2009 Volume 55 Issue 3 Pages 468-472
Transforming growth factor-β (TGF-β) is a potent growth factor that contributes to wound healing. TGF-β is usually secreted in a latent form complexed with its propeptide, latency-associated peptide (LAP), and LAP covalently binds to a molecule of latent TGF-β binding protein (LTBP). Fibrillin-1 sequesters TGF-β within connective tissue microfibrils through interaction with LTBP-1. However, it is not clear whether TGF-β bound to LTBP-1 is available during wound healing. Therefore, we further characterized LTBP-1, the extracellular regulator of TGF-β in wound healing. LTBP-1 fragments were released from skin by plasmin treatment. The LTBP-1 fragment that is similar to plasmin treatment was also detected in a wound surface. The enzymatic activity of plasmin was also detected in wound surfaces. Immunoblotting analyses showed that the LTBP-1 fragment was preferentially detected in a wound surface with proliferating granulation tissues. These results suggest that proteolytic release of LTBP-1 from a wound surface is physiological and important in regulating wound healing.
