Table 4 Glycosylation of hydroxylysine residues estimated by mass spectrometry of non-cross-linked glycosylated residues.
From: Lysyl hydroxylase 2 mediated collagen post-translational modifications and functional outcomes
| Â | Â | Site occupancy (%) | ||||
|---|---|---|---|---|---|---|
MC | EV | KO-1 | KO-2 | KO-3 | ||
α1(I) K87 | Hyl | 4.0 ± 0.2 | 3.3 ± 0.1 | 13.0 ± 0.3***,### | 12.6 ± 0.2***,### | 5.3 ± 0.1***,### |
Glycosylated-Hyl | 96.0 ± 0.2 | 96.7 ± 0.1 | 87.0 ± 0.3***,### | 87.4 ± 0.2***,### | 94.7 ± 0.1**,### | |
α1(I) K99 | Hyl | 65.3 ± 0.5 | 67.0 ± 0.6 | 74.5 ± 0.2***,### | 73.5 ± 0.6***,### | 76.5 ± 0.1***,### |
Glycosylated-Hyl | 34.7 ± 0.5 | 33.0 ± 0.6 | 25.5 ± 0.2***,### | 26.5 ± 0.6***,### | 23.5 ± 0.1***,### | |
α1(I) K174 | Hyl | 88.3 ± 1.0 | 89.7 ± 0.4 | 92.7 ± 0.5***,### | 92.2 ± 0.2***,### | 91.0 ± 0.2*** |
Glycosylated-Hyl | 11.7 ± 1.0 | 10.3 ± 0.4 | 7.3 ± 0.5***,### | 7.8 ± 0.2***,### | 9.0 ± 0.2*** | |
α1(I) K564 | Hyl | 72.3 ± 0.9 | 75.2 ± 0.2 | 84.3 ± 0.3***,### | 83.8 ± 0.5***,### | 84.2 ± 0.2***,### |
Glycosylated-Hyl | 27.7 ± 0.9 | 24.8 ± 0.2 | 15.7 ± 0.3***,### | 16.2 ± 0.5***,### | 15.8 ± 0.2***,### | |
α2(I) K174 | Hyl | 9.7 ± 0.5 | 9.2 ± 0.7 | 15.6 ± 0.8***,### | 16.0 ± 1.1***,### | 7.7 ± 0.1* |
Glycosylated-Hyl | 90.3 ± 0.5 | 90.8 ± 0.7 | 84.4 ± 0.8***,### | 84.0 ± 1.1***,### | 92.3 ± 0.1* | |
α2(I) K219 | Hyl | 94.3 ± 1.3 | 94.4 ± 0.8 | 96.8 ± 0.2**,## | 96.9 ± 0.5**,## | 94.9 ± 0.2 |
Glycosylated-Hyl | 5.7 ± 1.3 | 5.6 ± 0.8 | 3.2 ± 0.2**,## | 3.1 ± 0.5**,## | 5.1 ± 0.2 | |