A putative protein–RNA complex regulates posttranscriptional processing of cytochrome P450 aromatase (CYP19A1) in bovine granulosa cells

2019 ◽  
Vol 86 (12) ◽  
pp. 1901-1908
Author(s):  
Fatiha Sahmi ◽  
Malha Sahmi ◽  
Nicolas Gévry ◽  
Pramod Sahadevan ◽  
Bruce G. Allen ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Granulosa Cells ◽  
P450 Aromatase ◽  
Putative Protein ◽  
Cytochrome P450 Aromatase ◽  
Posttranscriptional Processing ◽  
Rna Complex

Cytochrome P450 Aromatase Promoter Usage in Bovine Granulosa Cells.

2012 ◽  
Vol 87 (Suppl_1) ◽  
pp. 578-578
Author(s):  
Fatiha Sahmi ◽  
Edmir Nicola ◽  
Gustavo Zamberlam ◽  
Christopher A. Price
Keyword(s):  
Cytochrome P450 ◽  
Granulosa Cells ◽  
P450 Aromatase ◽  
Cytochrome P450 Aromatase ◽  
Promoter Usage

scholarly journals Immunohistochemical localization of cytochrome P450 aromatase in equine gonads.

1995 ◽  
Vol 43 (6) ◽  
pp. 571-577 ◽  
Author(s):  
J Almadhidi ◽  
G E Seralini ◽  
J Fresnel ◽  
P Silberzahn ◽  
J L Gaillard
Keyword(s):  
Cytochrome P450 ◽  
Granulosa Cells ◽  
Immunoblot Analysis ◽  
Immunofluorescent Staining ◽  
Interstitial Tissue ◽  
Experimental Conditions ◽  
Specific Staining ◽  
P450 Aromatase ◽  
Estrogen Synthesis ◽  
Cytochrome P450 Aromatase

Estrogens are the major steroids produced by equine gonads. To identify the cells responsible for estrogen synthesis, an antiserum against purified equine testicular cytochrome P450 aromatase was produced in rabbits. The reactivity and specificity of the antiserum were assessed by ELISA, immunoblot analysis, and immunoneutralization studies. Immunofluorescence microscopy demonstrated that in the male gonad, cytochrome P450 aromatase (P450arom) was localized in the interstitial tissue, whereas, under the experimental conditions used, the Sertoli and germ cells did not show any specific staining. In the ovary, the granulosa cells of small follicles exhibited faint immunofluorescent staining for P450arom and the granulosa cells of large, viable more follicles showed a high degree of immunoreactivity. In the corpus luteum, all the luteinized cells showed immunoreactivity. No immunoreactivity was detected in other cells of small and large viable follicles. Immunolocalization of P450arom in the equine testicular Leydig cells and in ovarian granulosa and luteinized cells indicates that these cells have the ability to metabolize androgens to estrogens and possibly to catechol estrogens.

scholarly journals Hormonal regulation of cytochrome P450 aromatase mRNA stability in non-luteinizing bovine granulosa cells in vitro

2006 ◽  
Vol 190 (1) ◽  
pp. 107-115 ◽  
Author(s):  
Malha Sahmi ◽  
Edmir S Nicola ◽  
Christopher A Price
Keyword(s):  
Cytochrome P450 ◽  
Granulosa Cells ◽  
Half Life ◽  
Hormonal Regulation ◽  
Hormonal Control ◽  
Transcriptional Level ◽  
P450 Aromatase ◽  
Cytochrome P450 Aromatase ◽  
Mrna Half Life

In the present study, we determined the potential for post-transcriptional regulation of cytochrome P450 aromatase (Cyp19), cytochrome P450 side-chain cleavage (Cyp11a) and 17β-hydroxysteroid dehydrogenase I (Hsd17b1) mRNA. Bovine granulosa cells were cultured in non-luteinizing conditions that permit long-term oestradiol secretion. Half-lives of mRNA were measured by Northern and/or reverse transcriptase (RT)-PCR after inhibition of gene transcription. In FSH-stimulated cells, the Cyp11a and Hsd17b1 mRNAs had half-lives greater than 12 h. The half-life of Cyp19 mRNA was significantly shorter at 3 h. The addition of the translation inhibitor cycloheximide to FSH-stimulated cells significantly increased Cyp19 mRNA half-life to approximately 12 h. Stimulation of cells with insulin resulted in Cyp19 mRNA half-life that was double (P<0.05) that in FSH-stimulated cells. We conclude that bovine Cyp19 mRNA is very labile under physiological conditions, and that Cyp19 expression is under hormonal control at a post-transcriptional level.

Expression of 17β-hydroxysteroid dehydrogenase in human granulosa cells: correlation with follicular size, cytochrome P450 aromatase activity and oestradiol production

1994 ◽  
Vol 143 (1) ◽  
pp. 139-150 ◽  
Author(s):  
S A Ghersevich ◽  
M H Poutanen ◽  
H K Martikainen ◽  
R K Vihko
Keyword(s):  
Cytochrome P450 ◽  
Granulosa Cells ◽  
Protein Concentration ◽  
Hydroxysteroid Dehydrogenase ◽  
Enzyme Protein ◽  
P450 Aromatase ◽  
Human Granulosa Cells ◽  
Cytochrome P450 Aromatase ◽  
In Cells

Abstract The aim of this study was to examine the expression and regulation of type 1 17β-hydroxysteroid dehydrogenase (type 1 17-HSD) enzyme protein and mRNA, and 17-HSD activity in human granulosa cells. The cells were obtained from patients taking part in an in vitro fertilization programme. The cells from each patient were divided into two groups: cells obtained from preovulatory follicles (LGC=granulosa cells from large follicles ≥ 18 mm in diameter), and cells from other visible follicles (SGC=granulosa cells from small follicles, less than 15 mm in diameter). The identity of 17-HSD enzyme protein expressed in human granulosa cells with placental cytosolic 17-HSD (type 1 17-HSD) was assessed by immunoblot analysis using polyclonal antibodies, and the enzyme was immunolocalized in the cytoplasm of granulosa cells. Type 1 17-HSD protein concentration, 17-HSD and cytochrome P450 aromatase (P450arom) activities and oestradiol (OE2) production in cells from LGC were significantly lower than the corresponding values obtained in SGC in the same patient (paired t-test). The type 1 17-HSD protein concentration, 17-HSD activity and P450arom activity were 140±16% (mean±s.e.m.), 121±22% and 113±26% higher in cells from SGC, which was also reflected in a 70±12% higher OE2 production in these cells. In freshly isolated cells from LGC or SGC, a high correlation between 17-HSD and P450arom activities was observed (r=0·93, P<0·001). In long-term cultured cells, type 1 17-HSD was stably expressed at least until day 9, while P450arom expression decreased. In addition, treatments with gonadotrophins did not affect type 1 17-HSD protein concentration and 17-HSD activity. In contrast to this, both P450arom activity and OE2 production were significantly increased (P<0·05). The data, therefore, suggest that type 1 17-HSD and P450arom are expressed in parallel during the latest stages of follicular maturation but, in cultured granulosa-luteal cells, the enzymes are regulated by distinct mechanisms. Journal of Endocrinology (1994) 143, 139–150

Closely Related Genes Encode Developmental and Tissue Isoforms of Porcine Cytochrome P450 Aromatase

1997 ◽  
Vol 16 (6) ◽  
pp. 769-777 ◽  
Author(s):  
INHO CHOI ◽  
DERYL L. TROYER ◽  
DEAN L. CORNWELL ◽  
KATHY R. KIRBY-DOBBELS ◽  
WERNER R. COLLANTE ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
P450 Aromatase ◽  
Cytochrome P450 Aromatase
Sign in / Sign up

Export Citation Format

Share Document