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Development of Enabling Tools for Global Profiling and Quantitative Analysis of Protein Post-Translational Modifications
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Development of Enabling Tools for Global Profiling and Quantitative Analysis of Protein Post-Translational Modifications
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Dissertation
Development of Enabling Tools for Global Profiling and Quantitative Analysis of Protein Post-Translational Modifications
2020
Overview
Protein post-translational modifications (PTMs) involve the covalent chemical modifications of specific amino acid residues in proteins, which play crucial roles in protein physiochemical properties, structures and their physiological functions. Alterations in protein PTMs have been implicated in many serious diseases. Comprehensive study of disease-related protein PTMs is critical to explore their roles in the pathogenesis of diseases, contributing to the diagnosis and clinical treatment of diseases. Recently, given the capability of monitoring and identifying thousands of peptides simultaneously, mass spectrometry (MS) has evolved as a powerful tool in bottom-up proteomics, especially the protein PTM analysis.This dissertation is devoted to the development and application of novel electrospray ionization mass spectrometry (ESI-MS) based strategies for the in-depth profiling and quantitative analysis of several important protein PTMs as well as matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) technique for the in-situ imaging of biomolecules. A portion of this dissertation describes the development of a novel biotin tag-assisted MS-based method, as the first method, for the in-depth profiling of citrullinated and homocitrullinated proteins in biological samples. Its utility is demonstrated through its application in mouse tissue-specific citrullination and homocitrullination analysis. We further demonstrate the combination of the biotin tag-assisted MS-based method with different quantitative techniques, enabling the simultaneously qualitative and quantitative analysis of citrullinated and homocitrullinated proteins from different biological samples for the first time. Meanwhile, quantitative proteomics and phosphoproteomics was performed to reveal the signaling pathways involved in the macrophages treated by lipopolysaccharides (LPS) and thapsigargin (TPG).This dissertation also highlights two projects focusing on in-situ imaging of biomolecules from tissue sections using MALDI MS imaging (MSI). MALDI MSI of mouse arteries undergoing restenosis revealed the involvement of many bioactive lipids in the progress of restenosis. In addition, a novel subatmospheric pressure ionization source has been coupled with MS for the high-resolution imaging of N-glycans from formalin-fixed paraffin-embedded (FFPE) tissue sections. Application of this new SubAP/MALDI MS platform to FFPE mouse ovarian cancer tissue section unraveled the specific distribution of high-mannose N-glycans in the tumor region, suggesting potential association of this type of N-glycans with tumor progression.
Publisher
ProQuest Dissertations & Theses
Subject
ISBN
9798802713136
