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• W2416096752 abstract "PROTEOMICSVolume 14, Issue 7-8 p. 805-806 EditorialFree Access Tissue proteomics and imaging mass spectrometry First published: 01 April 2014 https://doi.org/10.1002/pmic.201470053Citations: 1AboutSectionsPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Carlos Lodeiro (left), José Luis Capelo Martínez (center), Hugo M. Santos (right) Tissues are an invaluable source of medical and biological information. It is well known that in medical diagnostics tissue components are studied at the molecular level. Nowadays the technology has evolved to a level in which molecules originating in a tissue can be detected in other parts of the body. Thus, one of the main applications currently performed in most laboratories consists in identifying molecules characteristic of a given status of a tissue, for instance a disease. Most likely, the molecules over-expressed in a tissue as a consequence of disease will be over-expressed in other body fluids, such as serum, plasma or urine. If such molecules could be detected at the very early stage of the disease, this would help in diagnostics. Also, following their concentration levels while the patient is under medical treatment would assist therapeutics. In addition, physicians have preserved tissue for many years as formalin-fixed, paraffin-embedded (FFPE) tissues which has led to the creation of so-called tissue bio-banks. The potential of such banks is very promising, as the tissues can be studied from a proteomic, metabolomic and genomic point of view. Moreover, the tissues provide a detailed clinical background of the patient, and thus the possibility for retrieving information for diagnosis, prognosis, and tailored therapy is enormous. Using the words “tissue” and “protein” in the search engine Scopus the oldest manuscript retrieved dates back to 1905 1, and yet there is still much work to be done in tissue proteomics and analysis. As an example, extraction of proteins from tissues is challenging because although there is agreement about the variables influencing the extraction process, namely composition of the extraction buffer (pH and glycerol), temperature of extraction and application of ultrasound, there is no agreement about the levels at which such variables must be set 2-5. Furthermore, in the case of FFPE tissues, the reaction of formaldehyde with proteins or peptides involves the formation of an unstable methylol group through the reaction of an amino or thiol group of lysine, histidine, arginine or cysteine residues. Then the methylol group reacts with lysine or tryptophan to yield Schiff bases which may induce the formation of stable intra- or inter-chain methylene bridges with amino acids such as arginine, asparagine, glutamine, histidine, tryptophan and tyrosine residues 5. Such changes promote the modification of the mass and composition of peptides, thus making protein identification by mass spectrometry difficult. As technology evolved, Caprioli et al 6 made a step forward in the analysis of tissues when they developed the modern concepts of so-called imaging mass spectrometry (IMS). At the beginning, matrix assisted laser desorption ionization time of flight mass spectrometry was the technique used to simultaneously analyse the distribution of hundreds of biomolecules. Nowadays, the hyphenation of different techniques of analysis has allowed IMS to develop further, for example, atmospheric laser desorption ionization combined with time of flight mass spectrometry, or with inductively coupled plasma mass spectrometry. Furthermore, the use of electrospray in IMS for imaging tissues is also breaking frontiers of knowledge and catching up with MALDI 7. Last but not least, the software currently being developed for IMS is going where no other has gone before in mass spectrometry, as the first steps towards 3D software for IMS are being taken 7. The importance of IMS is recognised by the EU through the funding given to the BMBS COST Action BM1104 (for further information, see web page at: http://www.maldi-msi.org/index.php?option=com_content&view=article&id=252&Itemid=78). This COST action is intended to expand the frontiers of knowledge in IMS as well as to bring together research experts in the field to share knowledge and new ideas to promote IMS. Some of the authors of this special issue participate in COST BM1104. In spite of the great amount of work already put by the research community into tissue proteomics, this field of research is, in our opinion, far from maturity and much work is still to be done. For instance, 3D IMS needs to be improved considerably and much effort is required to understand the protein modifications caused by FFPE techniques. Furthermore, shortening sample treatment time and increasing sample throughput still represent a challenge. Moreover, nanotechnology is going to play an important role in future developments. As analytical biochemists we are looking forward to the next advances in this field of research to which we hope to contribute as we have done in the past 5, 8, 9. In this special issue, relevant researchers in the area of tissue proteomics present some of their finest recent work. It includes papers on sample treatment for tissues, new insights into tissue cancer proteomics and new approaches to IMS. In addition, Professor Caprioli honours us by presenting his point of view about the future of tissue proteomics with a focus on imaging. We are in indebted to our colleagues and contributors to this special issue. Finally, Professor Michael J. Dunn, Dr. Hans-Joachim Kraus and Wiley are kindly acknowledged for allowing us to launch this special issue. We hope you enjoy it!. Carlos Lodeiro José Luis Capelo Martínez Hugo M. Santos BIOSCOPE Group, Chemistry Department, NOVA University of Lisbon, Caparica, Portugal. www.bioscopegroup.org References 1Robertson, T. B., On the conditions of equilibrium of an associating amphoteric electrolyte in the presence of any number of non-amphoteric electrolytes. J. Phys. Chem. 1905, 10, 524– 582. CrossrefGoogle Scholar 2Shi, S. R., Shi, Y., Taylor, C. R., Antigen retrieval immunohistochemistry: review and future prospects in research and diagnosis over two decades. J. Histochem. Cytochem. 2011, 59, 13– 32. CrossrefCASPubMedWeb of Science®Google Scholar 3Magdeldin, S., Yamamoto, T., Toward deciphering proteomes of formalin-fixed paraffin-embedded (FFPE) tissues. Proteomics 2012, 12, 1045– 1058. Wiley Online LibraryCASPubMedWeb of Science®Google Scholar 4Tian, K., Gurley, D., Meany, L., Kemp, C. J., Zhang, H., Protein phosphorylation analysis in archival clinical cancer samples by shotgun and targeted proteomics approaches. J. Proteome Res. 2009, 8, 1657– 1662. CrossrefCASPubMedWeb of Science®Google Scholar 5Araújo, J. E., Oliveira, E., Otero-Glez, A., Santos Nores, J. et al., A comprehensive factorial design study of variables affecting protein extraction from formalin-fixed kidney tissue samples. Talanta, 2014, 119, 90– 97. CrossrefCASWeb of Science®Google Scholar 6Giusti, L., Lucacchuni, A., Proteomic studies of formalin-fixed paraffin-embedded tissues. Expert. Rev. Proteomics 2013, 10, 165– 177. CrossrefCASPubMedWeb of Science®Google Scholar 7Caprioli, R. M., Farmer, T. B., Gile, J., Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS. Anal. Chem., 1997, 69, 4751– 4760. CrossrefCASPubMedWeb of Science®Google Scholar 8Santos, H. M., Kouvonen, P., Capelo, J. L., Corthals, G. L., Isotopic labelling of peptides in tissues enhances mass spectrometric profiling. Rapid Commun. Mass Spectrom. 2012, 26, 254– 262. Wiley Online LibraryCASPubMedWeb of Science®Google Scholar 9Santos, H. M., Kouvonen, P., Capelo, J. L., Corthals, G. L., On-target ultrasonic digestion of proteins. Proteomics, 2013, 13, 1423– 1427. Wiley Online LibraryCASPubMedWeb of Science®Google Scholar Citing Literature Volume14, Issue7-8Special Issue: Tissue Proteomics and Imaging Mass SpectrometryApril 2014Pages 805-806 ReferencesRelatedInformation" @default.
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