MAGP-2 can also interact with αvβ3 integrins via a RGD sequence that is not found in MAGP-1.
Furthermore, a decline in MAGP-1 expression with age was observed both at the gene level and at the protein level.
This suggests that declines in MAGP-1 may contribute to the disruption in the structural integrity of follicular regions in aged skin.
In the aged group, a significant reduction in the MAGP-1 level in both the reticular dermis as well as in areas surrounding the hair follicles was observed.
However, in photoexposed skin, a change in the MAGP-1 staining pattern was observed early in life.
In photoprotected skin (similar to the gene array data), a significant decline in the MAGP-1 protein was observed in aged skin (from the 57 79-year-old group) compared to the young skin (from the 18–21-year-old group).
After repetitive low-dose UV exposure, a significant reduction in the MAGP-1 level was observed.
A significant reduction in the MAGP-1 protein level was observed, as quantified by ImageJ (P<0.05).
Next, we observed the in vivo change of MAGP-1 in human skin.
A mature mycolic acid is eventually transferred either to arabinogalactan (to form mAGP) in part by the Ag85 proteins, or to an α,α-trehalose-6-phosphate (T6P, leading to TMM) by an unknown mycolyltransferase [9].
Long-term photoaging appears to result in the progression of MAGP-1 loss in the follicular regions and in the reticular dermis, which may lead to fragility and instability of the dermal matrix, and contribute to the various signs of an aged appearance such as wrinkles, sagging, loss of elasticity and bounciness, and enlarged pores.
