Phospholipases A2 in ras-transformed and immortalized human mammary epithelial cells.

Phospholipase A2 (PLA2) activities of non-tumorigenic and tumorigenic human mammary epithelial cells, 184B5 cells (immortalized cell line from a reduction mammoplasty) and B5KTu cells (cells from a tumor induced by ras-transformed 184B5 cells), are characterized, with emphasis on lipid biomediator-related phospholipases A2. Phospholipases A2 associated with regulation of arachidonic acid metabolism include the high molecular mass cytosolic PLA2 (cPLA2) and group II PLA2. The major PLA2 activity in the mammary epithelial cells has the characteristics of cPLA2; this activity is higher in the B5KTu cells. In contrast, the 184B5 and B5KTu cells have similar levels of a Ca(2+)-independent, cytosolic PLA2 activity and low levels of a particulate fraction PLA2 activity, which does not have the properties of group II PLA2. Thus, cPLA2 activity is selectively elevated in the tumorigenic human mammary epithelial cells and this may result in increased generation of lipid biomediators such as arachidonic acid metabolites.