Catecholestrogen synthesis and metabolism by human breast tumors in vitro

Andrew R. Hoffman, Steven M. Paul, Julius Axelrod

Research output: Contribution to journalArticlepeer-review

69 Scopus citations

Abstract

The activities of enzymes which synthesize and metabolize catechoiestrogens were studied in biopsy samples of human breast neoplasms. Estrogen 2-hydroxylase, a cytochrome P-450-dependent enzyme, was present in both benign and malignant neoplasms but not in normal breast tissue. Catechol O-methyltransferase activity was present in all samples examined and was significantly higher in malignant tumors [549 ± 31 (S.E.) pmol/20 min/mg protein] than in benign neoplasms (226 ± 41 pmol/20 min/mg protein) or in normal breast tissue (133 ± 28 pmol/20 min/mg protein). There was no correlation, however, between estrogen 2-hydroxylase and catechol O-methyltransferase activities. The enzymes responsible for the synthesis and metabolism of catechoiestrogens are present in some breast tumor specimens, suggesting that in such tissues these metabolites may be formed in vivo.

Original languageEnglish
Pages (from-to)4584-4587
Number of pages4
JournalCancer research
Volume39
Issue number11
StatePublished - Nov 1 1979

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