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. 5
... tissue levels of MMP expression are seen in repair or remodeling processes and in disease or inflamed tissue; higher plasma levels of MMPs are noted in these conditions (Zuckeret al., 1999). Some MMPs, including MMP-2, -7, -19, -24, -25 ...
... tissue levels of MMP expression are seen in repair or remodeling processes and in disease or inflamed tissue; higher plasma levels of MMPs are noted in these conditions (Zuckeret al., 1999). Some MMPs, including MMP-2, -7, -19, -24, -25 ...
Стр. 10
... Tissues The expression of MT-MMPs is differentially controlled at the transcriptional level as evident from the tissue distribution of their mRNAs (Puente et al., 1996; Shofuda et al., 1997; Takinoet al., 1995a,b; Will and Hinzmann ...
... Tissues The expression of MT-MMPs is differentially controlled at the transcriptional level as evident from the tissue distribution of their mRNAs (Puente et al., 1996; Shofuda et al., 1997; Takinoet al., 1995a,b; Will and Hinzmann ...
Стр. 24
... tissue factor. Incubation of VEGF-treated endothelial cells in the presence of coagulation factors VIIa, Va, prothrombin, and lipids resulted in the generation of thrombin and subsequent activation of endothelial secreted proMMP-2 ...
... tissue factor. Incubation of VEGF-treated endothelial cells in the presence of coagulation factors VIIa, Va, prothrombin, and lipids resulted in the generation of thrombin and subsequent activation of endothelial secreted proMMP-2 ...
Стр. 37
... tissue transglutaminase, from proteolysis by MT1-MMP, thereby supporting cell adhesion and locomotion. Transmigration of T lymphocytes into perivascular tissues involves cell movement across endothelial cell layers; α4β1 integrin ...
... tissue transglutaminase, from proteolysis by MT1-MMP, thereby supporting cell adhesion and locomotion. Transmigration of T lymphocytes into perivascular tissues involves cell movement across endothelial cell layers; α4β1 integrin ...
Стр. 39
... tissue organization of early human placenta acting alone and as a cell surface activator of proMMP-2 (Hurskainen et al., 1998; Tanaka et al., 1998). The most abundant MT1-MMP mRNA signal was in the invasive trophoblastic cells, less in ...
... tissue organization of early human placenta acting alone and as a cell surface activator of proMMP-2 (Hurskainen et al., 1998; Tanaka et al., 1998). The most abundant MT1-MMP mRNA signal was in the invasive trophoblastic cells, less in ...
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
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.