@article{oai:stella.repo.nii.ac.jp:00000438,
 author = {Mizuno, Koji and Wachi, Hiroshi and Isogai, Zenzo and Yoneda, Masahiko and Fujii, Satoshi and Watanabe, Ken and Seyama, Yoshiyuki},
 issue = {3},
 journal = {Journal of Health Science},
 month = {},
 note = {application/pdf, 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.},
 pages = {468--472},
 title = {Proteolytic Release of Latent Transforming Growth Factor-.BETA. (TGF-.BETA.) Binding Protein-1 (LTBP-1) Fragment in Wound Healing},
 volume = {55},
 year = {2009}
}