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J. Biol. Chem., Vol. 277, Issue 17, 14829-14837, April 26, 2002
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From the 12-O-Tetradecanoylphorbol-13-acetate
(TPA) suppresses the proliferation of the human breast epithelial cell
line MCF10A-Neo by initiating proteolytic processes that activate
latent transforming growth factor (TGF)- Institute of Environmental Health Sciences,
Wayne State University and the § Department of Pharmacology,
Wayne State University School of Medicine,
Detroit, Michigan 48201
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 -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- antibody. Pretreatment 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-.
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