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. 4
... ProMMP-2 is an exception to direct serine proteinase activation of MMPs. Plasmin generation at the cell surface is cited as a potential mechanism for the physiological activation of latent MMP-1, MMP-3, and MMP-9. However, data derived ...
... ProMMP-2 is an exception to direct serine proteinase activation of MMPs. Plasmin generation at the cell surface is cited as a potential mechanism for the physiological activation of latent MMP-1, MMP-3, and MMP-9. However, data derived ...
Стр. 6
... 2 form complexes with the C-terminal domains of proMMP-9 and proMMP-2, respectively. These complexes preserve the inhibitory activity of the TIMPs while dampening the activity of the bound MMP (Nagase and Woessner, 1999). α2 ...
... 2 form complexes with the C-terminal domains of proMMP-9 and proMMP-2, respectively. These complexes preserve the inhibitory activity of the TIMPs while dampening the activity of the bound MMP (Nagase and Woessner, 1999). α2 ...
Стр. 8
... proMMP-2, proMMP-13, types I, II, III collagen, gelatin, fibronectin, laminin, fibrin, proteoglycans, proTNFα Ubiquitous MT2-MMP MMP-15 Z48482 670 16q12.2-21 proMMP-2, fibronectin, tenascin, laminin, aggrecan, perlecan Ubiquitous MT3 ...
... proMMP-2, proMMP-13, types I, II, III collagen, gelatin, fibronectin, laminin, fibrin, proteoglycans, proTNFα Ubiquitous MT2-MMP MMP-15 Z48482 670 16q12.2-21 proMMP-2, fibronectin, tenascin, laminin, aggrecan, perlecan Ubiquitous MT3 ...
Стр. 11
... proMMP-2, binding of TIMP-2 to the cell surface, cell migration, and substrate degradation. Therefore, this four-residue amino acid sequence characteristic of MT-MMP propeptides contains important information for both the folding of ...
... proMMP-2, binding of TIMP-2 to the cell surface, cell migration, and substrate degradation. Therefore, this four-residue amino acid sequence characteristic of MT-MMP propeptides contains important information for both the folding of ...
Стр. 13
... 2, indicating that the net effect on affinity of the MT1-MMP:TIMP-2 complex is not influenced by this 8-residue loop (English et al., 2001a). By contrast, analysis of the kinetics of activation of proMMP-2 by the MT-loop mutants showed ...
... 2, indicating that the net effect on affinity of the MT1-MMP:TIMP-2 complex is not influenced by this 8-residue loop (English et al., 2001a). By contrast, analysis of the kinetics of activation of proMMP-2 by the MT-loop mutants showed ...
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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