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Papers In Press, published online ahead of print January 28, 2002
J. Biol. Chem, 10.1074/jbc.M108180200
Submitted on August 24, 2001
Revised on January 23, 2002
Accepted on January 28, 2002

Phorbol ester activation of a proteolytic cascade capable of activating latent TGF-beta : A process initiated by the exocytosis of cathepsin B

Meng Guo, Patricia A. Mathieu, Bruce Linebaugh, Bonnie F. Sloane, and John J. Reiners Jr.

Institute Environmental Health Sciences, Wayne State University, Detroit, MI 48201

Corresponding Author: john.reiners.jr{at}wayne.edu

12-0-tetradecanoylphorbol-13-acetate (TPA) suppresses the proliferation of the human breast epithelial cell line MCF10A-Neo by initiating proteolytic processes that activate latent TGF-beta in the serum used to supplement culture medium. Within 1 h of treatment cultures accumulated an extracellular activity capable of cleaving a substrate for urokinase-type plasminogen activator (uPA) and tissue plasminogen activator (tPA). This activity was inhibited by plasminogen activator inhibitor-1 or antibodies to uPA, but not tPA. Pro-uPA activation was preceded by dramatic changes in lysosome trafficking and the extracellular appearance of cathepsin B and beta -hexosaminidase, but not cathepsins D or L. Co-treatment of cultures with the cathepsin B inhibitors CA-074 or Z-FA-FMK suppressed the cytostatic effects of TPA and activation of pro-uPA. In the absence of TPA, exogenously added cathepsin B activated pro-uPA and suppressed MCF10A-Neo proliferation. The cytostatic effects of both TPA and cathepsin B were suppressed in cells cultured in medium depleted of plasminogen/plasmin or supplemented with neutralizing TGF-beta antibody. Pre-treatment with cycloheximide did not suppress the exocytosis of cathepsin B or the activation of pro-uPA. Hence, TPA activates signaling processes that trigger the exocytosis of a subpopulation of lysosomes/endosomes containing cathepsin B. Subsequently, extracellular cathepsin B initiates a proteolytic cascade involving uPA, plasminogen, and plasmin that activates serum-derived latent TGF-beta .


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