PMID: 6539716May 1, 1984Paper

The estrogen-regulated 52 K protein adn plasminogen activators released by MCF7 cells are different

Molecular and Cellular Endocrinology
O MassotH Rochefort

Abstract

In the MCF7 human breast cancer cell line, estradiol stimulates the synthesis of a 52 K secretory glycoprotein and has been reported to increase the plasminogen activator (PA) activity in the culture medium. Since one PA isozyme has a molecular weight close to 52 000 daltons under denaturing conditions, we asked whether the 52 K protein was a PA. The PA activity released in serum-free conditioned medium was evaluated by the increase in [125I]casein digestion observed in the presence of plasminogen. The 52 K protein was estimated by analysing the released proteins on SDS-polyacrylamide gel electrophoresis. When the conditioned medium was chromatographed on concanavalin A-Sepharose, the 52 K protein was retained on the gel, but not the PA. The two proteins also appeared different on the basis of their competing efficiency in a radioimmunoassay developed to quantify the 52 K protein. An antiserum against human urokinase failed to immunoprecipitate the 52 K protein. Under our culture conditions estradiol increased 52 K, but not PA, production. These results clearly indicate that the estradiol-regulated 52 K protein is not a plasminogen activator.

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Citations

Jan 1, 1986·Annals of the New York Academy of Sciences·H RochefortF Vignon
Jul 16, 1986·Biochemical and Biophysical Research Communications·M MorissetH Rochefort

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