Ultracytochemical localization of 3?-hydroxy-steroid ferricyanide reductase activity in the fetal mouse ovary

1980 ◽  
Vol 3 (4) ◽  
pp. 323-328 ◽  
Author(s):  
Masamichi Hiura ◽  
Georgiana Jagiello ◽  
James Dennis ◽  
Mercedes Ducayen
Keyword(s):  
Reductase Activity ◽  
Mouse Ovary ◽  
Fetal Mouse ◽  
Ferricyanide Reductase ◽  
Hydroxy Steroid

Etoposide results in follicle loss in the fetal mouse ovary, but does not block the ability of oocytes to progress through prophase I of meiosis

2016 ◽  
Author(s):  
Agnes Stefansdottir ◽  
Zoe Johnston ◽  
Nicola Powles-Glover ◽  
Richard Anderson ◽  
Ian Adams ◽  
...  
Keyword(s):  
Mouse Ovary ◽  
Fetal Mouse ◽  
Prophase I

scholarly journals Different mechanisms of regulation of nuclear reduced nicotinamide–adenine dinucleotide phosphate-dependent 3-oxo steroid 5α-reductase activity in rat liver, kidney and prostate

1974 ◽  
Vol 142 (2) ◽  
pp. 273-277 ◽  
Author(s):  
Jan-Åke Gustafsson ◽  
Åke Pousette
Keyword(s):  
Testosterone Propionate ◽  
Reductase Activity ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Female Rats ◽  
Male Rats ◽  
Regulatory Mechanisms ◽  
Oestradiol Benzoate ◽  
Liver And Kidney ◽  
Reduced Nicotinamide Adenine Dinucleotide ◽  
Hydroxy Steroid

The regulatory mechanisms involved in the control of the nuclear NADPH-dependent 3-ketosteroid 5α-reductase (5α-reductase) activity were studied in liver, kidney and prostate. The substrate used was [1,2-3H]androst-4-ene-3,17-dione (androstenedione) (for liver and kidney) or [4-14C]androstenedione (for prostate). The hepatic nuclear 5α-reductase activity was greater in female than in male rats, was greater in adult than in prepubertal female rats, increased after castration of male rats, but was not affected by treatment with testosterone propionate or oestradiol benzoate. These regulatory characteristics are in part different from those previously described for the hepatic microsomal 5α-reductase. The renal nuclear metabolism of androstenedione, i.e. 5α reduction and 17β-hydroxy steroid reduction, was relatively unaffected by sex, age, castration and treatment with testosterone propionate. However, treatment of castrated male rats with oestradiol benzoate led to a significant increase in the 5α-reductase activity and a significant decrease in the 17β-hydroxy steroid reductase activity. Finally, the nuclear 5α-reductase activity in prostate was androgen-dependent, decreasing after castration and increasing after treatment with testosterone propionate. In conclusion, the nuclear 5α-reductase activities in liver, kidney and prostate seem to be under the control of distinctly different regulatory mechanisms. The hypothesis is presented that whereas the prostatic nuclear 5α-reductase participates in the formation of a physiologically active androgen, 5α-dihydrotestosterone, this may not be the true function of the nuclear 5α-reductase in liver and kidney. These enzymes might rather serve to protect the androgen target sites in the chromatin from active androgens (e.g. testosterone) by transforming them into less active androgens (e.g. 5α-androstane-3,17-dione and/or 5α-dihydrotestosterone).

scholarly journals Marker genes identify three somatic cell types in the fetal mouse ovary

2014 ◽  
Vol 394 (2) ◽  
pp. 242-252 ◽  
Author(s):  
Raphael H. Rastetter ◽  
Pascal Bernard ◽  
James S. Palmer ◽  
Anne-Amandine Chassot ◽  
Huijun Chen ◽  
...  
Keyword(s):  
Somatic Cell ◽  
Cell Types ◽  
Marker Genes ◽  
Mouse Ovary ◽  
Fetal Mouse

Two Phases Of Ferricyanide Reductase Activity In Ehrlich Cell Plasma Membranes

1992 ◽  
Vol 47 (11-12) ◽  
pp. 929-931 ◽  
Author(s):  
Antonio del Castillo-Olivares ◽  
Javier Márquez ◽  
Ignacio Núñez de Castro ◽  
Miguel Angel Medina
Keyword(s):  
Plasma Membrane ◽  
Plasma Membranes ◽  
Reductase Activity ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Cell Plasma Membrane ◽  
Ferricyanide Reductase ◽  
Ehrlich Cell ◽  
Cell Plasma ◽  
Two Phases

Ehrlich cell plasma membrane vesicles have a ferricyanide reductase activity that shows two phases. These two phases were kinetically characterized. Evidence is presented for a differential effect of trypsin on both phases

Loss of Betaglycan Disrupts Somatic Cell Differentiation and Germ Cell Entry into Meiosis in the Fetal Mouse Ovary.

2010 ◽  
Vol 83 (Suppl_1) ◽  
pp. 178-178
Author(s):  
Mai A. Sarraj ◽  
Ruth Escalona ◽  
Alexandra Umbers ◽  
Jock K. Findlay ◽  
Kaye L. Stenvers
Keyword(s):  
Cell Differentiation ◽  
Germ Cell ◽  
Somatic Cell ◽  
Cell Entry ◽  
Mouse Ovary ◽  
Fetal Mouse

scholarly journals Characterization of membrane polypeptides from pea leaf peroxisomes involved in superoxide radical generation

1999 ◽  
Vol 337 (3) ◽  
pp. 531-536 ◽  
Author(s):  
Eduardo LÓPEZ-HUERTAS ◽  
Francisco J. CORPAS ◽  
Luisa M. SANDALIO ◽  
Luis A. DEL RÍO
Keyword(s):  
Cytochrome C ◽  
Electron Donor ◽  
Polyclonal Antibodies ◽  
Reductase Activity ◽  
Monodehydroascorbate Reductase ◽  
Peroxisomal Membrane ◽  
Cytochrome C Reductase ◽  
Ferricyanide Reductase ◽  
Sds Page ◽  
O2 Production

The production of superoxide radicals (O2-•) and the activities of ferricyanide reductase and cytochrome c reductase were investigated in peroxisomal membranes from pea (Pisum sativum L.) leaves using NADH and NADPH as electron donors. The generation of O2-• by peroxisomal membranes was also assayed in native polyacrylamide gels using an in situ staining method with NitroBlue Tetrazolium (NBT). When peroxisomal membranes were assayed under native conditions using NADH or NADPH as inducer, two different O2-•-dependent Formazan Blue bands were detected. Analysis by SDS/PAGE of these bands demonstrated that the NADH-induced NBT reduction band contained several polypeptides (PMP32, PMP61, PMP56 and PMP18, where PMP is peroxisomal membrane polypeptide and the number indicates molecular mass in kDa), while the NADPH-induced band was due exclusively to PMP29. PMP32 and PMP29 were purified by preparative SDS/PAGE and electroelution. Reconstituted PMP29 showed cytochrome c reductase activity and O2-• production, and used NADPH specifically as electron donor. PMP32, however, had ferricyanide reductase and cytochrome c reductase activities, and was also able to generate O2-• with NADH as electron donor, whereas NADPH was not effective as an inducer. The reductase activities of, and O2-• production by, PMP32 were inhibited by quinacrine. Polyclonal antibodies against cucumber monodehydroascorbate reductase (MDHAR) recognized PMP32, and this polypeptide is likely to correspond to the MDHAR reported previously in pea leaf peroxisomal membranes.

scholarly journals Ascorbate-mediated transplasma membrane electron transport in pulmonary arterial endothelial cells

1998 ◽  
Vol 274 (5) ◽  
pp. L685-L693 ◽  
Author(s):  
Marilyn P. Merker ◽  
Lars E. Olson ◽  
Robert D. Bongard ◽  
Meha K. Patel ◽  
John H. Linehan ◽  
...  
Keyword(s):  
Methylene Blue ◽  
Endothelial Cells ◽  
Plasma Membrane ◽  
Electron Transport ◽  
Electron Acceptor ◽  
Reductase Activity ◽  
Ferricyanide Reductase ◽  
Transplasma Membrane Electron Transport ◽  
Pulmonary Arterial ◽  
Arterial Endothelial Cells

Pulmonary endothelial cells are capable of reducing certain electron acceptors at the luminal plasma membrane surface. Motivation for studying this phenomenon comes in part from the expectation that it may be important both as an endothelial antioxidant defense mechanism and in redox cycling of toxic free radicals. Pulmonary arterial endothelial cells in culture reduce the oxidized forms of thiazine compounds that have been used as electron acceptor probes for studying the mechanisms of transplasma membrane electron transport. However, they reduce another commonly studied electron acceptor, ferricyanide, only very slowly by comparison. In the present study, we examined the influence of ascorbate [ascorbic acid (AA)] and dehydroascorbate [dehydroascorbic acid (DHAA)] on the ferricyanide and thiazine reductase activities of the bovine pulmonary arterial endothelial cell surface. The endothelial cells were grown on microcarrier beads so that the reduction of ferricyanide and methylene blue could be studied colorimetrically in spectrophotometer cuvettes and in flow-through cell columns. The ferricyanide reductase activity could be increased 80-fold by adding DHAA to the medium, with virtually no effect on methylene blue reduction. The DHAA effect persisted after the DHAA was removed from the medium. AA also stimulated the ferricyanide reductase activity but was less potent, and the relative potencies of AA and DHAA correlated with their relative rates of uptake by the cells. The results are consistent with the hypothesis that AA is an intracellular electron donor for an endothelial plasma membrane ferricyanide reductase and that the stimulatory effect of DHAA is the result of increasing intracellular AA. Adding sufficient DHAA to markedly increase extracellular ferricyanide reduction had little effect on the plasma membrane methylene blue reductase activity, suggesting that pulmonary arterial endothelial cells have at least two separate transplasma membrane electron transport systems.

An Atypical Substrate–inhibitor–Rate Relationship for the Action of Antimycin A on the Succinate–Ferricyanide Reductase Activity of Beef Heart Electron Transfer Particles

1971 ◽  
Vol 49 (8) ◽  
pp. 936-940 ◽  
Author(s):  
G. L. Perry ◽  
G. R. Williams
Keyword(s):  
Electron Transfer ◽  
Reductase Activity ◽  
Random Order ◽  
Beef Heart ◽  
Antimycin A ◽  
Ferricyanide Reductase ◽  
Rate Relationship ◽  
Alternative Routes ◽  
Substrate Inhibitor

The degree of inhibition of the succinate–ferricyanide reductase activity of beef heart electron transfer particles by antimycin A is negligible at low succinate concentrations (< 1 mM) but increases to about 40% at saturating concentrations of succinate. This behavior is explained on the basis of a random order mechanism for the primary dehydrogenase with alternative routes from the monosubstrate complexes, only one of which is sensitive to antimycin.

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