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Expression of cytochrome P450 mRNA in rat germ cells was characterized by reverse transcription PCR with various primers located at the 3'-end of the coding region. At least two unusual isoforms (Ex10-S and INT) of P450 aromatase (P450arom) mRNA were expressed. Analysis of their sequences demonstrated that an alternative splicing event occurred first at the(More)
BACKGROUND Patients with pseudohypoparathyroidism type Ib (PHP-1b) develop resistance toward PTH, leading to hypocalcemia and hyperphosphatemia. PHP-1b is an imprinted human disorder associated with methylation changes at one or several differentially methylated regions at the GNAS locus. This complex locus gives rise to several different transcripts with(More)
Aromatase is a steroidogenic enzyme complex which catalyses the conversion of androgens to estrogens. In a previous study, we elucidated the structure of a 2.9 kb aromatase cDNA from ovarian rabbit tissue. We report here, the structure of another shorter aromatase cDNA (1.5 kb) from the same tissue. This cDNA is likely to encode for a nonfunctional(More)
OBJECTIVE The aromatase enzyme catalyzes the final stage of estrogen biosynthesis pathway from androgens. Its expression in the adrenal is poorly studied except for the rare estrogen-producing adrenocortical tumors. In order to further characterize aromatase expression in the adrenal, we evaluated the aromatase enzyme activity, Cyp19a1 gene expression(More)
A 30-year-old male was referred for the rapid development of gynecomastia, and dramatic hyperestrogenemia was assessed: plasma estrone, estradiol but also cortisol were not suppressed by high-dose dexamethasone, while gonadotropin pulsatility was completely abolished. A 60-mm right adrenal tumor was evidenced on computed tomography-scan, and the patient(More)
Estrogens are synthesized from C19 steroids by a unique form of cytochrome P450 aromatase. Expression of the human CYP19 gene involves tissue specific use of alternative promoters. In the present study, an RT-PCR procedure was used to amplify and quantify various transcripts expressed in human granulosa cells. Cells were aspirated together with follicular(More)
Aromatase protein is synthesized in response to gonadotropins that activate expression of their target genes via the cAMP second messenger system. The -882/+103 bp region of the rabbit ovarian promoter (PII) was ligated to a luciferase vector and transfected into granulosa cells to elucidated the mechanism by which cAMP stimulates transcription. Deletions(More)
Transcription of the CYP19 gene encoding the aromatase P450 enzyme in ovarian cells is under the control of the two gonadotropins, follicle stimulating hormone (FSH) and luteinizing hormone (LH), via modulation of intracellular cyclic 3',5'-adenosine monophosphate (cAMP) levels. Primary cultures of rabbit ovarian cells were used to identify the functional(More)
We have previously suggested that the interaction between luteinizing hormone (LH) and its receptor, in addition to stimulating adenylate cyclase, is able to trigger a negative regulatory signal at a step beyond cAMP synthesis (Benhaim et al. (1987) FEBS Lett. 223, 321-326). The present study was conducted to determine whether the phospholipase C system is(More)
In previous studies we described the synthesis of three mitochondrial proteins (A, B and C) in response to acute in vitro stimulation by lutropin of small bovine luteal cells. Protein A had a molecular weight of 28 kDa and an isoelectric point (pI) of 6.7. Proteins B and C had a molecular mass of 27 kDa and pI of 6.2 and 6.4, respectively. The appearance of(More)