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Tissue Profiling by Mass Spectrometry

Open access
Caldwell, Robert L., Caprioli, Richard M.·2005·Molecular & Cellular Proteomics

Abstract

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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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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CoChat. (2026). Citation check: Tissue Profiling by Mass Spectrometry. https://app.cochat.ai/papers/10.1074/mcp.r500006-mcp200
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Caldwell, R. L., & Caprioli, R. M. (2005). Tissue Profiling by Mass Spectrometry. Molecular & Cellular Proteomics. https://doi.org/10.1074/mcp.r500006-mcp200

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