Tag-Mass:  Specific Molecular Imaging of Transcriptome and Proteome by Mass Spectrometry Based on Photocleavable Tag

Lemaire, R.; Stauber, Jonathan; Wisztorski, Maxence; Camp, Christelle Van; Desmons, Annie; Deschamps, Mathieu C.; Proess, G.; Rudlof, I.; Woods, Amina S.; Day, Robert; Salzet, Michel; Fournier, Isabelle

doi:10.1021/pr0700044

Cited by 75 publications

(84 citation statements)

References 18 publications

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“…Our group previously developed and patented a method for mapping specific compounds in ovarian cancer tissues (Fournier et al, 2006;Lemaire et al, 2005aLemaire et al, , 2007b. In this method, called Tag Mass, an antibody is linked to a lasercleavable peptide of known sequence.…”

Section: Resultsmentioning

confidence: 99%

“…In this method, called Tag Mass, an antibody is linked to a lasercleavable peptide of known sequence. The image of the m/z ratio of this peptide is generated, and the peptide's sequence is determined by MS/MS (Lemaire et al, 2007b). Here, another method to screen for the presence of antibodies raised against specific markers in tissue sections is described.…”

Section: Resultsmentioning

confidence: 99%

“…Tag-Mass involves a modified probe bearing a reporter group that is used in MALDI-MSI. The image of the marker is then indirectly generated from the probe (Lemaire et al, 2007b). This technology is compatible with all types of probes, including mRNA, antibodies, or even lectins or aptamers.…”

Section: Discussionmentioning

confidence: 99%

“…One application of the Tag-Mass technology is MSI based and uses photocleavable, tagged antibody probes grafted to specific antibodies for a given biomarker (Gagnon et al, 2012;Lemaire et al, 2005aLemaire et al, , 2007bStauber et al, 2009). This strategy relies on the design of specific antibodies that are used for immunohistochemistry (IHC), which are linked to tag peptides of known sequences (Gagnon et al, 2012) and can be detected by mass spectrometry.…”

mentioning

confidence: 99%

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Spectroimmunohistochemistry: A Novel Form of MALDI Mass Spectrometry Imaging Coupled to Immunohistochemistry for Tracking Antibodies

Longuespée

Boyon

Desmons

et al. 2014

OMICS: A Journal of Integrative Biology

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MALDI mass spectrometry imaging (MALDI-MSI) is currently used for clinical applications, such as biomarker identification, particularly for the study of solid tumors. The ability to map specific compounds that have been determined to be biomarkers and therapeutic targets is relevant for the evaluation of the efficacy of targeted therapies. This article describes a new method called Spectro-ImmunoHistoChemistry (SIHC), which combines the use of specific antibodies against markers and mass spectrometric imaging in the MS/MS mode. SIHC is based on direct primary antibody-antigen recognition, trypsin digestion of the antibody overlaying the markers of interest in the tissue section, and MALDI-MSI of the tryptic peptides generated from the antibody. This approach has both clinical and pharmacological applications. First, it can be used as a cross-validation method to monitor the presence specifically of a marker in a tissue section. Second, SIHC could potentially be used as a novel technology for tracking specific antibodies after in vivo injection for anti-cancer treatments. Additionally, SIHC could enable novel clinical applications of MSI, such as monitoring the efficacy of cytotoxic antibody treatments.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Spectroimmunohistochemistry: A Novel Form of MALDI Mass Spectrometry Imaging Coupled to Immunohistochemistry for Tracking Antibodies

Longuespée

Boyon

Desmons

et al. 2014

OMICS: A Journal of Integrative Biology

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“…6, d, e, and f), specific MALDI-MSI using the Tag-mass concept (Fig. 6g) (59), quantitative PCR, and Western blot (Fig. 6h).…”

Section: Early Disease Detectionmentioning

confidence: 99%

MALDI Imaging Mass Spectrometry

Franck

Arafah

Elayed

et al. 2009

Molecular & Cellular Proteomics

152

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A decade after its inception, MALDI imaging mass spectrometry has become a unique technique in the proteomics arsenal for biomarker hunting in a variety of diseases. At this stage of development, it is important to ask whether we can consider this technique to be sufficiently developed for routine use in a clinical setting or an indispensable technology used in translational research. In this report, we consider the contributions of MALDI imaging mass spectrometry and profiling technologies to clinical studies. In addition, we outline new directions that are required to align these technologies with the objectives of clinical proteomics, including: 1) diagnosis based on profile signatures that complement histopathology, 2) early detection of disease, 3) selection of therapeutic combinations based on the individual patient's entire disease-specific protein network, 4) real time assessment of therapeutic efficacy and toxicity, 5) rational redirection of therapy based on changes in the diseased protein network that are associated with drug resistance, and 6) combinatorial therapy in which the signaling pathway itself is viewed as the target rather than any single "node" in the pathway.

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Imaging Mass Spectrometry

Remoortere¹,

Jones²,

Deelder³

et al. 2012

Encyclopedia of Drug Metabolism and Interactions

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Imaging mass spectrometry combines the chemical specificity and parallel detection of mass spectrometry with microscopic imaging capabilities. The ability to simultaneously obtain images from all analytes detected, from atomic to macromolecular ions, allows the analyst to probe the chemical organization of a sample and to correlate this with physical features. The sensitivity of the ionization step, sample preparation, the spatial resolution, and the speed of the technique are all important parameters that affect the type of information obtained. Recently, significant progress has been made in each of these steps for both secondary ion mass spectrometry (SIMS) and matrix-assisted laser desorption/ionization (MALDI) imaging of biological samples. Examples demonstrating localization of proteins in tumors, a reduction of lamellar phospholipids in the region binding two single celled organisms, and sub-cellular distributions of several biomolecules have all contributed to an increasing upsurge in interest in imaging mass spectrometry. Here we review many of the instrumental developments and methodological approaches responsible for this increased interest, compare and contrast the information provided by SIMS and MALDI imaging, and discuss future possibilities.

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Tag-Mass: Specific Molecular Imaging of Transcriptome and Proteome by Mass Spectrometry Based on Photocleavable Tag

Cited by 75 publications

References 18 publications

Spectroimmunohistochemistry: A Novel Form of MALDI Mass Spectrometry Imaging Coupled to Immunohistochemistry for Tracking Antibodies

Spectroimmunohistochemistry: A Novel Form of MALDI Mass Spectrometry Imaging Coupled to Immunohistochemistry for Tracking Antibodies

MALDI Imaging Mass Spectrometry

Imaging Mass Spectrometry

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