Cell-cell and cell-collagen interactions influence gelatinase production by human breast-carcinoma cell line 8701-BC

✍ Scribed by Salvatore Minafra; Carola Giambelluca; Maria Andriolo; Ida Pucci-Minafra

• Publisher: John Wiley and Sons
• Year: 1995
• Tongue: French
• Weight: 884 KB
• Volume: 62
• Category: Article
• ISSN: 0020-7136
• DOI: 10.1002/ijc.2910620622

✦ Synopsis

We previously produced evidence that the human mammarycarcinoma cell line 870 I -BC expresses several metalloproteinases (MMP-I, -2, -9, and -10) and their tissue inhibitors). In order to obtain a better understanding of the environmental control over gelatinolytic activities, we have tested the enzyme production of 8701-BC cells, at time intervals after plating on different collagen substrates, i.e., types I, 111, IV, V and OF/LB, used as films in culture dishes. Proteinase activities, released in the conditioned culture media, were tested by zymography on SDS-PAGE, and by quantificative analyses, using I4C carboxymethylated transferrin as substrate in a liquid incubation medium. Enzymatic activities varied with time and were inversely related to cell densities, with minimum values at cell confluence. The enzymatic activity was positively supported by collagen substrates, with a maximal increase in activity when OFAB collagen was used. In addition to the known MMPs, we found a proteinase with an M, of about 20 kDa, which displayed higher activity at 48 hr after cell plating and gradually decreased with cell increment. In contrast to the other MMPs, this proteinase is inhibited by soybean trypsin inhibitor, but it does not display a complete identity with trypsin, since it does not digest casein and is not inhibited by other serine proteinase inhibitors.