The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Tissue Profiling by Mass Spectrometry
Open accessAbstract
Matrix-assisted laser desorption ionization mass spectrometry (MALDI MS) has become a valuable tool to address a broad range of questions in many areas of biomedical research. One such application allows spectra to be obtained directly from intact tissues, termed "profiling" (low resolution) and "imaging" (high resolution). In light of the fact that MALDI tissue profiling allows over a thousand peptides and proteins to be rapidly detected from a variety of tissues, its application to disease processes is of special interest. For example, protein profiles from tumors may allow accurate prediction of tumor behavior, diagnosis, and prognosis and uncover etiologies underlying idiopathic diseases. MALDI MS, in conjunction with laser capture microdissection, is able to produce protein expression profiles from a relatively small number of cells from specific regions of heterogeneous tissue architectures. Imaging mass spectrometry enables the investigator to assess the spatial distribution of proteins, drugs, and their metabolites in intact tissues. This article provides an overview of several tissue profiling and imaging applications performed by MALDI MS, including sample preparation, matrix selection and application, histological staining prior to MALDI analysis, tissue profiling, imaging, and data analysis. Several applications represent direct translation of this technology to clinically relevant problems.
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Citations
Cites
Molecular Imaging of Biological Samples: Localization of Peptides and Proteins Using MALDI-TOF MS
Caprioli, R. M., Farmer, T. B., & Gile, J. (1997) · Analytical Chemistry · doi:10.1021/ac970888i · Cited by 2,234
Self-citation
Cited by
Norris, J. L., & Caprioli, R. M. (2013) · Chemical Reviews · doi:10.1021/cr3004295 · Cited by 696
Self-citationAmbient mass spectrometry: bringing MS into the “real world”
Alberici, R. M., Simas, R. C., Sanvido, G. B., Romão, W., Lalli, P. M., Benassi, M., Cunha, I. B. S., & Eberlin, M. N. (2010) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-010-3808-3 · Cited by 340
Methods for samples preparation in proteomic research
Bodzon-Kulakowska, A., Bierczynska-Krzysik, A., Dylag, T., Drabik, A., Suder, P., Noga, M., Jarzebinska, J., & Silberring, J. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.10.040 · Cited by 254
Porcine Models of Cutaneous Wound Healing
Seaton, M., Hocking, A., & Gibran, N. S. (2015) · ILAR Journal · doi:10.1093/ilar/ilv016 · Cited by 249
Sumner, L. W., Lei, Z., Nikolau, B. J., & Saito, K. (2015) · Natural Product Reports · doi:10.1039/c4np00072b · Cited by 233
Metadata
- Authors
- Caldwell, R. L., & Caprioli, R. M.
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2005-04
- Volume
- 4
- Issue
- 4
- Pages
- 394-401
- ISSN
- 1535-9476 (ISSN-L)
- OpenAlex
- W2106034668
- Cited by
- 259
- References
- 1
- FWCI
- 12.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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