Species specificity of estrogen biosynthesis in pregnancy. Immunochemical difference of placental NADPH-cytochrome c (P-450) reductase in human, baboon and horse.
Abstract: NADPH-cytochrome c (P-450) reductases from human placental aromatase II and from horse placental microsomes were solubilized and purified to show a single band of 83,000 daltons in SDS-polyacrylamide gel electrophoresis. Rabbits were immunized with purified human placental aromatase II NADPHcytochrome c (P-450) reductase. The resulting antibodies (Reduc-Ab) were used to examine the species specificity of estrogen biosynthesis and the reductase activity in humans, baboons, horses and rats. Rcduc-Ab suppressed androstenedione aromatase activity in human, baboon and horse placental microsomes with sensitivities in the order of human ⪢ baboon ⪢ horse. Reduc-Ab was much less effective in inhibiting baboon and horse placental NADPH-cytochrome c reductase activity. On the other hand, rat liver microsomal NADPH-cytochrome c reductase activity and its purified preparation were effectively suppressed by Reduc-Ab and the sensitivity was much closer to that of human than to horse. The results suggest that there are common antigenic structure(s) in human, baboon and horse placental and rat liver NADPH-cytochrome c (P-450) reductases and also that there are distinct structural portions or multiple forms of NADPH-cytochrome c reductase among different species.
Publication Date: 1981-12-01 PubMed ID: 6175794DOI: 10.1016/0022-4731(81)90313-7Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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This study investigates the species-specific nature of estrogen biosynthesis during pregnancy, focusing on the immunochemical difference of placental NADPH-cytochrome c (P-450) reductase in humans, baboons, and horses.
Research Methodology
- The researchers extracted and refined NADPH-cytochrome c (P-450) reductases from human and horse placentas. This protein demonstrates a mass of 83,000 daltons as evidenced in SDS-polyacrylamide gel electrophoresis.
- Rabbits were then immunized with the purified human placental enzyme. The antibodies produced by the rabbits (named Reduc-Ab) were earmarked for subsequent stages of the study.
Investigation of Species Specificity
- The next stage of the study concerned itself with the investigation of the species-specific nature of estrogen biosynthesis and the reductase activity across humans, baboons, horses and rats.
- The antibodies (Reduc-Ab) were found to suppress androstenedione aromatase activity in human, baboon, and horse placental microsomes, with varying degrees of sensitivity.
- The antibodies were much less effective in inhibiting the reductase activity in baboon and horse placental microsomes compared to the human placenta.
Results with Rat Liver Microsomes
- Interestingly, the Reduc-Ab antibodies proved quite efficient at suppressing NADPH-cytochrome c reductase activity in rat liver microsomes, as well as in a purified preparation.
- The sensitivity of the response in rat liver microsomes was much more comparable to that in humans than it was to that in horses.
Interpretation of Results
- The results of the study imply that there are some shared antigenic structures in the NADPH-cytochrome c (P-450) reductase enzymes of humans, baboons, horses, and rat livers.
- However, there is also evidence suggesting the existence of unique structural components or multiple forms of NADPH-cytochrome c reductase specific to different species.
Conclusion
- This study provides critical insight into the workings of estrogen biosynthesis during pregnancy, offering a profound understanding of species-specific variations in the underlying biochemical pathways, including those involving the enzyme NADPH-cytochrome c (P-450) reductase.
Cite This Article
APA
Osawa Y, Higashiyama T, Nakamura T.
(1981).
Species specificity of estrogen biosynthesis in pregnancy. Immunochemical difference of placental NADPH-cytochrome c (P-450) reductase in human, baboon and horse.
J Steroid Biochem, 15, 449-452.
https://doi.org/10.1016/0022-4731(81)90313-7 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Epitopes
- Estrogens / biosynthesis
- Female
- Horses
- Humans
- Immunochemistry
- NADPH-Ferrihemoprotein Reductase / immunology
- NADPH-Ferrihemoprotein Reductase / metabolism
- Papio
- Placenta / metabolism
- Pregnancy
- Species Specificity
Grant Funding
- HD04945 / NICHD NIH HHS
Citations
This article has been cited 1 times.- Kurosumi M, Ishimura K, Fujita H, Osawa Y. Immunocytochemical localization of aromatase in rat testis. Histochemistry 1985;83(5):401-4.
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