Structural changes in the glycosaminoglycan chain of rat skin decorin with growth.

Abstract

Decorin controls collagen fibrilogenesis in skin, and its molecular weight changes in wound healing and with age. In this report, the quantitative and structural changes of decorin were investigated with growth in rat skin from the fetus to the young adult. A northern blot analysis showed that the highest level of skin decorin mRNA was at post partus 0.5 days; this level was about 3.7 times the level at embryo 16.5 days. The mRNA level in the rat skin decreased by 1/5 from post partus 0.5 days until 90 days of age. Western blotting showed that the amount of decorin increased with age in protein level. The molecule size of decorin at embryo 18.5 days was about 110 kDa, and that at post partus 90 days was about 70 kDa. There were no changes in molecular size of its core protein, so the reduction in the size of decorin was dependent on the size of the glycosaminoglycan (GAG) as shown by western blot analyses. Electron micrography of the rat skin with cupromeronic blue staining showed that the length of GAG at embryo 18.5 days was about 78.58 +/- 13.94 nm, and that at post partus 90 days was about 54.05 +/- 4.79 nm. The reduction in length of decorin GAG with age shrunk the distance between the collagen fibrils. We suggested that decorin changes the GAG length in order to control skin reconstruction in response to inflammation and injury.