Abstract
The effects of 20 μg/ml exogenous arachidonic acid (AA) and prostaglandin A2 (PGA2) were evaluated on total tyrosine kinase (TK) activity and tyrosine phosphorylation status in HeLa and MCF-7 cells. AA and PGA2 increased TK activity in both HeLa and MCF-7 cells. Western blotting employing an anti-phosphotyrosine antibody showed only one protein of approximately 55 kDa (∼55 kDa) to be phosphorylated in the MCF-7 cells, while a variety of proteins were phosphorylated in the HeLa cells, including the ∼55 kDa protein. Amino acid analyses as well as Matrix Assisted Laser Desorption Ionization were conducted on this protein from different cell lines and it was shown to be similar. Comparison to p53 did not show similarities. The identity of this protein needs to be further characterized to help elucidate the signal transduction pathways of AA and PGA2.
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