Mass spectrometry-based N-linked glycomic profiling as a means for tracking pancreatic cancer metastasis

Hae-Min Park; Mintai Peter Hwang; Yoon-Woo Kim; Kyoung-Jin Kim; Jang Mi Jin; Young Hwan Kim; Yung-Hun Yang; Kwan Hyi Lee; Yun-Gon Kim

doi:10.1016/j.carres.2015.04.019

Mass spectrometry-based N-linked glycomic profiling as a means for tracking pancreatic cancer metastasis

Carbohydr Res. 2015 Sep 2:413:5-11. doi: 10.1016/j.carres.2015.04.019. Epub 2015 May 2.

Authors

Hae-Min Park¹, Mintai Peter Hwang², Yoon-Woo Kim³, Kyoung-Jin Kim³, Jang Mi Jin⁴, Young Hwan Kim⁵, Yung-Hun Yang⁶, Kwan Hyi Lee⁷, Yun-Gon Kim⁸

Affiliations

¹ School of Chemical and Biological Engineering, Seoul National University, Seoul 151-742, South Korea.
² Biomedical Research Institute, Korea Institute of Science and Technology (KIST), 5 Hwarangno 14-gil, Seongbuk-gu, Seoul 136-791, South Korea.
³ Department of Chemical Engineering, Soongsil University, 369 Sangdo-Ro, Seoul 156-743, South Korea.
⁴ Biomedical Omics Team, Korea Basic Science Institute, Ochang 363-883, South Korea.
⁵ Biomedical Omics Team, Korea Basic Science Institute, Ochang 363-883, South Korea; Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon 305-764, South Korea; Department of Bio-Analytical Science, University of Science and Technology, Daejeon 305-333, South Korea.
⁶ Department of Microbial Engineering, College of Engineering, Konkuk University, Seoul 143-701, South Korea.
⁷ Biomedical Research Institute, Korea Institute of Science and Technology (KIST), 5 Hwarangno 14-gil, Seongbuk-gu, Seoul 136-791, South Korea. Electronic address: kwanhyi@kist.re.kr.
⁸ Department of Chemical Engineering, Soongsil University, 369 Sangdo-Ro, Seoul 156-743, South Korea. Electronic address: ygkim@ssu.ac.kr.

PMID: 26057990
DOI: 10.1016/j.carres.2015.04.019

Abstract

The aberrant glycosylation profile on the surface of cancer cells has been recognized for its potential diagnostic value towards assessing tumor progression. In this study, we initially investigate N-glycan profiles on the surface of normal (HPDE) and cancerous (Capan-1, Panc-1, and MIA PaCa-2) pancreatic cell lines, which are from different sites of pancreatic tumor. The enzymatically deglycosylated total N-glycans are permethylated via a quantitative solid-phase method and then analyzed by using MALDI-TOF MS and MALDI-QIT-TOF MS. We demonstrate that the level of high-mannose type glycans is higher among Capan-1 cells-pancreatic cancer cells that have metastasized to the liver-than that observed among Panc-1 and MIA PaCa-2 cells-pancreatic cancer cells from the pancreas duct head and tail regions, respectively. Furthermore, the relative abundance of highly-branched sialyted N-glycans is significantly up-regulated on Panc-1 and MIA PaCa-2 pancreatic cancer cells compared to that of normal HPDE pancreas cells. Taken together, these results indicate that specific N-glycosylation profile changes in pancreatic cancer cells can be used to not only distinguish between normal and cancerous cells but also provide more information on their location and metastatic potential.

Keywords: MALDI-TOF MS; N-glycans; Pancreatic cells; Qualitative and quantitative analysis.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Biomarkers, Tumor / chemistry
Cell Line, Tumor
Glycoconjugates / chemistry
Glycomics*
Humans
Mass Spectrometry
Neoplasm Metastasis
Nitrogen / chemistry*
Pancreatic Neoplasms / pathology*
Polysaccharides / chemistry*

Substances

Biomarkers, Tumor
Glycoconjugates
Polysaccharides
Nitrogen