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Extracellular matrix (ECM) research
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Methods 45 (2008) 1 www.elsevier.com/locate/ymeth
Guest Editor’s Introduction
Extracellular matrix (ECM) research
Research experimentalists require robust and wellproven protocols to perform even the simplest of experiments. Each laboratory has its own library of tried-and-tested recipes that are ‘inherited’ by successive generations of postgraduate students and postdoctoral fellows. In addition, an increasing number of commercial ‘kits’ are available for routine procedures such as RNA isolation, protein quantitation, and immunodetection. Specialised companies and organisations will also perform more complex procedures such as yeast two-hybrid molecular fishing and transgenic mouse generation. And of course, there is a wealth of literature from which to select peer-reviewed methods. However, despite this apparent glut of technical information, it is often difficult for newcomers to a research field to find a good protocol or to adapt an existing one. Furthermore, there is the lengthy process of acquiring detailed knowledge of the structure and solution properties of the molecule being studied, and this is especially important when the molecule being studied is an extracellular matrix (ECM) protein. In addition, with an established field such as matrix biology, there is always the risk that the older (but still extremely valuable) protocols become buried in the literature. For these reasons, this issue of
1046-2023/$ - see front matter Ó 2008 Elsevier Inc. All rights reserved. doi:10.1016/j.ymeth.2008.04.001
Methods focuses on some of the methods and protocols that are in danger of being lost or re-invented. ECM proteins can be relatively large (many exceed 500 kDa), extensively post-translationally modified, and sparingly soluble. Furthermore, some ECM proteins readily polymerise into macromolecular aggregates that contain non-reducible crosslinks. Thus, ECM proteins can be refractory to conventional biochemical analysis and structure determination by standard high-resolution techniques of X-ray diffraction and NMR. Consequently, the protocols described in this issue of Methods have been optimised for the study of ECM macromolecules and macromolecular assemblies. Excellent reviews are cited as sources of more detailed descriptions and discussions. Readers are encouraged to contact the contributors directly for help and guidance before establishing the procedures in their own laboratories. Karl E. Kadler Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, ichael Smith Building, Oxford Road, Manchester M13 9PT, UK E-mail address: [email protected]
Methods 45 (2008) 1 www.elsevier.com/locate/ymeth
Guest Editor’s Introduction
Extracellular matrix (ECM) research
Research experimentalists require robust and wellproven protocols to perform even the simplest of experiments. Each laboratory has its own library of tried-and-tested recipes that are ‘inherited’ by successive generations of postgraduate students and postdoctoral fellows. In addition, an increasing number of commercial ‘kits’ are available for routine procedures such as RNA isolation, protein quantitation, and immunodetection. Specialised companies and organisations will also perform more complex procedures such as yeast two-hybrid molecular fishing and transgenic mouse generation. And of course, there is a wealth of literature from which to select peer-reviewed methods. However, despite this apparent glut of technical information, it is often difficult for newcomers to a research field to find a good protocol or to adapt an existing one. Furthermore, there is the lengthy process of acquiring detailed knowledge of the structure and solution properties of the molecule being studied, and this is especially important when the molecule being studied is an extracellular matrix (ECM) protein. In addition, with an established field such as matrix biology, there is always the risk that the older (but still extremely valuable) protocols become buried in the literature. For these reasons, this issue of
1046-2023/$ - see front matter Ó 2008 Elsevier Inc. All rights reserved. doi:10.1016/j.ymeth.2008.04.001
Methods focuses on some of the methods and protocols that are in danger of being lost or re-invented. ECM proteins can be relatively large (many exceed 500 kDa), extensively post-translationally modified, and sparingly soluble. Furthermore, some ECM proteins readily polymerise into macromolecular aggregates that contain non-reducible crosslinks. Thus, ECM proteins can be refractory to conventional biochemical analysis and structure determination by standard high-resolution techniques of X-ray diffraction and NMR. Consequently, the protocols described in this issue of Methods have been optimised for the study of ECM macromolecules and macromolecular assemblies. Excellent reviews are cited as sources of more detailed descriptions and discussions. Readers are encouraged to contact the contributors directly for help and guidance before establishing the procedures in their own laboratories. Karl E. Kadler Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, ichael Smith Building, Oxford Road, Manchester M13 9PT, UK E-mail address: [email protected]