor Angiogenesis and Cancer Invasion
201(1)
8.7 Cancer Cell Intravasation: MMP-Dependent Vascular Invasion
202(2)
8.8 Cancer Cell Extravasation: MMP-Dependent Invasion of the Endothelial Barrier and Subendothelial Stroma
204(2)
8.8.1 Transmigration across Endothelial Monolayers In Vitro
204(1)
8.8.2 Tumor Cell Extravasation In Vivo
205(1)
8.9 Metastatic Site: Involvement of MMPs in the Preparation, Colonization, and Invasion of Distal Organ Stroma
206(5)
8.9.1 MMPs as Determinants of Organ-Specific Metastases
207(1)
8.9.2 MMP-Dependent Preparation of the PreMetastatic Microenvironment
208(2)
8.9.3 Invasive Expansion of Cancer Cells at the Metastatic Site
210(1)
8.10 Perspectives: MMPs in the Early Metastatic Dissemination and Awakening of Dormant Metastases
211(16)
References
212(15)
9 Plasminogen Activators and Their Inhibitors in Cancer
227(24)
Joerg Hendrik Leupold
Heike Allgayer
9.1 Introduction
227(1)
9.2 The Plasminogen Activator System
228(23)
9.2.1 Molecular Characteristics and Physiological Functions of the u-PA System
228(2)
9.2.2 Expression in Cancer
230(1)
9.2.3 Regulation of Expression of the u-PA System in Cancer
231(4)
9.2.4 Regulation of Cell Signaling by the u-PA System
235(3)
9.2.5 Conclusion
238(1)
References
238(13)
10 Protease Nexin-1 - a Serpin with a Possible Proinvasive Role in Cancer
251(32)
Tina M. Kousted
Jan K. Jensen
Shan Gao
Peter A. Andreasen
10.1 Introduction - Serpins and Cancer
251(1)
10.2 History of PN-1
252(1)
10.3 General Biochemistry of PN-1
253(1)
10.4 Inhibitory Properties of PN-1
254(3)
10.5 Binding of PN-1 and PN-1-Protease Complexes to Endocytosis Receptors of the Low-Density Lipoprotein Receptor Family
257(3)
10.6 Pericellular Functions of PN-1 in Cell Cultures
260(1)
10.7 PN-1 Expression Patterns
261(2)
10.7.1 Expression of PN-1 in Cultured Cells
261(1)
10.7.2 Mechanisms of Transcriptional Regulation of PN-1 Expression
262(1)
10.7.3 Expression of PN-1 in the Intact Organism
263(1)
10.8 Functions of PN-1 in Normal Physiology
263(3)
10.8.1 Reproductive Organs
263(1)
10.8.2 Neurobiological Functions
264(1)
10.8.3 Vascular Functions
265(1)
10.9 Functions of PN-1 in Cancer
266(4)
10.9.1 PN-1 Expression is Upregulated in Human Cancers, and a High Expression Is a Marker for a Poor Prognosis
266(1)
10.9.2 Studies with Cell Cultures and Animal Tumor Models Indicate a Proinvasive Role of PN-1
267(3)
10.10 Conclusions
270(13)
References
271(12)
11 Secreted Cysteine Cathepsins - Versatile Players in Extracellular Proteolysis
283(16)
Fee Werner
Kathrin Sachse
Thomas Reinheckel
11.1 Introduction
283(1)
11.2 Structure and Function of Cysteine Cathepsins
283(1)
11.3 Synthesis, Processing, and Sorting of Cysteine Cathepsins
284(2)
11.4 Extracellular Enzymatic Activity of Lysosomal Cathepsins
286(1)
11.5 Endogenous Cathepsin Inhibitors as Regulators of Extracellular Cathepsins
286(1)
11.6 Extracellular Substrates of Cysteine Cathepsins
287(1)
11.7 Cysteine Cathepsins in Cancer: Clinical Associations
287(1)
11.8 Cysteine Cathepsins in Cancer: Evidence from Animal Models
288(1)
11.9 Molecular Dysregulation of Cathepsins in Cancer Progression
289(1)
11.10 Extracellular Cathepsins in Cancer
289(1)
11.11 Conclusions and Further Directions
290(9)
Acknowledgments
291(1)
References
291(8)
12 ADAMs in Cancer
299(26)
Dorte Stautz
Sarah Louise Dombernowsky
Marie Kveiborg
12.1 ADAMs-Multifunctional Proteins
299(2)
12.1.1 Structure and Biochemistry
299(1)
12.1.2 Biological Functions
300(1)
12.1.3 Pathological Functions
301(1)
12.2 ADAMs in Tumors and Cancer Progression
301(6)
12.2.1 Self-Sufficiency in Growth Signals
303(1)
12.2.2 Evasion of Apoptosis
303(1)
12.2.3 Sustained Angiogenesis
304(1)
12.2.4 Tissue Invasion and Metastasis
305(1)
12.2.5 Cancer-Related Inflammation
306(1)
12.2.6 Tumor-Stroma Interactions
307(1)
12.3 ADAMs in Cancer-Key Questions Yet to Be Answered
307(2)
12.3.1 ADAM Upregulation
308(1)
12.3.2 Isoforms
308(1)
12.3.3 Proteolytic versus Nonproteolytic Effect
309(1)
12.4 The Clinical Potential of ADAMs
309(2)
12.4.1 Diagnostic or Prognostic Biomarkers
309(1)
12.4.2 ADAMs as Therapeutic Targets
310(1)
12.5 Concluding Remarks
311(14)
References
311(14)
13 Urokinase-Type Plasminogen Activator, Its Receptor and Inhibitor as Biomarkers in Cancer
325(20)
Tine Thurison
Ida K. Lund
Martin Illemann
Ib J. Christensen
Gunilla Høyer-Hansen
13.1 Introduction
325(2)
13.2 Breast Cancer
327(4)
13.3 Colorectal Cancer
331(2)
13.4 Lung Cancer
333(1)
13.5 Gynecological Cancers
334(1)
13.6 Prostate Cancer
335(2)
13.7 Conclusion and Perspectives
337(8)
Acknowledgment
339(1)
Abbreviations
339(1)
References
339(6)
14 Clinical Relevance of MMP and TIMP Measurements in Cancer Tissue
345(28)
Omer Bashir
Jian Cao
Stanley Zucker
14.1 Introduction
345(1)
14.2 MMP Structure
346(1)
14.3 MMP Biology and Pathology
346(1)
14.4 Natural Inhibitors of MMPs
347(1)
14.5 Regulation of MMP Function
347(1)
14.5.1 MMPs in Cancer
347(1)
14.6 Cancer Stromal Cell Production of MMPs
348(1)
14.7 Anticancer Effects of MMPs
348(1)
14.8 Tissue Levels of MMPs and TIMPs in Cancer Patients
349(15)
14.8.1 Breast Cancer
349(2)
14.8.2 Gastrointestinal (GI) Cancer
351(1)
14.8.2.1 Colorectal Cancer
351(2)
14.8.2.2 Gastric Cancer
353(2)
14.8.2.3 Pancreatic Cancer
355(1)
14.8.2.4 Non-Small-Cell Lung Cancer (NSCLC)
355(2)
14.8.3 Genitourinary Cancers
357(1)
14.8.3.1 Bladder Cancer
357(2)
14.8.3.2 Renal Cancer
359(1)
14.8.3.3 Prostate Cancer
359(1)
14.8.3.4 Ovarian Cancer
359(4)
14.8.4 Brain Cancer
363(1)
14.9 Conclusions
364(9)
Acknowledgments
365(1)
References
365(8)
15 New Prospects for Matrix Metalloproteinase Targeting in Cancer Therapy
373(16)
Emilie Buache
Marie-Christine Rio
15.1 Introduction
373(1)
15.2 Lessons Learned from Preclinical and Clinical Studies of MMPIs in Cancer and Possible Alternatives
374(5)
15.2.1 Improve Specificity/Affinity/Selectivity
374(1)
15.2.2 Increase Knowledge of Multifaceted Activities for a given MMP
375(1)
15.2.2.1 Target an Active MMP
375(1)
15.2.2.2 Fully Characterize the Spatio-Temporal Function of Each MMP: the MMP-11 Example
376(1)
15.2.3 Minimize Negative Side Effects
377(1)
15.2.4 Optimize MMPI Administration Schedule
378(1)
15.3 Novel Generation of MMPIs
379(1)
15.3.1 Target the Hemopexin Domain
379(1)
15.3.2 Antibodies as MMPIs
379(1)
15.3.3 Immunotherapy
380(1)
15.4 Exploit MMP Function to Improve Drug Bioavailability
380(1)
15.5 Conclusion
381(8)
Acknowledgments
381(1)
References
381(8)
Index 389
Niels Behrendt is a research group leader at the Finsen Laboratory at the Rigshospitalet (Copenhagen University Hospital), Denmark. He obtained his Ph.D. in 1989 and his D.Sc. degree from Copenhagen University in 2004. The main focus of his work is in protease-dependent tissue remodeling, the interplay of these processes with other cellular functions and their role in cancer invasion.
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