Cell Surface Proteases
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
Отзывы - Написать отзыв
Не удалось найти ни одного отзыва.
Chapter 3 Biochemical Properties and Functions of MembraneAnchored MetalloproteaseDisintegrin Proteins ADAMs
Chapter 4 Shedding of Plasma Membrane Proteins
Chapter 5 Expression of Meprins in Health and Disease
Chapter 6 Type II Transmembrane Serine Proteases
Chapter 7 DPPIV Seprase and Related Serine Peptidases in Multiple Cellular Functions
Chapter 8 The Secretases of Alzheimers Disease
Chapter 9 Plasminogen Activation at the Cell Surface
Understanding Its Functional Significance
Chapter 11 ProteaseActivated Receptors
Chapter 12 Emmprin CD147 a Cell Surface Regulator of Matrix Metalloproteinase Production and Function
Implications for Developmental Adaptive Inflammatory and Neoplastic Processes
Chapter 14 Shed Membrane Vesicles and Clustering of MembraneBound Proteolytic Enzymes
Contents of Previous Volumes
Другие издания - Просмотреть все
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
Стр. 68 - Sato. H.. Takino. T.. Okada. Y., Cao. J.. Shinagawa. A.. Yamamoto, E. and Seiki. M. (1994). A matrix metalloproteinase expressed on the surface of invasive tumour cells [see comments].
Стр. 254 - Goate, A., Chartier-Harlin, M.-C, Mullan, M., Brown, J., Crawford, F., Fidani, L, Giuffra. L., Haynes. A., Irving, N., James, L, Mant. R., Newton, P., Rooke, K., Roques. P., Talbot, C., Pericak-Vance, M., Roses, A.. Williamson, R., Rossor, M., Owen, M., and Hardy, J. (1991 ). Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease.
Стр. 254 - JJ, et al. (1992) Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene.
Стр. 139 - RA, 1998, Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol Chem.
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.
Стр. 259 - Younkin SG (1994) An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants.
Стр. 99 - Yu, Q., and Stamenkovic, I. (1999). Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev. 13, 35-48.
Стр. 96 - Holmbeck K, Bianco P, Caterina J, Yamada S, Kromer M, Kuznetsov SA, Mankani M, Robey PG, Poole AR, Pidoux I, Ward JM, Birkedal-Hansen H.
Стр. 144 - Transforming growth factors produced by certain human tumor cells: Polypeptides that interact with epidermal growth factor receptors. Proc.