Redox-Mediated Activation of Latent Transforming Growth Factor-p1

The efficiency of ascorbate activation de-pended on ascorbate concentration and the presence of transition metal ions. We postulate that oxidation of specific amino acids in the latency-conferring peptide leads to a conformation change in the latent complex that allows release of TGFP. Oxidative activation offers a novel route for the involvement of TGF6 in tissue processes in which ROS are implicated and endows LTGFP with the ability to act as a sensor of oxidative stress and, by releasing TGF6, to function as a signal for orches-trating the response of multiple cell types. LTGFP redox sensitivity is presumably directed toward recovery of homeostasis; however, oxidation may also be a mechanism of LTGFP activation that can be deleterious during disease mechanisms involv-0888-8809/96/53.00/O