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. xvii
... proteolysis. Proteolytic events occur intracellularly, pericellularly, and extracellularly, but for many years the majority of studies have dealt with intracellular and extracellular proteolysis. Although the importance of pericellular ...
... proteolysis. Proteolytic events occur intracellularly, pericellularly, and extracellularly, but for many years the majority of studies have dealt with intracellular and extracellular proteolysis. Although the importance of pericellular ...
Стр. 3
... (proteolytic cleavage, oxidation, mercurial compounds, etc.) resulted in activation of the enzyme. The contact Cys-SH with zinc was later confirmed directly. MMP-23 is the only exception without a cysteine residue in its putative domain ...
... (proteolytic cleavage, oxidation, mercurial compounds, etc.) resulted in activation of the enzyme. The contact Cys-SH with zinc was later confirmed directly. MMP-23 is the only exception without a cysteine residue in its putative domain ...
Стр. 5
... proteolytic attack at focal sites. Heparan sulfate proteoglycans has been demonstrated to be an important docking molecule for MMPs in proximity to epithelial cells and underlying basement membranes (Yu and Woessner, 2000). Proteolytic ...
... proteolytic attack at focal sites. Heparan sulfate proteoglycans has been demonstrated to be an important docking molecule for MMPs in proximity to epithelial cells and underlying basement membranes (Yu and Woessner, 2000). Proteolytic ...
Стр. 6
... proteolytic activity. Mice lacking a functional RECK gene die in utero with defects in collagen fibrils, the basal lamina, and vascular development, thereby suggesting unimpeded MMP degradation of ECM proteins. Vascular sprouting is ...
... proteolytic activity. Mice lacking a functional RECK gene die in utero with defects in collagen fibrils, the basal lamina, and vascular development, thereby suggesting unimpeded MMP degradation of ECM proteins. Vascular sprouting is ...
Стр. 7
... proteolysis of activated MMPs. Whereas some cleavages of activated MMPs lead to inactivation, others, such as those that ... proteolytic enzymes was increasingly recognized to be important in the cell's ability to adapt and modify its ...
... proteolysis of activated MMPs. Whereas some cleavages of activated MMPs lead to inactivation, others, such as those that ... proteolytic enzymes was increasingly recognized to be important in the cell's ability to adapt and modify its ...
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
Популярные отрывки
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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.
Стр. 94 - H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. J. Biol. Chem., 263, 6579-6587.
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