MCF-7 mammary tumour cells express the myeloid cell differentiation controlling factor, serine protease 3/myeloblastin.

Our previous data indicated that HSP27 plays a role in MCF-7 cell differentiation similar to that it has in HL-60 cells. In the latter case, this involves a control of its levels by proteinase 3/myeloblastin (PR3/Mbn), a serine proteinase hitherto considered specific of the myeloid lineage. Having observed that the treatment of MCF-7 cells with the serine protease inhibitor N-tosyl-l-phenylalanine-chloromethyl ketone (TPCK) increased their content in HSP27 and induced them to acquire a secretory phenotype, we undertook this work to test the assumption that an enzyme similar or identical to PR3/Mbn might be expressed in this cell line. The data show that MCF-7 cells exhibited specific immunopositivity for a monoclonal antibody against PR3/Mbn. Western blot analysis of immunoprecipitates from MCF-7 cell extracts, obtained and checked with PR3/Mbn monoclonal antibodies, confirmed the presence of the 35 kDa glycosylated and 29 kDa mature forms of the protein. Finally, Northern blot analysis confirmed the expression of the corresponding mRNA. Together with our data with TPCK, this substantiates our hypothesis that, as in HL-60 cells, regulation of MCF-7 cells differentiation might involve a postranslation control on HSP27 levels by a serine protease.