Induction of prostaglandin endoperoxide synthase-1 (COX-1) in a human promonocytic cell line by treatment with the differentiating agent TPA.

Smith CJ, Morrow JD, Roberts LJ, Marnett LJ
Adv Exp Med Biol. 1997 400A: 99-106

PMID: 9547543 · DOI:10.1007/978-1-4615-5325-0_14

Prostaglandin endoperoxide synthase (PGH synthase) is responsible for converting arachdonic acid to PGH2, the common precursor of prostaglandins. It has been shown previously that phorbol ester-induced differentiation of human promonocytic leukemia cell lines is accompanied by induction of PGH synthase enzyme and enhanced capacity to produce prostaglandins. However, the identity of the isoform of PGH synthase, i.e., PGH synthase-1 or -2, that is induced under these conditions has not been established. Northern and Western analyses revealed a dramatic increase in levels of PGH synthase-1 mRNA and protein levels within 24 hr after treatment of THP-1 cells with phorbol ester. No significant increase in PGH synthase-2 mRNA or protein was observed. The increases in PGH synthase-1 were accompanied by an enhanced capacity of the cells to produce PGE2. The current findings indicate that expression of PGH synthase-1 is greatly enhanced in a promonocytic cell line by treatment with an agent that induces differentiation.

MeSH Terms (18)

Calcium Cell Differentiation Cyclooxygenase 1 Cyclooxygenase 2 Dexamethasone Dinoprostone Enzyme Induction Humans Isoenzymes Magnesium Membrane Proteins Monocytes Prostaglandin-Endoperoxide Synthases Protein Biosynthesis RNA, Messenger Tetradecanoylphorbol Acetate Transcription, Genetic Tumor Cells, Cultured

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