Extracellular Matrix: Pathobiology and Signaling / / ed. by Nikos Karamanos.

• Superior document: Title is part of eBook package: De Gruyter DGBA Backlist Complete English Language 2000-2014 PART1
• MitwirkendeR: Afratis, Nikos,; Aletras, Alexios J.,; Bell, Rebecca,; Bendeck, Michelle P.,; Berdiaki, Aikaterini,; Boudko, Sergei P.,; Bouga, Helen,; Brakebusch, Cord,; Brodsky, Barbara,; Bächinger, Hans Peter,; Capurro, Mariana,; Casu, Benito,; Couchman, John R.,; Dagälv, Anders,; De Luca, Giancarlo,; Deligny, Audrey,; Des Parkin, J.,; Do, Anh-Tri,; Dobra, Katalin,; Dufour, Antoine,; Elkin, Michael,; Fadnes, Bodil,; Filmus, Jorge,; Filou, Serafoula,; Gabison, Eric E,; Gao, Congxiao,; Ghatak, Shibnath,; Gialeli, Chrisostomi,; Gorski, Daniel J.,; Gu, Jianguo,; Gullberg, Donald,; Hadler-Olsen, Elin,; Hascall, Vincent C.,; Hascall, Vincent,; Heinegård, Dick,; Heldin, Paraskevi,; Hinz, Boris,; Hjerpe, Anders,; Huet, Eric,; Hulmes, David J. S.,; Ilan, Neta,; Iozzo, Renato V.,; Jacenko, Olena,; Jokela, Tiina A.,; Karamanos, Nikos K.,; Karousou, Evgenia,; Kjelle, Lena,; Kletsas, Dimitris,; Kolliopoulos, Constantine,; Korpetinou, Angeliki,; Koutsioumpa, Marina,; Kovalszky, Ilona,; Kozlowski, Eliene O.,; Kähäri, Veli-Matti,; Labropoulou, Vassiliki,; Li, Jin-Ping,; Lu, Ning,; Maffei, Joseph S.,; Magnussen, Synnøve,; Markwald, Roger R.,; McCulloch, Christopher A.,; McNicols, Colton,; Menashi, Suzanne,; Merline, Rosetta,; Milia-Argeiti, Eleni,; Misra, Suniti,; Mizumoto, Shuji,; Moali, Catherine,; Mourah, Samia,; Nagase, Hideaki,; Nastase, Madalina V.,; Nikitovic, Dragana,; Ohtsubo, Kazuaki,; Oikari, Sanna,; Orgel, Joseph P. R. O.,; Overall, Christopher M.,; Papadimitriou, Evangelia,; Passi, Alberto,; Pataki, Csilla,; Pavao, Mauro S. G.,; Persikov, Anton V.,; Pikas, Dagmar S.,; Plaas, Anna,; Pratsinis, Harris,; Pucci-Minafra, Ida,; Puré, Ellen,; Raspanti, Mario,; Rocca, Antonio S.,; Rydén, Cecilia,; San Antonio, James D.,; Sanderson, Ralph D.,; Sandy, John,; Sasaki, Takako,; Savige, Judy,; Schaefer, Liliana,; Schick, Barbara P.,; Skandalis, Spyros S.,; Solberg, Rigmor,; Sugahara, Kazuyuki,; Svineng, Gunbjørg,; Sylte, Ingebrigt,; Tammi, Markku I.,; Tammi, Raija H.,; Taniguchi, Naoyuki,; Teixeira, Felipe C.O.B.,; Tenni, Ruggero,; Theocharis, Achilleas D.,; Theocharis, Achilleas,; Thidemann Johansen, Harald,; Toriseva, Mervi,; Triantaphyllidou, Irene-Eva,; Tsegenidis, Theodore,; Tzanakakis, George N.,; Uhlin-Hansen, Lars,; Velasco, Jennifer,; Vigetti, Davide,; Viola, Manuela,; Vlodavsky, Israel,; Vynios, Demitrios H.,; Wang, Vincent,; Whiteford, James R.,; Wight, Thomas N.,; Willis, Chris D.,; Winberg, Jan-Olof,; Xian, Xiaojie,; Zaman, Muhammad H.,; Zong, Fang,
• TeilnehmendeR: Gullberg, Donald.; Paraskevi, Heldin.; Schaefer, Liliana.; Tenni, Ruggero.; Theocharis, Achilleas.; Winberg, Jan-Olof.
• HerausgeberIn: Karamanos, Nikos,
• Place / Publishing House: Berlin ;, Boston : : De Gruyter, , [2012]; ©2012
• Year of Publication: 2012
• Language: English
• Physical Description: 1 online resource (888 p.)

Over the last decades cell biology and biological chemistry have increasingly turned their attention to the space between cells and revealed an elaborate network of macromolecules essential for structural support, cell adhesion and signaling. This comprehensive handbook of the extracellular matrix w...

Table of Contents

• Frontmatter
• Contents
• Preface
• Comments on the book Extracellular Matrix: Pathobiology & Signaling
• About the Editor/Section Editors
• List of contributing authors
• Abbreviations and acronyms used
• 1 An introduction to the extracellular matrix molecules and their importance in pathobiology and signaling
• 1.1 Extracellular matrix: a functional scaffold
• 2 Insights into the function of glycans
• 2.1 Introduction
• 2.2 Metabolic control of hyaluronan synthesis
• 2.3 Multiple roles of hyaluronan as a target and modifier of the inflammatory response
• 2.4 Roles of sulfated and nonsulfated glycosaminoglycans in cancer growth and progression-therapeutic implications
• 2.5 Heparan sulfate design: regulation of biosynthesis
• 2.6 Bone and skin disorders caused by a disturbance in the biosynthesis of chondroitin sulfate and dermatan sulfate
• 2.7 Biological functions of branched N-glycans related to physiology and pathology of extracellular matrix
• 3 Proteoglycans: structure, pathobiology, and signaling
• 3.1 Introduction
• 3.2 Aggrecan in skeletal development and regenerative medicine
• 3.3 The pathobiology of versican
• 3.4 The biology of perlecan and its bioactive modules
• 3.5 Small leucine-rich proteoglycans: multifunctional signaling effectors
• 3.6 Structure and function of syndecans
• 3.7 The glypican family
• 3.8 Serglycin proteoglycan: implications for thrombosis, inflammation, atherosclerosis, and metastasis
• 4 Matrix Proteinases: biological significance in health and disease
• 4.1 Introduction
• 4.2 Extracellular functions of cysteine proteases
• 4.3 Plasmin and the plasminogen activator system in health and disease
• 4.4 Matrix metalloproteinase complexes and their biological significance
• 4.5 The ADAMTS family of metalloproteinases
• 4.6 Proteinases in wound healing
• 4.7 Rock, paper, and molecular scissors: regulating the game of extracellular matrix homeostasis, remodeling, and inflammation
• 5 ECM cell surface receptors
• 5.1 Introduction
• 5.2 Integrin function in heart fibrosis: mechanical strain, transforming growth factor-beta 1 activation, and collagen glycation
• 5.3 Cancer-associated fibroblast integrins as therapeutic targets in the tumor microenvironment
• 5.4 Discoidin domain receptors: non-integrin collagen receptors on the move
• 5.5 Syndecans as receptors for pericellular molecules
• 5.6 CD44: a Sensor of tissue damage critical for restoring homeostasis
• 6 Collagens: insights into the folding, assembly and functions
• 6.1 Introduction
• 6.2 Trimerization domains in collagens: chain selection, folding initiation, and triple-helix stabilization
• 6.3 Structural basis of collagen missense mutations
• 6.4 Roles and regulation of BMP1/Tolloid-like proteinases: collagen/matrix assembly, growth factor activation, and beyond
• 6.5 Supramolecular assembly of type I collagen
• 6.6 Collagen interactomes: mapping functional domains and mutations on fibrillar and network-forming collagens
• 6.7 Collagen-binding proteins
• 7 Emerging aspects in extracellular matrix pathobiology
• 7.1 Introduction
• 7.2 Extracellular matrix in breast cancer: permissive and restrictive influences emanating from the stroma
• 7.3 EMMPRIN/CD147: potential functions in tumor microenvironment and therapeutic target for human cancer
• 7.4 Implication of hyaluronidases in cancer growth, metastasis, diagnosis, and treatment
• 7.5 Structure-function relationship of syndecan-1, with focus on nuclear translocation and tumor cell behavior
• 7.6 Serglycin: a novel player in the terrain of neoplasia
• 7.7 Quantifying cell-ECM pathobiology in 3D
• 7.8 Diabetic foot infections
• 8 Targeting tumor microenvironment at the ECM level
• 8.1 Introduction
• 8.2 Targeting the tumor microenvironment in cancer progression
• 8.3 Growth factor signaling and extracellular matrix
• 8.4 Targeting protein-glycan interactions at cell surface during EMT and hematogenous metastasis: consequences on tumor invasion and metastasis
• 8.5 Pharmacological targeting of proteoglycans and metalloproteinases: an emerging aspect in cancer treatment
• 8.6 Targeting syndecan shedding in cancer
• 8.7 PG receptors with phosphatase action in cancer and angiogenesis
• 8.8 Heparanase, a multifaceted protein involved in cancer, chronic inflammation, and kidney dysfunction
• 8.9 Delivery systems targeting cancer at the level of ECM
• Index