MALDI Tissue Profiling of Integral Membrane Proteins from Ocular Tissues.

@article{citeulike:2648254, abstract = {MALDI tissue profiling and imaging have become valuable tools for rapid, direct analysis of tissues to investigate spatial distributions of proteins, potentially leading to an enhanced understanding of the molecular basis of disease. Sample preparation methods developed to date for these techniques produce protein expression profiles from predominantly hydrophilic, soluble proteins. The ability to obtain information about the spatial distribution of integral membrane proteins is critical to more fully understand their role in physiological processes, including transport, adhesion, and signaling. In this article, a sample preparation method for direct tissue profiling of integral membrane proteins is presented. Spatially resolved profiles for the abundant lens membrane proteins aquaporin 0 (AQP0) and MP20, and the retinal membrane protein opsin, were obtained using this method. MALDI tissue profiling results were validated by analysis of dissected tissue prepared by traditional membrane protein processing methods. Furthermore, direct tissue profiling of lens membrane proteins revealed age related post-translational modifications, as well as a novel modification that had not been detected using conventional tissue homogenization methods.}, address = {Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, South Carolina, USA.}, author = {Thibault, Danielle B B. and Gillam, Christopher J J. and Grey, Angus C C. and Han, Jun and Schey, Kevin L L. }, citeulike-article-id = {2648254}, doi = {http://dx.doi.org/10.1016/j.jasms.2008.03.002}, issn = {1044-0305}, journal = {Journal of the American Society for Mass Spectrometry}, keywords = {imaging, maldi}, month = {March}, posted-at = {2008-04-10 08:24:45}, priority = {4}, title = {MALDI Tissue Profiling of Integral Membrane Proteins from Ocular Tissues.}, url = {http://dx.doi.org/10.1016/j.jasms.2008.03.002}, year = {2008} }

TY - JOUR ID - citeulike:2648254 L3 - citeulike-article-id:2648254 N2 - MALDI tissue profiling and imaging have become valuable tools for rapid, direct analysis of tissues to investigate spatial distributions of proteins, potentially leading to an enhanced understanding of the molecular basis of disease. Sample preparation methods developed to date for these techniques produce protein expression profiles from predominantly hydrophilic, soluble proteins. The ability to obtain information about the spatial distribution of integral membrane proteins is critical to more fully understand their role in physiological processes, including transport, adhesion, and signaling. In this article, a sample preparation method for direct tissue profiling of integral membrane proteins is presented. Spatially resolved profiles for the abundant lens membrane proteins aquaporin 0 (AQP0) and MP20, and the retinal membrane protein opsin, were obtained using this method. MALDI tissue profiling results were validated by analysis of dissected tissue prepared by traditional membrane protein processing methods. Furthermore, direct tissue profiling of lens membrane proteins revealed age related post-translational modifications, as well as a novel modification that had not been detected using conventional tissue homogenization methods. JF - Journal of the American Society for Mass Spectrometry SN - 1044-0305 AD - Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, South Carolina, USA. TI - MALDI Tissue Profiling of Integral Membrane Proteins from Ocular Tissues. KW - imaging KW - maldi AU - Thibault, Danielle B AU - Gillam, Christopher J AU - Grey, Angus C AU - Han, Jun AU - Schey, Kevin L PY - 2008/03/18/ UR - http://dx.doi.org/10.1016/j.jasms.2008.03.002 ER -