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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... mice have provided a fertile experimental model to delineate the function of various proteases. Multiple interactions between cell surface proteases have complicated interpretation of the biological role of individual enzymes. A given ...
... mice have provided a fertile experimental model to delineate the function of various proteases. Multiple interactions between cell surface proteases have complicated interpretation of the biological role of individual enzymes. A given ...
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... 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 dramatically suppressed ...
... 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 dramatically suppressed ...
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... mice and humans (Balbın et al., 2001). MT-MMPs have been also identified in many other mammalian species, as well as in birds and in fish (Kimura et al., 2001; Yang et al., 1996). However, in addition to these studies on vertebrate MMPs ...
... mice and humans (Balbın et al., 2001). MT-MMPs have been also identified in many other mammalian species, as well as in birds and in fish (Kimura et al., 2001; Yang et al., 1996). However, in addition to these studies on vertebrate MMPs ...
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... mice revealed that MT1-MMP null fibroblasts exhibit a late compensatory fibrin-invasive activity. The MT1MMP-independent proinvasive process was identified as due to MT2-MMP and MT3-MMP. However, MT4-MMP transfected cells lacked fibrin ...
... mice revealed that MT1-MMP null fibroblasts exhibit a late compensatory fibrin-invasive activity. The MT1MMP-independent proinvasive process was identified as due to MT2-MMP and MT3-MMP. However, MT4-MMP transfected cells lacked fibrin ...
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... mice by gene targeting in embryonic stem cells (Holmbeck et al., 1999; Zhou et al., 2000). Knockout mice exhibited severe defects in skeletal development and angiogenesis. Postnatal development of secondary ossification centers was ...
... mice by gene targeting in embryonic stem cells (Holmbeck et al., 1999; Zhou et al., 2000). Knockout mice exhibited severe defects in skeletal development and angiogenesis. Postnatal development of secondary ossification centers was ...
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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