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

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...

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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:
HerausgeberIn:
Place / Publishing House:Berlin ;, Boston : : De Gruyter, , [2012]
©2012
Year of Publication:2012
Language:English
Online Access:
Physical Description:1 online resource (888 p.)
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spelling Extracellular Matrix: Pathobiology and Signaling / ed. by Nikos Karamanos.
Berlin ; Boston : De Gruyter, [2012]
©2012
1 online resource (888 p.)
text txt rdacontent
computer c rdamedia
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text file PDF rda
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
restricted access http://purl.org/coar/access_right/c_16ec online access with authorization star
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 will give an overview of the current state of knowledge of matrix components (structure and function), their role in heath and disease (matrix pathobiology) and new aspects related to pharmacological targeting.It will provide an introduction to the extracellular matrix and detailed sections and chapters on: Importance of extracellular matrix in health and disease Matrix proteoglycans (aggrecan, versican, perlecan, SLRPs, syndecans, glypicans, serglycin) Matrix proteinases (remodeling, would healing, regulatory roles in health and disease, metalloproteinases, cystein proteases, plasmin and plasminogen activator system) Glycobiology (hyaluronan and sulfated glycosaminoglycans in cancer, inflammation and metabolic control) Collagens (supramolecular assembly, proteins binding collagen, scaffolds, bacterial and mutated collagens, procollagen proteinases) Cell surface receptors (integrins, syndecans, mechanical strain and TGFb, CD44 and DDR). Biotechnological and pharmacological outlook (matrix regulation by growth factors, hyaluronidases, pathobiology, disease targeting, delivery systems, EMT and proteomics). "The book Extracellular Matrix: Pathobiology and Signaling provides a comprehensive and up to date collection of very relevant topics for understanding the various facets of extracellular matrix and its interactions with cells in normal tissue as well as in disease. It represents the current front-line and will serve as a reference for extracellular matrix and posttranslational modifications." Dick Heinegård, Department of Clinical Sciences Lund, Section Rheumatology, Lund University, Sweden
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 migration, adhesion and signaling. This comprehensive handbook of the extracellular matrix is organized into seven thematic sections, giving an overview of the current state of knowledge of matrix components (structure and function), their roles in health and disease (matrix pathobiology) as well as new concepts of pharmacological targeting.
Mode of access: Internet via World Wide Web.
In English.
Description based on online resource; title from PDF title page (publisher's Web site, viewed 30. Aug 2021)
Cellular signal transduction.
Extracellular matrix Pathophysiology.
Extracellular matrix Physiology.
Biochemie.
Glykane.
Kollagene.
Matrix.
Metalloproteinasen.
SCIENCE / Life Sciences / Biochemistry. bisacsh
Biochemistry.
Collagens.
Glycans.
Metalloproteinases.
Afratis, Nikos, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Aletras, Alexios J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bell, Rebecca, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bendeck, Michelle P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Berdiaki, Aikaterini, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Boudko, Sergei P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bouga, Helen, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Brakebusch, Cord, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Brodsky, Barbara, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Bächinger, Hans Peter, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Capurro, Mariana, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Casu, Benito, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Couchman, John R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Dagälv, Anders, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
De Luca, Giancarlo, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Deligny, Audrey, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Des Parkin, J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Do, Anh-Tri, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Dobra, Katalin, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Dufour, Antoine, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Elkin, Michael, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Fadnes, Bodil, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Filmus, Jorge, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Filou, Serafoula, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Gabison, Eric E, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Gao, Congxiao, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Ghatak, Shibnath, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Gialeli, Chrisostomi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Gorski, Daniel J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Gu, Jianguo, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Gullberg, Donald, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Gullberg, Donald.
Hadler-Olsen, Elin, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Hascall, Vincent C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Hascall, Vincent, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Heinegård, Dick, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Heldin, Paraskevi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Hinz, Boris, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Hjerpe, Anders, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Huet, Eric, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Hulmes, David J. S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Ilan, Neta, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Iozzo, Renato V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Jacenko, Olena, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Jokela, Tiina A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Karamanos, Nikos K., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Karamanos, Nikos, editor. edt http://id.loc.gov/vocabulary/relators/edt
Karousou, Evgenia, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Kjelle, Lena, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Kletsas, Dimitris, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Kolliopoulos, Constantine, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Korpetinou, Angeliki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Koutsioumpa, Marina, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Kovalszky, Ilona, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Kozlowski, Eliene O., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Kähäri, Veli-Matti, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Labropoulou, Vassiliki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Li, Jin-Ping, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Lu, Ning, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Maffei, Joseph S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Magnussen, Synnøve, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Markwald, Roger R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
McCulloch, Christopher A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
McNicols, Colton, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Menashi, Suzanne, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Merline, Rosetta, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Milia-Argeiti, Eleni, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Misra, Suniti, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Mizumoto, Shuji, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Moali, Catherine, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Mourah, Samia, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Nagase, Hideaki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Nastase, Madalina V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Nikitovic, Dragana, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Ohtsubo, Kazuaki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Oikari, Sanna, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Orgel, Joseph P. R. O., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Overall, Christopher M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Papadimitriou, Evangelia, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Paraskevi, Heldin.
Passi, Alberto, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Pataki, Csilla, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Pavao, Mauro S. G., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Persikov, Anton V., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Pikas, Dagmar S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Plaas, Anna, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Pratsinis, Harris, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Pucci-Minafra, Ida, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Puré, Ellen, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Raspanti, Mario, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Rocca, Antonio S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Rydén, Cecilia, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
San Antonio, James D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Sanderson, Ralph D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Sandy, John, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Sasaki, Takako, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Savige, Judy, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Schaefer, Liliana, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Schaefer, Liliana.
Schick, Barbara P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Skandalis, Spyros S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Solberg, Rigmor, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Sugahara, Kazuyuki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Svineng, Gunbjørg, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Sylte, Ingebrigt, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Tammi, Markku I., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Tammi, Raija H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Taniguchi, Naoyuki, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Teixeira, Felipe C.O.B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Tenni, Ruggero, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Tenni, Ruggero.
Theocharis, Achilleas D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Theocharis, Achilleas, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Theocharis, Achilleas.
Thidemann Johansen, Harald, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Toriseva, Mervi, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Triantaphyllidou, Irene-Eva, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Tsegenidis, Theodore, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Tzanakakis, George N., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Uhlin-Hansen, Lars, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Velasco, Jennifer, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Vigetti, Davide, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Viola, Manuela, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Vlodavsky, Israel, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Vynios, Demitrios H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Wang, Vincent, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Whiteford, James R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Wight, Thomas N., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Willis, Chris D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Winberg, Jan-Olof, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Winberg, Jan-Olof.
Xian, Xiaojie, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Zaman, Muhammad H., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Zong, Fang, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb
Title is part of eBook package: De Gruyter DGBA Backlist Complete English Language 2000-2014 PART1 9783110238570
Title is part of eBook package: De Gruyter DGBA Backlist Medicine and Life Sciences 2000-2014 (EN) 9783110238495
Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences 2000 - 2014 9783110637915 ZDB-23-GML
Title is part of eBook package: De Gruyter E-BOOK GESAMTPAKET / COMPLETE PACKAGE 2012 9783110288995 ZDB-23-DGG
Title is part of eBook package: De Gruyter E-BOOK PACKAGE BIOLOGY, CHEMISTRY, GEOSCIENCES 2012 9783110294071 ZDB-23-DBE
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print 9783110258769
https://doi.org/10.1515/9783110258776
https://www.degruyter.com/isbn/9783110258776
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author2 Afratis, Nikos,
Afratis, Nikos,
Aletras, Alexios J.,
Aletras, Alexios J.,
Bell, Rebecca,
Bell, Rebecca,
Bendeck, Michelle P.,
Bendeck, Michelle P.,
Berdiaki, Aikaterini,
Berdiaki, Aikaterini,
Boudko, Sergei P.,
Boudko, Sergei P.,
Bouga, Helen,
Bouga, Helen,
Brakebusch, Cord,
Brakebusch, Cord,
Brodsky, Barbara,
Brodsky, Barbara,
Bächinger, Hans Peter,
Bächinger, Hans Peter,
Capurro, Mariana,
Capurro, Mariana,
Casu, Benito,
Casu, Benito,
Couchman, John R.,
Couchman, John R.,
Dagälv, Anders,
Dagälv, Anders,
De Luca, Giancarlo,
De Luca, Giancarlo,
Deligny, Audrey,
Deligny, Audrey,
Des Parkin, J.,
Des Parkin, J.,
Do, Anh-Tri,
Do, Anh-Tri,
Dobra, Katalin,
Dobra, Katalin,
Dufour, Antoine,
Dufour, Antoine,
Elkin, Michael,
Elkin, Michael,
Fadnes, Bodil,
Fadnes, Bodil,
Filmus, Jorge,
Filmus, Jorge,
Filou, Serafoula,
Filou, Serafoula,
Gabison, Eric E,
Gabison, Eric E,
Gao, Congxiao,
Gao, Congxiao,
Ghatak, Shibnath,
Ghatak, Shibnath,
Gialeli, Chrisostomi,
Gialeli, Chrisostomi,
Gorski, Daniel J.,
Gorski, Daniel J.,
Gu, Jianguo,
Gu, Jianguo,
Gullberg, Donald,
Gullberg, Donald,
Gullberg, Donald.
Hadler-Olsen, Elin,
Hadler-Olsen, Elin,
Hascall, Vincent C.,
Hascall, Vincent C.,
Hascall, Vincent,
Hascall, Vincent,
Heinegård, Dick,
Heinegård, Dick,
Heldin, Paraskevi,
Heldin, Paraskevi,
Hinz, Boris,
Hinz, Boris,
Hjerpe, Anders,
Hjerpe, Anders,
Huet, Eric,
Huet, Eric,
Hulmes, David J. S.,
Hulmes, David J. S.,
Ilan, Neta,
Ilan, Neta,
Iozzo, Renato V.,
Iozzo, Renato V.,
Jacenko, Olena,
Jacenko, Olena,
Jokela, Tiina A.,
Jokela, Tiina A.,
Karamanos, Nikos K.,
Karamanos, Nikos K.,
Karamanos, Nikos,
Karamanos, Nikos,
Karousou, Evgenia,
Karousou, Evgenia,
Kjelle, Lena,
Kjelle, Lena,
Kletsas, Dimitris,
Kletsas, Dimitris,
Kolliopoulos, Constantine,
Kolliopoulos, Constantine,
Korpetinou, Angeliki,
Korpetinou, Angeliki,
Koutsioumpa, Marina,
Koutsioumpa, Marina,
Kovalszky, Ilona,
Kovalszky, Ilona,
Kozlowski, Eliene O.,
Kozlowski, Eliene O.,
Kähäri, Veli-Matti,
Kähäri, Veli-Matti,
Labropoulou, Vassiliki,
Labropoulou, Vassiliki,
Li, Jin-Ping,
Li, Jin-Ping,
Lu, Ning,
Lu, Ning,
Maffei, Joseph S.,
Maffei, Joseph S.,
Magnussen, Synnøve,
Magnussen, Synnøve,
Markwald, Roger R.,
Markwald, Roger R.,
McCulloch, Christopher A.,
McCulloch, Christopher A.,
McNicols, Colton,
McNicols, Colton,
Menashi, Suzanne,
Menashi, Suzanne,
Merline, Rosetta,
Merline, Rosetta,
Milia-Argeiti, Eleni,
Milia-Argeiti, Eleni,
Misra, Suniti,
Misra, Suniti,
Mizumoto, Shuji,
Mizumoto, Shuji,
Moali, Catherine,
Moali, Catherine,
Mourah, Samia,
Mourah, Samia,
Nagase, Hideaki,
Nagase, Hideaki,
Nastase, Madalina V.,
Nastase, Madalina V.,
Nikitovic, Dragana,
Nikitovic, Dragana,
Ohtsubo, Kazuaki,
Ohtsubo, Kazuaki,
Oikari, Sanna,
Oikari, Sanna,
Orgel, Joseph P. R. O.,
Orgel, Joseph P. R. O.,
Overall, Christopher M.,
Overall, Christopher M.,
Papadimitriou, Evangelia,
Papadimitriou, Evangelia,
Paraskevi, Heldin.
Passi, Alberto,
Passi, Alberto,
Pataki, Csilla,
Pataki, Csilla,
Pavao, Mauro S. G.,
Pavao, Mauro S. G.,
Persikov, Anton V.,
Persikov, Anton V.,
Pikas, Dagmar S.,
Pikas, Dagmar S.,
Plaas, Anna,
Plaas, Anna,
Pratsinis, Harris,
Pratsinis, Harris,
Pucci-Minafra, Ida,
Pucci-Minafra, Ida,
Puré, Ellen,
Puré, Ellen,
Raspanti, Mario,
Raspanti, Mario,
Rocca, Antonio S.,
Rocca, Antonio S.,
Rydén, Cecilia,
Rydén, Cecilia,
San Antonio, James D.,
San Antonio, James D.,
Sanderson, Ralph D.,
Sanderson, Ralph D.,
Sandy, John,
Sandy, John,
Sasaki, Takako,
Sasaki, Takako,
Savige, Judy,
Savige, Judy,
Schaefer, Liliana,
Schaefer, Liliana,
Schaefer, Liliana.
Schick, Barbara P.,
Schick, Barbara P.,
Skandalis, Spyros S.,
Skandalis, Spyros S.,
Solberg, Rigmor,
Solberg, Rigmor,
Sugahara, Kazuyuki,
Sugahara, Kazuyuki,
Svineng, Gunbjørg,
Svineng, Gunbjørg,
Sylte, Ingebrigt,
Sylte, Ingebrigt,
Tammi, Markku I.,
Tammi, Markku I.,
Tammi, Raija H.,
Tammi, Raija H.,
Taniguchi, Naoyuki,
Taniguchi, Naoyuki,
Teixeira, Felipe C.O.B.,
Teixeira, Felipe C.O.B.,
Tenni, Ruggero,
Tenni, Ruggero,
Tenni, Ruggero.
Theocharis, Achilleas D.,
Theocharis, Achilleas D.,
Theocharis, Achilleas,
Theocharis, Achilleas,
Theocharis, Achilleas.
Thidemann Johansen, Harald,
Thidemann Johansen, Harald,
Toriseva, Mervi,
Toriseva, Mervi,
Triantaphyllidou, Irene-Eva,
Triantaphyllidou, Irene-Eva,
Tsegenidis, Theodore,
Tsegenidis, Theodore,
Tzanakakis, George N.,
Tzanakakis, George N.,
Uhlin-Hansen, Lars,
Uhlin-Hansen, Lars,
Velasco, Jennifer,
Velasco, Jennifer,
Vigetti, Davide,
Vigetti, Davide,
Viola, Manuela,
Viola, Manuela,
Vlodavsky, Israel,
Vlodavsky, Israel,
Vynios, Demitrios H.,
Vynios, Demitrios H.,
Wang, Vincent,
Wang, Vincent,
Whiteford, James R.,
Whiteford, James R.,
Wight, Thomas N.,
Wight, Thomas N.,
Willis, Chris D.,
Willis, Chris D.,
Winberg, Jan-Olof,
Winberg, Jan-Olof,
Winberg, Jan-Olof.
Xian, Xiaojie,
Xian, Xiaojie,
Zaman, Muhammad H.,
Zaman, Muhammad H.,
Zong, Fang,
Zong, Fang,
author_facet Afratis, Nikos,
Afratis, Nikos,
Aletras, Alexios J.,
Aletras, Alexios J.,
Bell, Rebecca,
Bell, Rebecca,
Bendeck, Michelle P.,
Bendeck, Michelle P.,
Berdiaki, Aikaterini,
Berdiaki, Aikaterini,
Boudko, Sergei P.,
Boudko, Sergei P.,
Bouga, Helen,
Bouga, Helen,
Brakebusch, Cord,
Brakebusch, Cord,
Brodsky, Barbara,
Brodsky, Barbara,
Bächinger, Hans Peter,
Bächinger, Hans Peter,
Capurro, Mariana,
Capurro, Mariana,
Casu, Benito,
Casu, Benito,
Couchman, John R.,
Couchman, John R.,
Dagälv, Anders,
Dagälv, Anders,
De Luca, Giancarlo,
De Luca, Giancarlo,
Deligny, Audrey,
Deligny, Audrey,
Des Parkin, J.,
Des Parkin, J.,
Do, Anh-Tri,
Do, Anh-Tri,
Dobra, Katalin,
Dobra, Katalin,
Dufour, Antoine,
Dufour, Antoine,
Elkin, Michael,
Elkin, Michael,
Fadnes, Bodil,
Fadnes, Bodil,
Filmus, Jorge,
Filmus, Jorge,
Filou, Serafoula,
Filou, Serafoula,
Gabison, Eric E,
Gabison, Eric E,
Gao, Congxiao,
Gao, Congxiao,
Ghatak, Shibnath,
Ghatak, Shibnath,
Gialeli, Chrisostomi,
Gialeli, Chrisostomi,
Gorski, Daniel J.,
Gorski, Daniel J.,
Gu, Jianguo,
Gu, Jianguo,
Gullberg, Donald,
Gullberg, Donald,
Gullberg, Donald.
Hadler-Olsen, Elin,
Hadler-Olsen, Elin,
Hascall, Vincent C.,
Hascall, Vincent C.,
Hascall, Vincent,
Hascall, Vincent,
Heinegård, Dick,
Heinegård, Dick,
Heldin, Paraskevi,
Heldin, Paraskevi,
Hinz, Boris,
Hinz, Boris,
Hjerpe, Anders,
Hjerpe, Anders,
Huet, Eric,
Huet, Eric,
Hulmes, David J. S.,
Hulmes, David J. S.,
Ilan, Neta,
Ilan, Neta,
Iozzo, Renato V.,
Iozzo, Renato V.,
Jacenko, Olena,
Jacenko, Olena,
Jokela, Tiina A.,
Jokela, Tiina A.,
Karamanos, Nikos K.,
Karamanos, Nikos K.,
Karamanos, Nikos,
Karamanos, Nikos,
Karousou, Evgenia,
Karousou, Evgenia,
Kjelle, Lena,
Kjelle, Lena,
Kletsas, Dimitris,
Kletsas, Dimitris,
Kolliopoulos, Constantine,
Kolliopoulos, Constantine,
Korpetinou, Angeliki,
Korpetinou, Angeliki,
Koutsioumpa, Marina,
Koutsioumpa, Marina,
Kovalszky, Ilona,
Kovalszky, Ilona,
Kozlowski, Eliene O.,
Kozlowski, Eliene O.,
Kähäri, Veli-Matti,
Kähäri, Veli-Matti,
Labropoulou, Vassiliki,
Labropoulou, Vassiliki,
Li, Jin-Ping,
Li, Jin-Ping,
Lu, Ning,
Lu, Ning,
Maffei, Joseph S.,
Maffei, Joseph S.,
Magnussen, Synnøve,
Magnussen, Synnøve,
Markwald, Roger R.,
Markwald, Roger R.,
McCulloch, Christopher A.,
McCulloch, Christopher A.,
McNicols, Colton,
McNicols, Colton,
Menashi, Suzanne,
Menashi, Suzanne,
Merline, Rosetta,
Merline, Rosetta,
Milia-Argeiti, Eleni,
Milia-Argeiti, Eleni,
Misra, Suniti,
Misra, Suniti,
Mizumoto, Shuji,
Mizumoto, Shuji,
Moali, Catherine,
Moali, Catherine,
Mourah, Samia,
Mourah, Samia,
Nagase, Hideaki,
Nagase, Hideaki,
Nastase, Madalina V.,
Nastase, Madalina V.,
Nikitovic, Dragana,
Nikitovic, Dragana,
Ohtsubo, Kazuaki,
Ohtsubo, Kazuaki,
Oikari, Sanna,
Oikari, Sanna,
Orgel, Joseph P. R. O.,
Orgel, Joseph P. R. O.,
Overall, Christopher M.,
Overall, Christopher M.,
Papadimitriou, Evangelia,
Papadimitriou, Evangelia,
Paraskevi, Heldin.
Passi, Alberto,
Passi, Alberto,
Pataki, Csilla,
Pataki, Csilla,
Pavao, Mauro S. G.,
Pavao, Mauro S. G.,
Persikov, Anton V.,
Persikov, Anton V.,
Pikas, Dagmar S.,
Pikas, Dagmar S.,
Plaas, Anna,
Plaas, Anna,
Pratsinis, Harris,
Pratsinis, Harris,
Pucci-Minafra, Ida,
Pucci-Minafra, Ida,
Puré, Ellen,
Puré, Ellen,
Raspanti, Mario,
Raspanti, Mario,
Rocca, Antonio S.,
Rocca, Antonio S.,
Rydén, Cecilia,
Rydén, Cecilia,
San Antonio, James D.,
San Antonio, James D.,
Sanderson, Ralph D.,
Sanderson, Ralph D.,
Sandy, John,
Sandy, John,
Sasaki, Takako,
Sasaki, Takako,
Savige, Judy,
Savige, Judy,
Schaefer, Liliana,
Schaefer, Liliana,
Schaefer, Liliana.
Schick, Barbara P.,
Schick, Barbara P.,
Skandalis, Spyros S.,
Skandalis, Spyros S.,
Solberg, Rigmor,
Solberg, Rigmor,
Sugahara, Kazuyuki,
Sugahara, Kazuyuki,
Svineng, Gunbjørg,
Svineng, Gunbjørg,
Sylte, Ingebrigt,
Sylte, Ingebrigt,
Tammi, Markku I.,
Tammi, Markku I.,
Tammi, Raija H.,
Tammi, Raija H.,
Taniguchi, Naoyuki,
Taniguchi, Naoyuki,
Teixeira, Felipe C.O.B.,
Teixeira, Felipe C.O.B.,
Tenni, Ruggero,
Tenni, Ruggero,
Tenni, Ruggero.
Theocharis, Achilleas D.,
Theocharis, Achilleas D.,
Theocharis, Achilleas,
Theocharis, Achilleas,
Theocharis, Achilleas.
Thidemann Johansen, Harald,
Thidemann Johansen, Harald,
Toriseva, Mervi,
Toriseva, Mervi,
Triantaphyllidou, Irene-Eva,
Triantaphyllidou, Irene-Eva,
Tsegenidis, Theodore,
Tsegenidis, Theodore,
Tzanakakis, George N.,
Tzanakakis, George N.,
Uhlin-Hansen, Lars,
Uhlin-Hansen, Lars,
Velasco, Jennifer,
Velasco, Jennifer,
Vigetti, Davide,
Vigetti, Davide,
Viola, Manuela,
Viola, Manuela,
Vlodavsky, Israel,
Vlodavsky, Israel,
Vynios, Demitrios H.,
Vynios, Demitrios H.,
Wang, Vincent,
Wang, Vincent,
Whiteford, James R.,
Whiteford, James R.,
Wight, Thomas N.,
Wight, Thomas N.,
Willis, Chris D.,
Willis, Chris D.,
Winberg, Jan-Olof,
Winberg, Jan-Olof,
Winberg, Jan-Olof.
Xian, Xiaojie,
Xian, Xiaojie,
Zaman, Muhammad H.,
Zaman, Muhammad H.,
Zong, Fang,
Zong, Fang,
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author_sort Afratis, Nikos,
title Extracellular Matrix: Pathobiology and Signaling /
spellingShingle Extracellular Matrix: Pathobiology and Signaling /
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
title_full Extracellular Matrix: Pathobiology and Signaling / ed. by Nikos Karamanos.
title_fullStr Extracellular Matrix: Pathobiology and Signaling / ed. by Nikos Karamanos.
title_full_unstemmed Extracellular Matrix: Pathobiology and Signaling / ed. by Nikos Karamanos.
title_auth Extracellular Matrix: Pathobiology and Signaling /
title_alt 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
title_new Extracellular Matrix: Pathobiology and Signaling /
title_sort extracellular matrix: pathobiology and signaling /
publisher De Gruyter,
publishDate 2012
physical 1 online resource (888 p.)
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
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callnumber-first Q - Science
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https://www.degruyter.com/isbn/9783110258776
https://www.degruyter.com/cover/covers/9783110258776.jpg
illustrated Not Illustrated
dewey-hundreds 600 - Technology
dewey-tens 610 - Medicine & health
dewey-ones 610 - Medicine & health
dewey-full 610
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dewey-raw 610
dewey-search 610
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Title is part of eBook package: De Gruyter DGBA Backlist Medicine and Life Sciences 2000-2014 (EN)
Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences 2000 - 2014
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code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">computer</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">online resource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="347" ind1=" " ind2=" "><subfield code="a">text file</subfield><subfield code="b">PDF</subfield><subfield code="2">rda</subfield></datafield><datafield tag="505" ind1="0" ind2="0"><subfield code="t">Frontmatter -- </subfield><subfield code="t">Contents -- </subfield><subfield code="t">Preface -- </subfield><subfield code="t">Comments on the book Extracellular Matrix: Pathobiology &amp; Signaling -- </subfield><subfield code="t">About the Editor/Section Editors -- </subfield><subfield code="t">List of contributing authors -- </subfield><subfield code="t">Abbreviations and acronyms used -- </subfield><subfield code="t">1 An introduction to the extracellular matrix molecules and their importance in pathobiology and signaling -- </subfield><subfield code="t">1.1 Extracellular matrix: a functional scaffold -- </subfield><subfield code="t">2 Insights into the function of glycans -- </subfield><subfield code="t">2.1 Introduction -- </subfield><subfield code="t">2.2 Metabolic control of hyaluronan synthesis -- </subfield><subfield code="t">2.3 Multiple roles of hyaluronan as a target and modifier of the inflammatory response -- </subfield><subfield code="t">2.4 Roles of sulfated and nonsulfated glycosaminoglycans in cancer growth and progression-therapeutic implications -- </subfield><subfield code="t">2.5 Heparan sulfate design: regulation of biosynthesis -- </subfield><subfield code="t">2.6 Bone and skin disorders caused by a disturbance in the biosynthesis of chondroitin sulfate and dermatan sulfate -- </subfield><subfield code="t">2.7 Biological functions of branched N-glycans related to physiology and pathology of extracellular matrix -- </subfield><subfield code="t">3 Proteoglycans: structure, pathobiology, and signaling -- </subfield><subfield code="t">3.1 Introduction -- </subfield><subfield code="t">3.2 Aggrecan in skeletal development and regenerative medicine -- </subfield><subfield code="t">3.3 The pathobiology of versican -- </subfield><subfield code="t">3.4 The biology of perlecan and its bioactive modules -- </subfield><subfield code="t">3.5 Small leucine-rich proteoglycans: multifunctional signaling effectors -- </subfield><subfield code="t">3.6 Structure and function of syndecans -- </subfield><subfield code="t">3.7 The glypican family -- </subfield><subfield code="t">3.8 Serglycin proteoglycan: implications for thrombosis, inflammation, atherosclerosis, and metastasis -- </subfield><subfield code="t">4 Matrix Proteinases: biological significance in health and disease -- </subfield><subfield code="t">4.1 Introduction -- </subfield><subfield code="t">4.2 Extracellular functions of cysteine proteases -- </subfield><subfield code="t">4.3 Plasmin and the plasminogen activator system in health and disease -- </subfield><subfield code="t">4.4 Matrix metalloproteinase complexes and their biological significance -- </subfield><subfield code="t">4.5 The ADAMTS family of metalloproteinases -- </subfield><subfield code="t">4.6 Proteinases in wound healing -- </subfield><subfield code="t">4.7 Rock, paper, and molecular scissors: regulating the game of extracellular matrix homeostasis, remodeling, and inflammation -- </subfield><subfield code="t">5 ECM cell surface receptors -- </subfield><subfield code="t">5.1 Introduction -- </subfield><subfield code="t">5.2 Integrin function in heart fibrosis: mechanical strain, transforming growth factor-beta 1 activation, and collagen glycation -- </subfield><subfield code="t">5.3 Cancer-associated fibroblast integrins as therapeutic targets in the tumor microenvironment -- </subfield><subfield code="t">5.4 Discoidin domain receptors: non-integrin collagen receptors on the move -- </subfield><subfield code="t">5.5 Syndecans as receptors for pericellular molecules -- </subfield><subfield code="t">5.6 CD44: a Sensor of tissue damage critical for restoring homeostasis -- </subfield><subfield code="t">6 Collagens: insights into the folding, assembly and functions -- </subfield><subfield code="t">6.1 Introduction -- </subfield><subfield code="t">6.2 Trimerization domains in collagens: chain selection, folding initiation, and triple-helix stabilization -- </subfield><subfield code="t">6.3 Structural basis of collagen missense mutations -- </subfield><subfield code="t">6.4 Roles and regulation of BMP1/Tolloid-like proteinases: collagen/matrix assembly, growth factor activation, and beyond -- </subfield><subfield code="t">6.5 Supramolecular assembly of type I collagen -- </subfield><subfield code="t">6.6 Collagen interactomes: mapping functional domains and mutations on fibrillar and network-forming collagens -- </subfield><subfield code="t">6.7 Collagen-binding proteins -- </subfield><subfield code="t">7 Emerging aspects in extracellular matrix pathobiology -- </subfield><subfield code="t">7.1 Introduction -- </subfield><subfield code="t">7.2 Extracellular matrix in breast cancer: permissive and restrictive influences emanating from the stroma -- </subfield><subfield code="t">7.3 EMMPRIN/CD147: potential functions in tumor microenvironment and therapeutic target for human cancer -- </subfield><subfield code="t">7.4 Implication of hyaluronidases in cancer growth, metastasis, diagnosis, and treatment -- </subfield><subfield code="t">7.5 Structure-function relationship of syndecan-1, with focus on nuclear translocation and tumor cell behavior -- </subfield><subfield code="t">7.6 Serglycin: a novel player in the terrain of neoplasia -- </subfield><subfield code="t">7.7 Quantifying cell-ECM pathobiology in 3D -- </subfield><subfield code="t">7.8 Diabetic foot infections -- </subfield><subfield code="t">8 Targeting tumor microenvironment at the ECM level -- </subfield><subfield code="t">8.1 Introduction -- </subfield><subfield code="t">8.2 Targeting the tumor microenvironment in cancer progression -- </subfield><subfield code="t">8.3 Growth factor signaling and extracellular matrix -- </subfield><subfield code="t">8.4 Targeting protein-glycan interactions at cell surface during EMT and hematogenous metastasis: consequences on tumor invasion and metastasis -- </subfield><subfield code="t">8.5 Pharmacological targeting of proteoglycans and metalloproteinases: an emerging aspect in cancer treatment -- </subfield><subfield code="t">8.6 Targeting syndecan shedding in cancer -- </subfield><subfield code="t">8.7 PG receptors with phosphatase action in cancer and angiogenesis -- </subfield><subfield code="t">8.8 Heparanase, a multifaceted protein involved in cancer, chronic inflammation, and kidney dysfunction -- </subfield><subfield code="t">8.9 Delivery systems targeting cancer at the level of ECM -- </subfield><subfield code="t">Index</subfield></datafield><datafield tag="506" ind1="0" ind2=" "><subfield code="a">restricted access</subfield><subfield code="u">http://purl.org/coar/access_right/c_16ec</subfield><subfield code="f">online access with authorization</subfield><subfield code="2">star</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">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 will give an overview of the current state of knowledge of matrix components (structure and function), their role in heath and disease (matrix pathobiology) and new aspects related to pharmacological targeting.It will provide an introduction to the extracellular matrix and detailed sections and chapters on: Importance of extracellular matrix in health and disease Matrix proteoglycans (aggrecan, versican, perlecan, SLRPs, syndecans, glypicans, serglycin) Matrix proteinases (remodeling, would healing, regulatory roles in health and disease, metalloproteinases, cystein proteases, plasmin and plasminogen activator system) Glycobiology (hyaluronan and sulfated glycosaminoglycans in cancer, inflammation and metabolic control) Collagens (supramolecular assembly, proteins binding collagen, scaffolds, bacterial and mutated collagens, procollagen proteinases) Cell surface receptors (integrins, syndecans, mechanical strain and TGFb, CD44 and DDR). Biotechnological and pharmacological outlook (matrix regulation by growth factors, hyaluronidases, pathobiology, disease targeting, delivery systems, EMT and proteomics). "The book Extracellular Matrix: Pathobiology and Signaling provides a comprehensive and up to date collection of very relevant topics for understanding the various facets of extracellular matrix and its interactions with cells in normal tissue as well as in disease. It represents the current front-line and will serve as a reference for extracellular matrix and posttranslational modifications." Dick Heinegård, Department of Clinical Sciences Lund, Section Rheumatology, Lund University, Sweden</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">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 migration, adhesion and signaling. This comprehensive handbook of the extracellular matrix is organized into seven thematic sections, giving an overview of the current state of knowledge of matrix components (structure and function), their roles in health and disease (matrix pathobiology) as well as new concepts of pharmacological targeting.</subfield></datafield><datafield tag="538" ind1=" " ind2=" "><subfield code="a">Mode of access: Internet via World Wide Web.</subfield></datafield><datafield tag="546" ind1=" " ind2=" "><subfield code="a">In English.</subfield></datafield><datafield tag="588" ind1="0" ind2=" "><subfield code="a">Description based on online resource; title from PDF title page (publisher's Web site, viewed 30. Aug 2021)</subfield></datafield><datafield tag="650" ind1=" " ind2="0"><subfield code="a">Cellular signal transduction.</subfield></datafield><datafield tag="650" ind1=" " ind2="0"><subfield code="a">Extracellular matrix</subfield><subfield code="x">Pathophysiology.</subfield></datafield><datafield tag="650" ind1=" " ind2="0"><subfield code="a">Extracellular matrix</subfield><subfield code="x">Physiology.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Biochemie.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Glykane.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Kollagene.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Matrix.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Metalloproteinasen.</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">SCIENCE / Life Sciences / 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