Peptide and protein imaging mass spectrometry in cancer research

McDonnell, Liam A.; Corthals, Garry L.; Willems, Stefan M.; Remoortere, Alexandra van; Zeijl, René J. M. van; Deelder, André M.

doi:10.1016/j.jprot.2010.05.007

Cited by 151 publications

(132 citation statements)

References 99 publications

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“…MALDI imaging has found a large panel of applications in pharmacology and pathology fields (El Ayed et al, 2010;Longuespee et al, 2012;2014a;McDonnell et al, 2010;Meding et al, 2012;Willems et al, 2010). This technology is a valuable tool for biomarker hunting in pathology and is complementary to the use of classical methods in histopathology (Meding et al, 2012).…”

Section: Tissue Proteomics 7 Maldi Mass Spectrometry Imagingmentioning

confidence: 99%

Tissue Proteomics for the Next Decade? Towards a Molecular Dimension in Histology

Longuespée

Fléron

Pottier

et al. 2014

OMICS: A Journal of Integrative Biology

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Section: Tissue Proteomics 7 Maldi Mass Spectrometry Imagingmentioning

confidence: 99%

Tissue Proteomics for the Next Decade? Towards a Molecular Dimension in Histology

Longuespée

Fléron

Pottier

et al. 2014

OMICS: A Journal of Integrative Biology

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“…This technology allows for the visualization of the distribution of biomolecules (peptides, proteins and lipids) across a tissue section where the relative abundance of hundreds of biomolecules can be mapped across the entire tissue section [8][9][10][11][12][13]. It is thus possible to use MALDI-IMS spectral data of tissue biopsies to detect numerous cancer-associated biochemical changes [14].…”

Section: Introductionmentioning

confidence: 99%

Assessment of molecular differentiation in FFPE colon adenocarcinoma tissues using PCA analysis of MALDI IMS spectral data

Panderi¹,

Perez²,

Cao³

et al. 2017

J Appl Bioanal

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MALDI IMS datasets comprise huge amounts of spectra and their interpretation requires the use of multivariate statistical methods. MALDI IMS spectral data have been processed using sequential principal component analysis and 2-D peak distribution tests so as to investigate the molecular differentiation of tumor regions in formalin-fixed paraffin-embedded tissue biopsies of colorectal adenocarcinoma. In some of the cases fresh frozen tissue section samples were also analyzed for comparison. Multivariate analysis of spectral data revealed a specific pattern of mass ion peaks in different tumor regions that were distinguishable from the adjacent normal regions within a given specimen. Moreover, similar mass ion peaks could be detected in both FFPE and fresh-frozen tissue section samples. These significant mass ion peaks have been used to generate ion images and visualize the difference between tumor and normal regions. These specific and statistically significant ion peaks may serve as potential biomarkers for colorectal adenocarcinoma.

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“…The detector enables proteins up to 70 kDa to be imaged, and proteins up to 110 kDa to be detected, directly from tissue, and indicates new directions by which the mass range amenable to MALDI imaging MS and MALDI profiling MS may be extended. (J Am Soc Mass Spectrom 2010, 21, 1922-1929) © 2010 American Society for Mass Spectrometry S ince its inception ϳ10 y ago, MALDI imaging mass spectrometry (imaging MS) has developed into a powerful and versatile tool for biomedical research [1,2]. It is now routinely used for analyzing peptides and small proteins up to 25 kDa [3-6], administered drugs and their metabolites [7], and recently major improvements have been reported for lipids [8].…”

mentioning

confidence: 99%

“…S ince its inception ϳ10 y ago, MALDI imaging mass spectrometry (imaging MS) has developed into a powerful and versatile tool for biomedical research [1,2]. It is now routinely used for analyzing peptides and small proteins up to 25 kDa [3][4][5][6], administered drugs and their metabolites [7], and recently major improvements have been reported for lipids [8].…”

mentioning

confidence: 99%

“…In principal, this 'bottom-up' strategy could enable proteins of any mass to be detected. In practice the large increase in complexity associated with proteolysing the entire tissue's protein content will cause many tryptic peptides to have identical nominal mass [1], thus undermining the identification of potential biomarkers. Furthermore, bottom-up MALDI imaging MS discards all information regarding protein isoforms unless the appropriate tryptic peptides are explicitly included in the analysis.…”

mentioning

confidence: 99%

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MALDI imaging and profiling MS of higher mass proteins from tissue

Remoortere

Zeijl

Oever

et al. 2010

J. Am. Soc. Mass Spectrom.

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111

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MALDI imaging and profiling mass spectrometry of proteins typically leads to the detection of a large number of peptides and small proteins but is much less successful for larger proteins: most ion signals correspond to proteins of m/z Ͻ 25,000. This is a severe limitation as many proteins, including cytokines, growth factors, enzymes, and receptors have molecular weights exceeding 25 kDa. The detector technology typically used for protein imaging, a microchannel plate, is not well suited to the detection of high m/z ions and is prone to detector saturation when analyzing complex mixtures. Here we report increased sensitivity for higher mass proteins by using the CovalX high mass HM1 detector (Zurich, Switzerland), which has been specifically designed for the detection of high mass ions and which is much less prone to detector saturation. The results demonstrate that a range of different sample preparation strategies enable higher mass proteins to be analyzed if the detector technology maintains high detection efficiency throughout the mass range. The detector enables proteins up to 70 kDa to be imaged, and proteins up to 110 kDa to be detected, directly from tissue, and indicates new directions by which the mass range amenable to MALDI imaging MS and MALDI profiling MS may be extended. (J Am Soc Mass Spectrom 2010, 21, 1922-1929) © 2010 American Society for Mass Spectrometry S ince its inception ϳ10 y ago, MALDI imaging mass spectrometry (imaging MS) has developed into a powerful and versatile tool for biomedical research [1,2]. It is now routinely used for analyzing peptides and small proteins up to 25 kDa [3-6], administered drugs and their metabolites [7], and recently major improvements have been reported for lipids [8]. Despite this success, proteins exceeding 25 kDa are not routinely detected. Proteins larger than 25 kDa include many proteins with important biological activities, such as most cytokines, growth factors, enzymes, receptors, proproteins, and neuropeptide precursors. Increasing the mass range of proteins amenable to MALDI imaging MS might enable these biologically crucial proteins to be included in current applications, e.g., biomarker discovery.The most common technique currently used to access larger proteins in MALDI imaging MS analyses is based on proteolytic digestion of the tissue's proteins followed by MALDI imaging MS of their tryptic peptides. Note on-tissue digestion has the additional advantage that it can be applied to formalin fixed tissues as proteolytic peptides can be generated that are not bound within the cross-linked protein matrix. For example, Djidja et al. used on-tissue digestion to determine that the 78 kDa protein GRP78 may be a new candidate protein biomarker of pancreatic adenocarcinoma [9]. In principal, this 'bottom-up' strategy could enable proteins of any mass to be detected. In practice the large increase in complexity associated with proteolysing the entire tissue's protein content will cause many tryptic peptides to have identical nominal mass [1], thus under...

show abstract

Peptide and protein imaging mass spectrometry in cancer research

Cited by 151 publications

References 99 publications

Tissue Proteomics for the Next Decade? Towards a Molecular Dimension in Histology

Tissue Proteomics for the Next Decade? Towards a Molecular Dimension in Histology

Assessment of molecular differentiation in FFPE colon adenocarcinoma tissues using PCA analysis of MALDI IMS spectral data

MALDI imaging and profiling MS of higher mass proteins from tissue

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