Investigation of post-translational modifications in type 2 diabetes

Table 1 Post-translational modifications compatible to high throughput mass spectrometry based proteomics analysis in diabetes

Post-translational modifications	ΔMass^a (monoisotopic mass) in Da	Largest MS dataset^b sites/peptides	Organisms	Enrichment mode
Phosphorylation	79.96633 [129]	12,294 sites [76]	Rat hepatocytes	TiO₂ beads
Acetylation	42.01056 [129]	1604 sites [123]	Mouse liver	Polyclonal acetyl-lysine K(ac) antibody
O-GlcNAcylation	203.07937 [129]	1750 sites [99]	Synaptosome (mouse)	Lectin wheat germ agglutinin column
N-Glycosylation	HexNAcoxonium ions (138.0545 and 204.0867), deamidation of asparagine and glutamine (0.9848)	951 unique deamidation sites, 1580 unique N-glycopeptides [90]	3T3-L1 adipocytes/fibroblasts (mouse)	zic-HILIC SPE column, PNGase F
Advanced glycation end products	Amadori compound modification at lysine (162.0528 Da)	7749 unique glycated peptides [124]	Diabetes human plasma and erythrocytes	Boronate affinity chromatography

Largest post-translational modified sites detected using mass spectrometry from different sources by different enrichment methods
MS mass spectrometry
^aReference for ΔMass
^bReference to the largest proteomics dataset for each post-translational modifications

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