TY - JOUR
T1 - Characterizing disease-associated changes in post-translational modifications by mass spectrometry
AU - Thygesen, Camilla
AU - Boll, Inga
AU - Finsen, Bente
AU - Modzel, Maciej
AU - Larsen, Martin R.
PY - 2018/3
Y1 - 2018/3
N2 - Introduction: Exploring post-translational modifications (PTMs) with the use of mass spectrometry (PTMomics) is a rapidly developing area, with methods for discovery/quantification being developed and advanced on a regular basis. PTMs are highly important for the regulation of protein function, interaction and activity, both in physiological and disease states. Changes in PTMs can either cause, or be the result of a disease, making them central for biomarker studies and studies of disease pathogenesis. Recently, it became possible to study multiple PTMs simultaneously from low amount of sample material, thereby increasing coverage of the PTMome obtainable from a single sample. Thus, quantitative PTMomics holds great potential to discover biomarkers from tissue and body fluids as well as elucidating disease mechanisms through characterization of signaling pathways. Areas covered: Recent mass spectrometry-based methods for assessment of the PTMome, with focus on the most studied PTMs, are highlighted. Furthermore, both data dependent and data independent acquisition methods are evaluated. Finally, current challenges in the field are discussed. Expert commentary: PTMomics holds great potential for clinical and biomedical research, especially with the generation of spectral libraries of peptides and PTMs from individual patients (permanent PTM maps) for use in personalized medicine.
AB - Introduction: Exploring post-translational modifications (PTMs) with the use of mass spectrometry (PTMomics) is a rapidly developing area, with methods for discovery/quantification being developed and advanced on a regular basis. PTMs are highly important for the regulation of protein function, interaction and activity, both in physiological and disease states. Changes in PTMs can either cause, or be the result of a disease, making them central for biomarker studies and studies of disease pathogenesis. Recently, it became possible to study multiple PTMs simultaneously from low amount of sample material, thereby increasing coverage of the PTMome obtainable from a single sample. Thus, quantitative PTMomics holds great potential to discover biomarkers from tissue and body fluids as well as elucidating disease mechanisms through characterization of signaling pathways. Areas covered: Recent mass spectrometry-based methods for assessment of the PTMome, with focus on the most studied PTMs, are highlighted. Furthermore, both data dependent and data independent acquisition methods are evaluated. Finally, current challenges in the field are discussed. Expert commentary: PTMomics holds great potential for clinical and biomedical research, especially with the generation of spectral libraries of peptides and PTMs from individual patients (permanent PTM maps) for use in personalized medicine.
KW - clinical proteomics
KW - DDA strategies
KW - DIA strategies
KW - enrichment strategies
KW - mass spectrometry
KW - Post-translational modification
KW - Biomarkers/chemistry
KW - Humans
KW - Proteome/chemistry
KW - Animals
KW - Mass Spectrometry/methods
KW - Proteomics/methods
KW - Protein Processing, Post-Translational
U2 - 10.1080/14789450.2018.1433036
DO - 10.1080/14789450.2018.1433036
M3 - Journal article
C2 - 29376447
AN - SCOPUS:85043538535
VL - 15
SP - 245
EP - 258
JO - Expert Review of Proteomics
JF - Expert Review of Proteomics
SN - 1478-9450
IS - 3
ER -