Matrix metalloproteinase protocols / edited by Ian M. Clark.
Contributor(s): Clark, Ian M [editor].Material type: BookSeries: Methods in molecular biology v. 151.Copyright date: Totowa, N.J. : Humana Press, 2001Edition: First Edition.Description: xv, 545 pages : illustrations (some colours) ; 24 cm.ISBN: 0896037339 (alk. paper); 9780896037335.Subject(s): Metalloproteinases -- Laboratory manuals | Metaloproteinasas -- Manuales de laboratorio | Extracellular matrix proteins -- Laboratory manuals | Proteínas de matriz extracelularDDC classification: 572.76 Online resources: Publisher description | Table of contents only
|Item type||Current location||Call number||Copy number||Status||Date due||Item holds|
|Libro académico||Biblioteca del Campus||572.76 M4339 2001 (Browse shelf)||Ej. 1||Available|
Includes bibliographical references and index.
Part 1 -- MMPs and TIMPs -- an overview of the field -- Part II -- Expression and purification of MMPs and TIMPs -- Detection of MMPs and TIMPs -- Assay of MMP and TIMP activities. Mmps and timps. An historical perspective / J.F. Woessner, Jr. -- Strategies for cloning new mmps and timps / G. Velasco and C. Lopez-Otin -- Structural studies on mmps and timps / W. Bode and K. Maskos -- Matrix metalloproteinase substrate binding domains, modules and exosites. Overview and experimental strategies / C.M. Overall -- The matrix metalloproteinase (mmp) and tissue inhibitor of metalloproteinase (timp) genes. Transcriptional and posttranscriptional regulation, signal transduction and cell-type-specific expression / M.P. Vincenti -- Models for gain-of-function and loss-of-function of mmps. Transgenic and gene targeted mice / L.M. Coussens [and others] -- Expression of mmps and timps in mammalian cells / K.M. Yeow [and others] -- Expression of recombinant matrix metalloproteinases in escherichia coli / L.J. Windsor and D.L. Steele -- Expression of human collagenase i (mmp-1) and timp-1 in a baculovirus-based expression system / R. Vallon and P. Angel -- Expression of recombinant matrix metalloproteinases in yeast / G.A. Doyle -- Expression of recombinant membrane-type mmps / M.J. Butler, M.P. d'Ortho and S.J. Atkinson -- Refolding of timp-2 from escherichia coli inclusion bodies / R.A. Williamson -- Expression and refolding of full-length human timp-1 / D. Davis -- Purification of mmps and timps / K. Shimokawa and H. Nagase -- Monitoring mmp and timp mrna expression by rt-pcr / H. Wong [and others] -- Measuring transcription of metalloproteinase genes. Nuclear run-off assay vs analysis of hnrna / A.M. Delany -- In situ hybridization for metalloproteinases and their inhibitors / T.L. Hurskainen and S.S. Apte -- Use of eia to measure mmps and timps / N. Fujimoto and K. Iwata -- Immunohistochemistry of mmps and timps / Y. Okada -- Detecting polymorphisms in mmp genes / S. Ye and A.M. Henney -- Methods for studying activation of matrix metalloproteinases / V. Knauper and G. Murphy -- Assay of matrix metalloproteinases against matrix substrates / T.E. Cawston, P. Koshy and A.D. Rowan -- Zymography and reverse zymography for detecting mmps, and timps / S.P. Hawkes, H. Li and G.T. Taniguchi -- In situ zymography / S.J. George and J.L. Johnson -- Detection of focal proteolysis using texas-red-gelatin / R.M. Hembry -- Antibodies to mmp-cleaved aggrecan / A.J. Fosang [and others] -- Cartilage proteoglycan release assay / C.J. Billington -- Immunoassay for collagenase-mediated cleavage of types i and ii collagens / R.C. Billinghurst, M. Ionescu and A.R. Poole -- Collagen degradation assays / A.P. Hollander -- Invasion assays and matrix metalloproteinases. Quantification of cellular invasion using propidium iodide labeling and confocal laser scanning microscopy / U. Benbow, K.A. Orndorff and A.L. Givan -- Using fluorogenic peptide substrates to assay matrix metalloproteinases / G.B. Fields -- Kinetic analysis of the inhibition of matrix metalloproteinases by tissue inhibitor of metalloproteinases (timp) / M. Hutton and F. Willenbrock -- Assaying growth factor activity of tissue inhibitors of metalloproteinases / K. Yamashita and T. Hayakawa.
From the simple discovery in 1962 that resorbing tadpole tail expressed an enzyme (MMP) that could degrade collagen gels, matrix metalloproteinase (MMP) research has advanced to discover more than twenty distinct vertebrate MMPs and four specific inhibitors (TIMPS), a veritable family of enzymes involved in many physiological and pathological processes. In Matrix Metalloproteinase Protocols, leading experts detail proven laboratory techniques for the study of MMPs.