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J Pharm Biomed Anal. 2016 Jan 25;118:380-386. doi: 10.1016/j.jpba.2015.11.010. Epub 2015 Nov 14.

Changes of protein glycosylation in the course of radiotherapy.

Author information

1
MS Proteomics Research Group, Institute of Organic Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary; Semmelweis University, School of Ph.D. Studies, Budapest, Hungary.
2
Core Technologies Centre, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
3
MS Proteomics Research Group, Institute of Organic Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
4
Maria Sklodowska-Curie Memorial Cancer Center and Institute of Oncology, Gliwice Branch, Gliwice, Poland.
5
MS Proteomics Research Group, Institute of Organic Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary. Electronic address: drahos.laszlo@ttk.mta.hu.

Abstract

This is the first study of changes in protein glycosylation due to exposure of human subjects to ionizing radiation. Site specific glycosylation patterns of 7 major plasma proteins were analyzed; 171 glycoforms were identified; and the abundance of 99 of these was followed in the course of cancer radiotherapy in 10 individual patients. It was found that glycosylation of plasma proteins does change in response to partial body irradiation (∼ 60 Gy), and the effects last during follow-up; the abundance of some glycoforms changed more than twofold. Both the degree of changes and their time-evolution showed large inter-individual variability.

KEYWORDS:

Glycosylation; Glycosylation pattern; Head and neck cancer; Proteomics; Radiotherapy

PMID:
26609677
DOI:
10.1016/j.jpba.2015.11.010
[Indexed for MEDLINE]

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