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Characterization of phospholipase A2 activity in MDA-MB-435 human breast cancer cells
M A Hatala1, J Rayburn, D P Rose
1Division of Nutrition and Endocrinology, American Health Foundation, Valhalla, New York 10595.
Abstract:
Phospholipase A2 (PLA2) was identified and its properties characterized in MDA-MB-435 cells, a human breast cancer cell line. Cytosolic fractions, prepared in calcium-free buffer, were assayed using arachidonyl-containing phosphatidylcholine as substrate. PLA2 activity was linear as a function of both time and protein concentration. The enzyme was shown to be calcium-dependent and to require a basic pH of 9.5-10.0 for optimal activity. Activity was predominantly found in the cytosolic fraction when cells were harvested in calcium-free buffer. Phospholipase A2 may play a key role in linoleic acid-enhanced mammary tumorigenesis and metastasis.