Cell Surface ProteasesElsevier, 3 мая 2003 г. - Всего страниц: 452 Cell Surface Proteases provides a comprehensive overview of these important enzymes that catalyze the hydrolysis of a protein as it degrades to a simpler substance. In the 1990s, an explosion of new discoveries shed light on the role of cell surface proteases and extended it beyond degradation of extracellular matrix components to include its influence on growth factors, cell signaling, and other cellular events. This volume unites the scientific literature from across disciplines and teases out unified themes of interactions between cell surface proteases and interconnecting cell surface-related systems -- including integrins and other adhesion molecules. Scientists and students involved in developmental biology, cell biology and disease processes will find this an indispensable resource. * Provides an overview of the entire field of cell surface proteases in a single volume* Presents major issues and astonishing discoveries at the forefront of modern developmental biology and developmental medicine * A thematic volume in the longest-running forum for contemporary issues in developmental biology with over 30 years of coverage |
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Стр. v
... MMP) Stanley Zucker, Duanqing Pei, Jian Cao, and Carlos Lopez-Otin I. II. III. IV. 2 Introduction 2 Secreted MMPs 3 Membrane Type-Matrix Metalloproteinases (MT-MMPs) 7 Summary and Concluding Remarks 52 References 53 Surface Association ...
... MMP) Stanley Zucker, Duanqing Pei, Jian Cao, and Carlos Lopez-Otin I. II. III. IV. 2 Introduction 2 Secreted MMPs 3 Membrane Type-Matrix Metalloproteinases (MT-MMPs) 7 Summary and Concluding Remarks 52 References 53 Surface Association ...
Стр. xxi
... MMPs as well as several other MMPs have been reported in advanced cancer; the lack of positive results in this setting suggests that these drugs were employed too late in the course of the disease. An alternative explanation is that MMPs ...
... MMPs as well as several other MMPs have been reported in advanced cancer; the lack of positive results in this setting suggests that these drugs were employed too late in the course of the disease. An alternative explanation is that MMPs ...
Стр. 1
... MMPs A. Structural Features of Secreted MMPs B. Regulation of Secreted MMPs C. Naturally Occurring MMP Inhibitors D. Catabolism and Clearance of Secreted MMPs III. Membrane Type-Matrix Metalloproteinases (MT-MMPs) A. Identification of ...
... MMPs A. Structural Features of Secreted MMPs B. Regulation of Secreted MMPs C. Naturally Occurring MMP Inhibitors D. Catabolism and Clearance of Secreted MMPs III. Membrane Type-Matrix Metalloproteinases (MT-MMPs) A. Identification of ...
Стр. 2
... MMPs also generate matrix protein fragments, which have functional activity of their own. These various functions of MMPs modulate cell invasion and metastasis, cell migration, apoptosis, and angiogenesis, to name just a few. A major ...
... MMPs also generate matrix protein fragments, which have functional activity of their own. These various functions of MMPs modulate cell invasion and metastasis, cell migration, apoptosis, and angiogenesis, to name just a few. A major ...
Стр. 3
... MMPs (Apte et al., 1997). Alternative classification systems have been proposed. II. Secreted. MMPs. A. Structural Features of Secreted MMPs All MMPs share several highly conserved domains, most importantly a latency locus [PRCG(V/N)PDV] ...
... MMPs (Apte et al., 1997). Alternative classification systems have been proposed. II. Secreted. MMPs. A. Structural Features of Secreted MMPs All MMPs share several highly conserved domains, most importantly a latency locus [PRCG(V/N)PDV] ...
Содержание
75 | |
Chapter 3 Biochemical Properties and Functions of MembraneAnchored MetalloproteaseDisintegrin Proteins ADAMs | 101 |
Chapter 4 Shedding of Plasma Membrane Proteins | 125 |
Chapter 5 Expression of Meprins in Health and Disease | 145 |
Chapter 6 Type II Transmembrane Serine Proteases | 167 |
Chapter 7 DPPIV Seprase and Related Serine Peptidases in Multiple Cellular Functions | 207 |
Chapter 8 The Secretases of Alzheimers Disease | 233 |
Chapter 9 Plasminogen Activation at the Cell Surface | 263 |
Understanding Its Functional Significance | 313 |
Chapter 11 ProteaseActivated Receptors | 343 |
Chapter 12 Emmprin CD147 a Cell Surface Regulator of Matrix Metalloproteinase Production and Function | 371 |
Implications for Developmental Adaptive Inflammatory and Neoplastic Processes | 391 |
Chapter 14 Shed Membrane Vesicles and Clustering of MembraneBound Proteolytic Enzymes | 411 |
Index | 433 |
Contents of Previous Volumes | 447 |
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Часто встречающиеся слова и выражения
Acad ADAMs adhesion amino acid amyloid angiogenesis astacin binding Biochem breast C-terminal cancer cells Cancer Res carcinoma cells catalytic domain cathepsin cDNA Cell Biol cell lines cell migration cell surface cellular Chem chemokines cleavage cleaved Cloning collagen collagenase complex corin cytoplasmic degradation disease DPPIV emmprin endothelial cells enteropeptidase enzyme expression extracellular matrix fibroblasts fibronectin function gelatinase gene growth factor hepsin human induced inhibition inhibitors integrin interactions invasion involved kinase ligand lysosomes matriptase matrix metalloproteinase mechanism mediated membrane-type meprin metastasis mice MMPs module molecular molecules mouse mRNA MT1-MMP mutations Natl overexpression PAR1 peptidase peptide plasma membrane plasmin plasminogen activation system plasminogen activator platelet potential presenilin processing proMMP-2 protein proteolysis proteolytic receptor regulation residues role secreted Seiki seprase sequence serine protease signaling soluble specific structure substrate subunit TACE thrombin tissue transmembrane tumor tumor cells uPAR urokinase vascular vesicles shed vitro vivo
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Стр. 252 - Borchelt, DR, Thinakaran, G., Eckman, CB, Lee, MK, Davenport, F., Ratovitsky, T., Prada, CM, Kim, G., Seekins, S., Yager, D., Slunt, HH, Wang, R., Seeger, M., Levey, AI, Gandy, SE, Copeland, NG, Jenkins, NA, Price, DL, Younkin, SG, Sisodia, SS (1996) Familial Alzheimer's disease-linked presenilin 1 variants elevate Aft 1-42/1 -40 ratio in vitro and in vivo.
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