Matrix metalloproteinase protocols /

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Bibliographic Details
Edition:2nd ed.
Imprint:New York, N.Y. : Humana Press, ©2010.
Description:1 online resource (xii, 492 pages) : illustrations (some color)
Language:English
Series:Methods in molecular biology, 1064-3745 ; v. 622
Springer protocols
Methods in molecular biology (Clifton, N.J.) ; volume 622.
Springer protocols (Series)
Subject:
Format: E-Resource Book
URL for this record:http://pi.lib.uchicago.edu/1001/cat/bib/11228170
Hidden Bibliographic Details
Other authors / contributors:Clark, Ian M.
Young, David A., 1970-
Rowan, Andrew D.
ISBN:9781603272995
1603272992
9781603272988
1603272984
9781607614357
1607614359
9781493956227
1493956221
Notes:Previous edition: 2001.
Includes bibliographical references and index.
English.
Print version record.
Summary:Since the discovery of a collagen-degrading protease in the tadpole tail in 1962, matrix metalloproteinase research has led to the discovery of more than twenty distinct vertebrate MMPs, along with a variety of homologues from diverse organisms such as the sea urchin, plants, insects, and nematode worms. Fully updating and adding to the popular first edition, Matrix Metalloproteinase Protocols, Second Edition includes a series of state-of-the-art techniques provided by eminent experts in the field. Beginning with a brief overview of the MMP arena, from how these enzymes fit into the larger degradome to what occurs when their expression and function in the mouse is modulated, the volume continues with sections on the expression and purification of MMPs and TIMPs, the detection of MMPs and TIMPs at both the protein and mRNA level, and our ability to assay MMP and TIMP activities in a wide variety of circumstances. Written in the highly successful Methods in Molecular Biology"!series format, chapters contain introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and notes on troubleshooting and avoiding known pitfalls. Comprehensive and cutting-edge, Matrix Metalloproteinase Protocols, Second Edition is an ideal source for many of the essential laboratory techniques for both novice and seasoned researchers alike collected in one convenient volume
Other form:Print version: Matrix metalloproteinase protocols. 2nd ed. New York, N.Y. : Humana Press, ©2010 9781603272988 1603272984
Standard no.:10.1007/978-1-60327-299-5.
Table of Contents:
  • Metalloproteases and the degradome / Alejandro P. Ugalde [and others]
  • Mouse models of MMP and TIMP function / Sean E. Gill [and others]
  • Expression of recombinant MMP-28 in mammalian cells / Ursula R. Rodgers and Ian M. Clark
  • Expression of recombinant matrix metalloproteinases in Escherichia coli / L. Jack Windsor and Darin L. Steele
  • Expression of recombinant ADAMTS in insect cells / Gavin C. Jones, Mireille N. Vankemmelbeke and David J. Buttle
  • Expression and purification of membrane-type MMPs / Jing Nie and Duanqing Pei
  • Refolding of TIMP-2 from Escherichia coli inclusion bodies / Richard A. Williamson
  • Purification of MMPs and TIMPs / Ken-ichi Shimokawa and Hideaki Nagase
  • Real-time PCR expression profiling of MMPs and TIMPs / Caroline J. Pennington and Dylan R. Edwards
  • Analysis of the degradome with the CLIP-CHIP microarray / Reinhild Kappelhoff, Ulrich auf dem Keller, and Christopher M. Overall
  • In situ hybridization for metalloproteinases and their inhibitors / Tiina L. Hurskainen and Suneel S. Apte
  • Immunohistochemistry of MMPs and TIMPs / Yasunori Okada
  • Single nucleotide polymorphism genotyping in MMP genes : the 5' nuclease assay / Ross Laxton and Shu Ye
  • Methods for studying activation of matrix metalloproteinases / Vera Knäuper and Gillian Murphy
  • Assay of matrix metalloproteinases against matrix substrates / Tim E. Cawston, Rachel L. Lakey, and Andrew D. Rowan
  • Zymography and reverse zymography for detecting MMPs and TIMPs / Susan P. Hawkes, Hongxia Li, and Gary T. Taniguchi, with contributions from Marc A. Lafleur
  • In situ zymography / Sarah J. George and Jason L. Johnson
  • Near-infrared optical proteolytic beacons for in vivo imaging of matrix metalloproteinase activity / J. Oliver McIntyre, Randy L. Scherer, and Lynn M. Matrisian
  • Neoepitope antibodies against MMP-cleaved and aggrecanase-cleaved aggrecan / Amanda J. Fosang [and others]
  • In vitro model of cartilage degradation / Wang Hui and Tim E. Cawston
  • Immunoassays for collagenase-mediated cleavage of type I and II collagens / R. Clark Billinghurst, Mirela Ionescu, and A. Robin Poole
  • Collagen degradation assays / Anthony P. Hollander
  • Analysis of MMP-dependent cell migration and invasion / Ralf Palmisano and Yoshifumi Itoh
  • Using fluorogenic peptide substrates to assay matrix metalloproteinases / Gregg B. Fields
  • Kinetic analysis of the inhibition of matrix metalloproteinases : lessons from the study of tissue inhibitors of metalloproteinases / Frances Willenbrock, Daniel A. Thomas, and Augustin Amour
  • Identification of cellular MMP substrates using quantitative proteomics : isotope-coded affinity tags (ICAT) and isobaric tags for relative and absolute quantification (iTRAQ) / Georgina S. Butler [and others]
  • Mechanism-based profiling of MMPs / Jed F. Fisher and Shahriar Mobashery.