Table 1.

Collagen cross-link and mass spectral analysis to investigate the hydroxylation levels (A) of lysine and proline in type 1 collagen (n = 1 for patellar and n = 2 for Achilles tendon) and the collagen cross-linking levels (B) (* indicates P < 0.05 between genotypes, n = 1 for patellar and n = 3 for Achilles tendon) from wild-type mice and Scx-Cre; Rcn3^fl/fl (tendon-specific Rcn3 loss-of-function model) littermates at P30.

A
Hydroxylation analysis	Patellar tendon (n = 1) (%)		Achilles tendon (n = 2) (%)
Site	WT	Scx-Cre; Rcn3fl/fl	WT	Scx-Cre; Rcn3fl/fl
Hydroxylysine
α1(I)K87	100	100	100	100
			100	100
α2(I)K87	100	100	100	100
			100	100
α1(I) C-telo Hyl	45	65	33	53
			44	42
3-Hydroxyproline
α1(I)P986	92	96	93	93
			91	95
α1(I)P707	60	80	50	76
			50	65
α2(I)P707	45	65	79	85
			74	88

B
Cross-linking analysis	Patellar tendon (n = 1)		Achilles tendon (n = 3)
Site	WT	Scx-Cre; Rcn3fl/fl	WT	Scx-Cre; Rcn3fl/fl
Hydroxylysylpyridinoline (mol/mol)	0.25	0.56	0.07	0.11 *
			0.07	0.21
			0.075	0.19