TABLE 3.
Glycosylation of hydroxylysine residues estimated by mass spectrometry of non-cross-linked, glycosylated peptides
Hyl + G-Hyl + GG-Hyl = 100%.
| Site occupancy |
||||
|---|---|---|---|---|
| WT | Het | KO | ||
| % | % | % | ||
| α1(I) Lys-87 | Hyl | 73.5 ± 2.4 | 71.0 ± 1.9 | 63.6 ± 2.2a,b |
| G-Hyl | 5.4 ± 1.1 | 6.5 ± 0.9 | 6.6 ± 0.5 | |
| GG-Hyl | 21.1 ± 1.3 | 22.5 ± 1.2 | 29.8 ± 2.6a,b | |
| α1(I) Lys-174 | Hyl | 91.3 ± 0.1 | 91.7 ± 0.6 | 82.9 ± 1.2a,b |
| G-Hyl | 4.8 ± 0.1 | 4.6 ± 0.6 | 10.8 ± 0.7a,b | |
| GG-Hyl | 3.9 ± 0.2 | 3.7 ± 0.2 | 6.3 ± 0.5a,b | |
| α2(I) Lys-174 | Hyl | 94.9 ± 1.7 | 96.4 ± 0.8 | 82.6 ± 2.0a,b |
| G-Hyl | 4.7 ± 1.7 | 2.9 ± 0.5 | 9.7 ± 1.6a,b | |
| GG-Hyl | 0.4 ± 0.1 | 0.6 ± 0.4 | 7.7 ± 3.5 | |
| α2(I) Lys-219 | Hyl | 97.4 ± 0.2 | 98.0 ± 0.1 | 93.9 ± 1.0a,b |
| G-Hyl | 1.3 ± 0.4 | 0.9 ± 0.1 | 2.7 ± 0.4a,b | |
| GG-Hyl | 1.3 ± 0.2 | 1.1 ± 0.0 | 3.3 ± 0.7a,b | |
a p < 0.05 between WT and KO.
b p < 0.05 between Het and KO.