Hormonal regulation of oxytocin-induced prostaglandin F2α secretion by the bovine and ovine uterus in vivo

2001 ◽  
Vol 21 (2) ◽  
pp. 127-141 ◽  
Author(s):  
G.E Mann ◽  
J.H Payne ◽  
G.E Lamming
1997 ◽  
Vol 38 (12) ◽  
pp. 2483-2491 ◽  
Author(s):  
W M Pandak ◽  
D M Heuman ◽  
K Redford ◽  
R T Stravitz ◽  
J Y Chiang ◽  
...  

2010 ◽  
Vol 24 (3) ◽  
pp. 632-643 ◽  
Author(s):  
Edward Arvisais ◽  
Xiaoying Hou ◽  
Todd A. Wyatt ◽  
Koumei Shirasuna ◽  
Heinrich Bollwein ◽  
...  

Abstract Little is known about the early intracellular events that contribute to corpus luteum regression. Experiments were designed to determine the effects of prostaglandin F2α (PGF2α) on phosphatidylinositol-3-kinase (PI3K)/Akt signaling in the corpus luteum in vivo and in vitro. Treatment of midluteal-phase cows with a luteolytic dose of PGF2α resulted in a rapid increase in ERK and mammalian target of rapamycin (mTOR)/p70 ribosomal protein S6 kinase (p70S6K1) signaling and a rapid suppression of Akt phosphorylation in luteal tissue. In vitro treatment of primary cultures of luteal cells with PGF2α also resulted in an increase in ERK and mTOR/p70S6K1 signaling and a diminished capacity of IGF-I to stimulate PI3K, Akt, and protein kinase C ζ activation. Accounting for the reductions in PI3K and Akt activation observed in response to PGF2α treatment, we found that PGF2α promoted the phosphorylation of serine residues (307, 612, 636) in the insulin receptor substrate 1 (IRS1) peptide sequence in vivo and in vitro. Serine phosphorylation of IRS1 was associated with reduced formation of IGF-I-stimulated IRS1/PI3Kp85 complexes. Furthermore, treatment with inhibitors of the MAPK kinase 1/ERK or mTOR/p70S6K1 signaling pathways prevented PGF2α-induced serine phosphorylation of IRS1 and abrogated the inhibitory actions of PGF2α on Akt activation. Taken together, these experiments provide compelling evidence that PGF2α treatment stimulates IRS1 serine phosphorylation, which may contribute to a diminished capacity to respond to IGF-I. It seems likely that the rapid changes in phosphorylation events are among the early events that mediate PGF2α-induced corpus luteum regression.


ÈKOBIOTEH ◽  
2021 ◽  
Vol 4 (1) ◽  
pp. 11-23
Author(s):  
N.N. Kruglova ◽  

The article provides the brief review of the literature and own works devoted to the peculiarities of the cereal embryonic organogenesis at the early stages of ontogenesis in the conditions of in vitro culture (the so-called somatic embryogenesis, or embryoidogenesis in vitro). Particular attention is paid to the issues of hormonal regulation of the development of somatic cereal embryos from initial cells to mature structures in vitro. A comparison of somatic embryogenesis in vitro with similar events in zygotic embryogenesis in vivo confirms the validity of the principle of universality of morphogenesis processes in vivo and in vitro (Batygina, 2014). The prospects of using somatic embryogenesis in vitro as a model for studying the most complex biological phenomenon – zygotic plant embryogenesis in vivo – are discussed.


1990 ◽  
Vol 78 (2) ◽  
pp. 181-184 ◽  
Author(s):  
J. Haylor ◽  
C. J. Lote

1. The influence of urine pH on the urinary excretion of prostaglandin (PG) F2α and the PGE2/PGF2α ratio has been examined in the conscious rat. 2. The basal urinary PGF2α excretion rate of 3.9 pmol/h (n = 23) did not vary with urine pH. In marked contrast, PGE2 excretion increased as the urine became more alkaline. The PGE2/PGF2α ratio therefore progressively increased from 1.5 to 22 as the pH of the urine changed from pH 5.8 to pH 7.8. 3. The independence of PGF2α excretion from urine pH: (a) excludes cyclo-oxygenase as a potential site of action for the pH-dependence of urinary PGE2 excretion; (b) suggests that the urinary PGE2/PGF2α ratio measured in alkaline urine may be a more accurate reflection of the kidneys, ability to synthesize these two prostaglandins in vivo; (c) suggests that control of urine pH is required before the urinary PGE2/PGF2α ratio can be employed as an index of PGE2 9-ketoreductase (EC 1.1.1.189) activity in vivo.


1981 ◽  
Vol 240 (4) ◽  
pp. G274-G280
Author(s):  
M. W. Goodman ◽  
W. F. Prigge ◽  
R. L. Gebhard

Hormonal regulation of intestinal cholesterol synthesis was studied both in vitro and in vivo. Cholesterol synthesis rate was determined by measurement of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (EC 1.1.1.34) activity and by incorporation [14C]acetate into sterol. In vitro studies utilized organ culture of canine ileal mucosa. During 6-h culture, reductase activity was stimulated sevenfold. Insulin (10-6 M) augmented this rise to 144 +/- 7% of th control activity, while 10(-8) M glucagon, 10(-3) M adenosine 3',5'-cyclic monophosphate, and 3-isobutyl-1-methylxanthine suppressed activity (final reductase activity was 83 +/- 3%, 75 +/- 4%, and 41 +/- 3%, respectively, of cultured control values). In vivo studies utilized dogs with isolated Thiry-Vella ileal fistulas. In vivo, insulin doubled reductase activity while glucagon led to a 42 +/- 9% suppression. It is concluded that insulin and glucagon may be potential physiological regulators of intestinal cholesterol synthesis. The glucagon effect may be mediated by cyclic nucleotides.


2019 ◽  
Vol 36 (6) ◽  
pp. 1293-1293 ◽  
Author(s):  
Seyedeh Sima Daryabari ◽  
Abdol-Mohammad Kajbafzadeh ◽  
Kiarad Fendereski ◽  
Fariba Ghorbani ◽  
Mehrshad Dehnavi ◽  
...  
Keyword(s):  

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