This protein has been shown to inhibit endometrial prostaglandin production and to decrease the amount of PGF2 alpha released in response to oxytocin. Reduction of uterine oxytocin receptor concentrations by conceptus secretory proteins or by interferons related to oTP-1 remains equivocal. Inhibition of uterine oxytocin receptors is, however
The control group received a standard intravenous oxytocin regimen. The PGF2 alpha treated group had a significantly shorter length of labour (6.2 /- 3.6 hours) compared to the oxytocin group (7.5 /- 4.3 hours) (p less than 0.05). The analgesic requirements were significantly reduced in the PGF2 alpha treated patients.
Oxytocin stimulated secretion of PGF2 alpha and PGE2 (P 0.01) from epithelial cells, but both basal secretion and oxytocin-induced secretion of PGF2 alpha and PGE2 decreased with increasing dose of either nbIFN tau or rbIFN tau (P 0.01). At comparable doses, rbIFN tau inhibited PGF2 alpha and PGE2 secretion more strongly than did nbIFN tau
Background: Previous studies have demonstrated that neonatal manipulation of oxytocin (OT) has effects on the expression of estrogen receptor alpha (ER alpha) and the central production of oxytocin observed in juveniles (at weaning, 21 days of age). The goal of this study was to determine whether the effects of neonatal manipulation of OT last
The pulsatile release of oxytocin from the corpus luteum in the sheep is responsible for the pulsatile release of prostaglandin F2 alpha (PGF2 alpha) from the uterus at luteolysis. It has been proposed that PGF2 alpha also reinforces this process by stimulating the release of oxytocin from the corpu
The final step in the enzymatic hydrolysis of the oxytocin precursor is mediated by the alpha-amidating monooxygenase peptidylglycine, which requires ascorbic acid as a cofactor . Oxytocin is metabolized in the liver and plasma, with the help of oxytocinases and a much smaller percentage in the mammary glands.
As a result, the release of TNF-alpha and other pro-inflammatory cytokines from macrophages is significantly inhibited by ligation of oxytocin to oxytocin receptor . Oxytocin has been shown to upregulate the expression of peroxisome proliferator-activated receptor gamma (PPAR-gamma), a potent transcription factor that dampens inflammatory
An anti-G alpha q/11 antibody inhibits both oxytocin-stimulated GTPase activity and phospholipase C activity in myometrial membranes. The stimulation by oxytocin of phosphoinositide turnover in COS cells transfected with a plasmid expressing the oxytocin receptor is enhanced by cotransfection of G alpha q. Co-transfection of intracellular
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