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临床相关的翻译后修饰特异性蛋白质组学的当前策略与研究成果

Current strategies and findings in clinically relevant post-translational modification-specific proteomics.

作者信息

Pagel Oliver, Loroch Stefan, Sickmann Albert, Zahedi René P

机构信息

Leibniz-Institut für Analytische Wissenschaften - ISAS - e.V., Otto-Hahn-Straße 6b, 44227 Dortmund, Germany.

出版信息

Expert Rev Proteomics. 2015 Jun;12(3):235-53. doi: 10.1586/14789450.2015.1042867. Epub 2015 May 8.

DOI:10.1586/14789450.2015.1042867
PMID:25955281
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4487610/
Abstract

Mass spectrometry-based proteomics has considerably extended our knowledge about the occurrence and dynamics of protein post-translational modifications (PTMs). So far, quantitative proteomics has been mainly used to study PTM regulation in cell culture models, providing new insights into the role of aberrant PTM patterns in human disease. However, continuous technological and methodical developments have paved the way for an increasing number of PTM-specific proteomic studies using clinical samples, often limited in sample amount. Thus, quantitative proteomics holds a great potential to discover, validate and accurately quantify biomarkers in body fluids and primary tissues. A major effort will be to improve the complete integration of robust but sensitive proteomics technology to clinical environments. Here, we discuss PTMs that are relevant for clinical research, with a focus on phosphorylation, glycosylation and proteolytic cleavage; furthermore, we give an overview on the current developments and novel findings in mass spectrometry-based PTM research.

摘要

基于质谱的蛋白质组学极大地扩展了我们对蛋白质翻译后修饰(PTM)的发生和动态变化的认识。到目前为止,定量蛋白质组学主要用于研究细胞培养模型中的PTM调控,为异常PTM模式在人类疾病中的作用提供了新的见解。然而,持续的技术和方法发展为越来越多使用临床样本的PTM特异性蛋白质组学研究铺平了道路,而临床样本的量往往有限。因此,定量蛋白质组学在发现、验证和准确量化体液和原发性组织中的生物标志物方面具有巨大潜力。一项主要工作将是改进将强大但灵敏的蛋白质组学技术完全整合到临床环境中。在此,我们讨论与临床研究相关的PTM,重点是磷酸化、糖基化和蛋白水解切割;此外,我们概述了基于质谱的PTM研究的当前进展和新发现。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1182/4487610/b39135718e53/ieru-12-235-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1182/4487610/0dc5d021a465/ieru-12-235-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1182/4487610/1480c1fb8c9c/ieru-12-235-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1182/4487610/4b9bd87f631c/ieru-12-235-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1182/4487610/b39135718e53/ieru-12-235-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1182/4487610/0dc5d021a465/ieru-12-235-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1182/4487610/1480c1fb8c9c/ieru-12-235-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1182/4487610/4b9bd87f631c/ieru-12-235-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1182/4487610/b39135718e53/ieru-12-235-g004.jpg

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