Matrix Metalloproteinase Protocols

ISBN-13: 9781493956227 / Angielski / Miękka / 2016 / 492 str.

Ian M. Clark; David A. Young; Andrew D. Rowan

Opis

Matrix Metalloproteinase research has led to the discovery of over twenty distinct vertebrate MMPs and a variety of homologues from diverse organisms. Updated and expanded from the first edition, this text includes state-of-the-art techniques for MMP research.

Recenzje

Review of the first edition: "The editor, Ian M. Clark, has done an excellent job in putting together a collection of articles that span what is now a fairly wide field. ...the content and writing are of a high standard...In chapter 3, covering structural studies and contributed by Wolfram Bode and Klaus Maskos, the authors point out the absence of specific discussions of three-dimensional structures amongst the plethora of general reviews on MMPs and TIMPs. Their contribution expertly fills that void....Indeed the 'Notes' section, at the end of each chapter, is where the benefit of much, often hard-earned, experience is to be reaped and is a valuable addition in almost every case. The last two sections, between them, cover detection of MMp and TIMP expression at both RNA and protein levels, and actively assays. Hore, particular mention must be made of the chapter dealing with zymography and reverse zymography in which Susan Hawkes and coauthors have carefully explained this technique. Their use of figures with detailed interpretation is really excellent and alone could justify the purchase of this book for many labs....this book is recommended as a reference text for all labs engaged in MMP research. There is enough variety for established research labs to find some new methods, and, for newcomers to the field, it should make working with MMPs and their inhibitors a very straightforward prospect." - TRENDS in Cell Biology

Spis treści

Part I: MMPs and TIMPs: An Overview 1. Metalloproteases and the Degradome Alejandro P. Ugalde, Gonzalo R. Ordóñez, Pedro M. Quirós, Xose S. Puente, and Carlos López-Otín 2. Mouse Models of MMP and TIMP Function Sean Y. Kassim, Sean E. Gill, Timothy P. Birkland, and William C. Parks Part II: Expression and Purification of MMPs and TIMPs 3. Expression of Recombinant MMP-28 in Mammalian Cells Ursula R. Rodgers and Ian M. Clark 4. Expression of Recombinant Matrix Metalloproteinases in Escherichia coli L. Jack Windsor and Darin L. Steele 5. Expression of Recombinant ADAMTS in Insect Cells Gavin C. Jones, Mireille N. Vankemmelbeke, and David J. Buttle 6. Expression and Purification of Membrane-Type MMPs Jing Nie and Duanqing Pei 7. Refolding of TIMP-2 from Escherichia coli Inclusion Bodies Richard A. Williamson 8. Purification of MMPs and TIMPs Ken-ichi Shimokawa and Hideaki Nagase Part III: Detection of MMPs and TIMPs 9. Real-Time PCR Expression Profiling of MMPs and TIMPs Caroline J. Pennington and Dylan R. Edwards 10. Analysis of the Degradome with the CLIP-CHIPÔ Microarray Reinhild Kappelhoff, Ulrich auf dem Keller, and Christopher M. Overall 11. In Situ Hybridization for Metalloproteinases and Their Inhibitors Tiina L. Hurskainen and Suneel S. Apte 12. Immunohistochemistry of MMPs and TIMPs Yasunori Okada 13. Single Nucleotide Polymorphism Genotyping in MMP Genes: The 5’ Nuclease Assay Ross Laxton and Shu Ye Part IV: Assay of MMP and TIMP Activities 14. Methods for Studying Activation of Matrix Metalloproteinases Vera Knäuper andGillian Murphy 15. Assay of Matrix Metalloproteinases Against Matrix Substrates Tim E. Cawston, Rachel L. Lakey, and Andrew D. Rowan 16. Zymography and Reverse Zymography for Detecting MMPs and TIMPs Susan P. Hawkes, Hongxia Li, Gary T. Taniguchi, and Marc Lafleur 17. In situ Zymography Sarah J. George and Jason L. Johnson 18. Near Infrared Optical Proteolytic Beacons for In Vivo Imaging of Matrix Metalloproteinase Activity J. Oliver McIntyre, Randy L. Scherer, and Lynn M. Matrisian 19. Neoepitope Antibodies Against MMP-Cleaved and Aggrecanase-Cleaved Aggrecan Amanda J. Fosang, Karena Last, Heather Stanton, Suzanne B. Golub, Christopher B. Little, Lorena Brown, and David C. Jackson 20. In Vitro Model of Cartilage Degradation Wang Hui and Tim Cawston 21. Immunoassays for Collagenase-Mediated Cleavage of Types I and II Collagens R. Clark Billinghurst, Mirela Lonescu, and A. Robin Poole 22. Collagen Degradation Assays Anthony P. Hollander 23. Analysis of MMP-Dependent Cell Migration and Invasion Ralf Palmisano and Yoshifumi Itoh 24. Using Fluorogenic Peptide Substrates to Assay Matrix Metalloproteinases Gregg B. Fields 25. 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 26. 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, Richard A. Dean, Charlotte J. Morrison, and Christopher M. Overall 27. Mechanism-Based Profiling of MMPs Jed F. Fisher and Shahriar Mobashery

Blurb

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.