Characterization of dermal type I collagen of C3H mouse at different stages of the hair cycle.

Abstract

Hair follicles develop or regress in accordance with the hair cycle. In this study, we partially characterized fibrillar type I collagen, the predominant component in the dermis, at two stages of the hair cycle: anagen and telogen. Skin samples were obtained from the backs of two groups of 11-week-old C3H mice: one at anagen stage induced by shaving and the other at telogen stage. The amount of neutral salt-soluble (newly synthesized) collagen obtained from anagen skin was about twofold that from telogen skin, while the level of acid-soluble collagen was not significantly different between the two groups. The degree of lysine hydroxylation of pepsinized type I collagen obtained from anagen skin was significantly higher than that in telogen (5.0% higher in alpha1 chain, and 15.6% higher in alpha2 chain). Proline hydroxylation at the anagen stage was also slightly higher than in the telogen stage. Two major collagen cross-links were found in both groups of skin; dehydro-hydroxylysinonorleucine and dehydro-histidinohydroxymerodesmosine. The concentration of the latter, a complex tetravalent cross-link, was significantly lower in anagen skin when compared with telogen skin (mean +/- SD 0.64 +/- 0. 07 vs. 0.78 +/- 0.06 mol/mol collagen). The former showed no significant difference between the two groups. In addition, a significant amount of lysyl-aldehyde (a cross-link precursor) was found in anagen (0.16 +/- 0.02 mol/mol collagen), while it was 0.12 mol/mol collagen in telogen. These results indicate that the remodelling of collagen is more active in anagen skin than in telogen, and that characteristic post-translational modifications of dermal collagen seen in anagen may play a part in facilitating an environment around hair follicles for their migration and growth.