MALDI mass spectrometry imaging of early- and late-stage serous ovarian cancer tissue reveals stage-specific N-glycans

Matthew T. Briggs; Mark R. Condina; Yin Ying Ho; Arun V. Everest-Dass; Parul Mittal; Gurjeet Kaur; Martin K. Oehler; Nicolle H. Packer; Peter Hoffmann

doi:10.1002/pmic.201800482

MALDI mass spectrometry imaging of early- and late-stage serous ovarian cancer tissue reveals stage-specific N-glycans

Matthew T. Briggs, Mark R. Condina, Yin Ying Ho, Arun V. Everest-Dass, Parul Mittal, Gurjeet Kaur, Martin K. Oehler, Nicolle H. Packer, Peter Hoffmann^*

^*Corresponding author for this work

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17 Citations (Scopus)

Abstract

Epithelial ovarian cancer is one of the most fatal gynecological malignancies in adult women. As studies on protein N-glycosylation have extensively reported aberrant patterns in the ovarian cancer tumor microenvironment, obtaining spatial information will uncover tumor-specific N-glycan alterations in ovarian cancer development and progression. matrix-assisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) is employed to investigate N-glycan distribution on formalin-fixed paraffin-embedded ovarian cancer tissue sections from early- and late-stage patients. Tumor-specific N-glycans are identified and structurally characterized by porous graphitized carbon-liquid chromatography-electrospray ionization-tandem mass spectrometry (PGC-LC-ESI-MS/MS), and then assigned to high-resolution images obtained from MALDI-MSI. Spatial distribution of 14 N-glycans is obtained by MALDI-MSI and 42 N-glycans (including structural and compositional isomers) identified and structurally characterized by LC-MS. The spatial distribution of oligomannose, complex neutral, bisecting, and sialylated N-glycan families are localized to the tumor regions of late-stage ovarian cancer patients relative to early-stage patients. Potential N-glycan diagnostic markers that emerge include the oligomannose structure, (Hex)₆ + (Man)₃(GlcNAc)₂, and the complex neutral structure, (Hex)₂ (HexNAc)₂ (Deoxyhexose)₁ + (Man)₃(GlcNAc)₂. The distribution of these markers is evaluated using a tissue microarray of early- and late-stage patients.

Original language	English
Article number	1800482
Pages (from-to)	1-11
Number of pages	11
Journal	Proteomics
Volume	19
Issue number	21-22
Early online date	31 Jul 2019
DOIs	https://doi.org/10.1002/pmic.201800482
Publication status	Published - Nov 2019

Keywords

formalin-fixed paraffin-embedded
mass spectrometry imaging
matrix-assisted laser desorption/ionization
N-glycan
ovarian cancer
tissue

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ARC CoE Nanoscale BioPhotonics (CNBP) (RAAP)
Piper, J., Goldys, E., Packer, N. & Jin, D.
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@article{2c701492335d44b3baacb45557c2f204,

title = "MALDI mass spectrometry imaging of early- and late-stage serous ovarian cancer tissue reveals stage-specific N-glycans",

abstract = "Epithelial ovarian cancer is one of the most fatal gynecological malignancies in adult women. As studies on protein N-glycosylation have extensively reported aberrant patterns in the ovarian cancer tumor microenvironment, obtaining spatial information will uncover tumor-specific N-glycan alterations in ovarian cancer development and progression. matrix-assisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) is employed to investigate N-glycan distribution on formalin-fixed paraffin-embedded ovarian cancer tissue sections from early- and late-stage patients. Tumor-specific N-glycans are identified and structurally characterized by porous graphitized carbon-liquid chromatography-electrospray ionization-tandem mass spectrometry (PGC-LC-ESI-MS/MS), and then assigned to high-resolution images obtained from MALDI-MSI. Spatial distribution of 14 N-glycans is obtained by MALDI-MSI and 42 N-glycans (including structural and compositional isomers) identified and structurally characterized by LC-MS. The spatial distribution of oligomannose, complex neutral, bisecting, and sialylated N-glycan families are localized to the tumor regions of late-stage ovarian cancer patients relative to early-stage patients. Potential N-glycan diagnostic markers that emerge include the oligomannose structure, (Hex)6 + (Man)3(GlcNAc)2, and the complex neutral structure, (Hex)2 (HexNAc)2 (Deoxyhexose)1 + (Man)3(GlcNAc)2. The distribution of these markers is evaluated using a tissue microarray of early- and late-stage patients.",

keywords = "formalin-fixed paraffin-embedded, mass spectrometry imaging, matrix-assisted laser desorption/ionization, N-glycan, ovarian cancer, tissue",

author = "Briggs, {Matthew T.} and Condina, {Mark R.} and Ho, {Yin Ying} and Everest-Dass, {Arun V.} and Parul Mittal and Gurjeet Kaur and Oehler, {Martin K.} and Packer, {Nicolle H.} and Peter Hoffmann",

year = "2019",

month = nov,

doi = "10.1002/pmic.201800482",

language = "English",

volume = "19",

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journal = "Proteomics",

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}

MALDI mass spectrometry imaging of early- and late-stage serous ovarian cancer tissue reveals stage-specific N-glycans. / Briggs, Matthew T.; Condina, Mark R.; Ho, Yin Ying; Everest-Dass, Arun V.; Mittal, Parul; Kaur, Gurjeet; Oehler, Martin K.; Packer, Nicolle H.; Hoffmann, Peter.

In: Proteomics, Vol. 19, No. 21-22, 1800482, 11.2019, p. 1-11.

Research output: Contribution to journal › Article › peer-review

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AU - Condina, Mark R.

AU - Ho, Yin Ying

AU - Everest-Dass, Arun V.

AU - Mittal, Parul

AU - Kaur, Gurjeet

AU - Oehler, Martin K.

AU - Packer, Nicolle H.

AU - Hoffmann, Peter

PY - 2019/11

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AB - Epithelial ovarian cancer is one of the most fatal gynecological malignancies in adult women. As studies on protein N-glycosylation have extensively reported aberrant patterns in the ovarian cancer tumor microenvironment, obtaining spatial information will uncover tumor-specific N-glycan alterations in ovarian cancer development and progression. matrix-assisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) is employed to investigate N-glycan distribution on formalin-fixed paraffin-embedded ovarian cancer tissue sections from early- and late-stage patients. Tumor-specific N-glycans are identified and structurally characterized by porous graphitized carbon-liquid chromatography-electrospray ionization-tandem mass spectrometry (PGC-LC-ESI-MS/MS), and then assigned to high-resolution images obtained from MALDI-MSI. Spatial distribution of 14 N-glycans is obtained by MALDI-MSI and 42 N-glycans (including structural and compositional isomers) identified and structurally characterized by LC-MS. The spatial distribution of oligomannose, complex neutral, bisecting, and sialylated N-glycan families are localized to the tumor regions of late-stage ovarian cancer patients relative to early-stage patients. Potential N-glycan diagnostic markers that emerge include the oligomannose structure, (Hex)6 + (Man)3(GlcNAc)2, and the complex neutral structure, (Hex)2 (HexNAc)2 (Deoxyhexose)1 + (Man)3(GlcNAc)2. The distribution of these markers is evaluated using a tissue microarray of early- and late-stage patients.

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KW - matrix-assisted laser desorption/ionization

KW - N-glycan

KW - ovarian cancer

KW - tissue

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JF - Proteomics

SN - 1615-9853

IS - 21-22

M1 - 1800482

ER -

MALDI mass spectrometry imaging of early- and late-stage serous ovarian cancer tissue reveals stage-specific N-glycans

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