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

Pagel O, Loroch S, Sickmann A, Zahedi RP - Expert Rev Proteomics (2015)

Bottom Line: 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.

View Article: PubMed Central - PubMed

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

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.

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Frequently reported post-translational protein modifications.
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Figure 0001: Frequently reported post-translational protein modifications.

Mentions: Biological systems maintain homeostasis by dynamic adaptation to the rapidly changing environment. While transcription, translation (and degradation) affect protein abundance, protein activity and function are mainly defined by structure (Figure 1). The latter can be regulated by post-translational modifications (PTMs), allowing rapid response to external/internal stimuli within (milli-)seconds.


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

Pagel O, Loroch S, Sickmann A, Zahedi RP - Expert Rev Proteomics (2015)

Frequently reported post-translational protein modifications.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4487610&req=5

Figure 0001: Frequently reported post-translational protein modifications.
Mentions: Biological systems maintain homeostasis by dynamic adaptation to the rapidly changing environment. While transcription, translation (and degradation) affect protein abundance, protein activity and function are mainly defined by structure (Figure 1). The latter can be regulated by post-translational modifications (PTMs), allowing rapid response to external/internal stimuli within (milli-)seconds.

Bottom Line: 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.

View Article: PubMed Central - PubMed

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

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.

Show MeSH