MALDI Tissue Profiling of Integral Membrane Proteins from Ocular Tissues
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...
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| Veröffentlicht in: | Journal of the American Society for Mass Spectrometry 2008-06, Vol.19 (6), p.814-822 |
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| container_title | Journal of the American Society for Mass Spectrometry |
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| creator | Thibault, Danielle B. Gillam, Christopher J. Grey, Angus C. Han, Jun Schey, Kevin L. |
| description | 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. |
| doi_str_mv | 10.1016/j.jasms.2008.03.002 |
| format | Article |
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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. 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Psychology ; Gene Expression Profiling - methods ; Lens, Crystalline - chemistry ; Membrane Proteins - chemistry ; Organic Chemistry ; Proteomics ; Rabbits ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods ; Swine ; Vertebrates: nervous system and sense organs</subject><ispartof>Journal of the American Society for Mass Spectrometry, 2008-06, Vol.19 (6), p.814-822</ispartof><rights>2008 American Society for Mass Spectrometry</rights><rights>American Society for Mass Spectrometry 2008</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c532t-63bb5b15648cbc328f6f735234c3bb811ca96733a49722038411bc7eea8f49373</citedby><cites>FETCH-LOGICAL-c532t-63bb5b15648cbc328f6f735234c3bb811ca96733a49722038411bc7eea8f49373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1016/j.jasms.2008.03.002$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1016/j.jasms.2008.03.002$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20384279$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18396059$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Thibault, Danielle B.</creatorcontrib><creatorcontrib>Gillam, Christopher J.</creatorcontrib><creatorcontrib>Grey, Angus C.</creatorcontrib><creatorcontrib>Han, Jun</creatorcontrib><creatorcontrib>Schey, Kevin L.</creatorcontrib><title>MALDI Tissue Profiling of Integral Membrane Proteins from Ocular Tissues</title><title>Journal of the American Society for Mass Spectrometry</title><addtitle>J Am Soc Mass Spectrom</addtitle><addtitle>J Am Soc Mass Spectrom</addtitle><description>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.</description><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cattle</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Eye and associated structures. Visual pathways and centers. Vision</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Profiling - methods</subject><subject>Lens, Crystalline - chemistry</subject><subject>Membrane Proteins - chemistry</subject><subject>Organic Chemistry</subject><subject>Proteomics</subject><subject>Rabbits</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</subject><subject>Swine</subject><subject>Vertebrates: nervous system and sense organs</subject><issn>1044-0305</issn><issn>1879-1123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhSNERUvhCZBQNnSX9NrXieMFSFVb6EhTlUVZW47HGRwldrGTSrw9npmo0E1Z2dL5zv07WfaBQEmA1Od92as4xpICNCVgCUBfZSek4aIghOLr9AfGCkCojrO3MfYAhIPgb7Jj0qCooRIn2c3txfpqld_bGGeTfw--s4N129x3-cpNZhvUkN-asQ3K7eXJWBfzLvgxv9PzoMJije-yo04N0bxf3tPsx9fr-8ubYn33bXV5sS50hXQqamzbqiVVzRrdaqRNV3ccK4pMJ6UhRCtRc0TFBKcUsGGEtJobo5qOCeR4mn051H2Y29FstHFTmlE-BDuq8Ft6ZeVzxdmfcusfJWUIQmAqcLYUCP5XGnySo43aDEPa0M9RcuCcYMUSiAdQBx9jMN1TEwJyl4Ds5T4BuUtAAsqUQHJ9_He-v57l5An4tAAqajV06bLaxiduvzPlO44duJgktzVB9n4OLt32P_0_H2wmhfBoky1qa5w2GxuMnuTG2xf9fwC6lLZl</recordid><startdate>20080601</startdate><enddate>20080601</enddate><creator>Thibault, Danielle B.</creator><creator>Gillam, Christopher J.</creator><creator>Grey, Angus C.</creator><creator>Han, Jun</creator><creator>Schey, Kevin L.</creator><general>Elsevier Inc</general><general>Springer-Verlag</general><general>Elsevier Science</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20080601</creationdate><title>MALDI Tissue Profiling of Integral Membrane Proteins from Ocular Tissues</title><author>Thibault, Danielle B. ; Gillam, Christopher J. ; Grey, Angus C. ; Han, Jun ; Schey, Kevin L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532t-63bb5b15648cbc328f6f735234c3bb811ca96733a49722038411bc7eea8f49373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Analytical Chemistry</topic><topic>Animals</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cattle</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Eye and associated structures. Visual pathways and centers. Vision</topic><topic>Fundamental and applied biological sciences. 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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. 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| subjects | Analytical Chemistry Animals Bioinformatics Biological and medical sciences Biotechnology Cattle Chemistry Chemistry and Materials Science Eye and associated structures. Visual pathways and centers. Vision Fundamental and applied biological sciences. Psychology Gene Expression Profiling - methods Lens, Crystalline - chemistry Membrane Proteins - chemistry Organic Chemistry Proteomics Rabbits Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods Swine Vertebrates: nervous system and sense organs |
| title | MALDI Tissue Profiling of Integral Membrane Proteins from Ocular Tissues |
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