Premium
Malate dependent synthesis of progesterone in the mitochondrial fraction of human term placenta
Author(s) -
Boguslawski W.,
Klimek J.,
Z̀elewski L.
Publication year - 1972
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(72)80437-x
Subject(s) - medical school , chemistry , library science , medicine , computer science , medical education
Ryan and co-workers[ l] demonstrated the important role of the placental cholesterol side-chain cleavage enzyme system in progesterone production. Mitochondria of human placenta contain an oxidative chain associated with cytochrome P-450 for the cleavage of the cholesterol side chain in the biosynthesis of pregnenolone. This system uses NADPH as the reducing source [2]. Mason and Boyd [3] recently confirmed that an NADPH generating system is essential for progesterone biosynthesis in mitochondria of human term placenta. Therefore, it seemed of interest to look for a stimulation of progesterone biosynthesis by malate; this might be due to the malic enzyme activity in the mitochondria, which would result in the generation of NADPH -a cofactor essential for the conversion of cholesterol to pregnenolone. The experimental results presented here provide evidence for a stimulatory effect of malate on biosynthesis of progesterone from cholesterol by placental mitochondrial fraction.