Mechanisms Controlling the Function and Life Span of the Corpus Luteum

2000 ◽  
Vol 80 (1) ◽  
pp. 1-29 ◽  
Author(s):  
Gordon D. Niswender ◽  
Jennifer L. Juengel ◽  
Patrick J. Silva ◽  
M. Keith Rollyson ◽  
Eric W. McIntush
Keyword(s):  
Protein Kinase ◽  
Corpus Luteum ◽  
Anterior Pituitary ◽  
Second Messenger ◽  
Cell Types ◽  
Normal Pregnancy ◽  
Luteal Cells ◽  
Steroidogenic Cell ◽  
Reflex Arc ◽  
And Function

The primary function of the corpus luteum is secretion of the hormone progesterone, which is required for maintenance of normal pregnancy in mammals. The corpus luteum develops from residual follicular granulosal and thecal cells after ovulation. Luteinizing hormone (LH) from the anterior pituitary is important for normal development and function of the corpus luteum in most mammals, although growth hormone, prolactin, and estradiol also play a role in several species. The mature corpus luteum is composed of at least two steroidogenic cell types based on morphological and biochemical criteria and on the follicular source of origin. Small luteal cells appear to be of thecal cell origin and respond to LH with increased secretion of progesterone. LH directly stimulates the secretion of progesterone from small luteal cells via activation of the protein kinase A second messenger pathway. Large luteal cells are of granulosal cell origin and contain receptors for PGF2αand appear to mediate the luteolytic actions of this hormone. If pregnancy does not occur, the corpus luteum must regress to allow follicular growth and ovulation and the reproductive cycle begins again. Luteal regression is initiated by PGF2αof uterine origin in most subprimate species. The role played by PGF2αin primates remains controversial. In primates, if PGF2αplays a role in luteolysis, it appears to be of ovarian origin. The antisteroidogenic effects of PGF2αappear to be mediated by the protein kinase C second messenger pathway, whereas loss of luteal cells appears to follow an influx of calcium, activation of endonucleases, and an apoptotic form of cell death. If the female becomes pregnant, continued secretion of progesterone from the corpus luteum is required to provide an appropriate uterine environment for maintenance of pregnancy. The mechanisms whereby the pregnant uterus signals the corpus luteum that a conceptus is present varies from secretion of a chorionic gonadotropin (primates and equids), to secretion of an antiluteolytic factor (domestic ruminants), and to a neuroendocrine reflex arc that modifies the secretory patterns of hormones from the anterior pituitary (most rodents).

scholarly journals Control of Steroidogenesis in Small and Large Bovine Luteal. Cells

1987 ◽  
Vol 40 (3) ◽  
pp. 331 ◽  
Author(s):  
William Hansel ◽  
Hector W Alila ◽  
Joseph P Dowd ◽  
Xiangzhong Yang
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Corpus Luteum ◽  
Luteal Cell ◽  
Lipoxygenase Pathway ◽  
Luteal Cells ◽  
Kinase C ◽  
Bovine Corpus Luteum ◽  
Progesterone Synthesis

Evidence was cited to show that: (1) prostacyclin (PGI2) plays a luteotrophic role in the bovine corpus luteum and that products of the lipoxygenase pathway of arachidonic acid metabolism, especially 5-hydroxyeicosatetraenoic acid play luteolytic roles; (2) oxytocin of luteal cell origin plays a role in development, and possibly in regression, of the bovine corpus luteum; and (3) luteal cells arise from two sources; the characteristic small luteal cells at all stages of the o~strous cycle and pregnancy are of theca cell origin; the large cells are of granulosa cell origin early in the cycle, but a population of theca-derived large cells appears later in the cycle. Results of in vitro studies with total dispersed cells and essentially pure preparations of large and small luteal cells indicate that : (1) the recently described Ca2+ -polyphosphoinositol-protein kinase C second messenger system is involved in progesterone synthesis in the bovine corpus luteum; (2) activation of protein kinase C is stimulatory to progesterone synthesis in the small luteal cells; (3) activation of protein kinase C has no effect on progesterone synthesis in the large luteal cells; and (4) protein kinase C exerts its luteotrophic effect in total cell preparations, in part at least, by stimulating the production of prostacyclin. The protein kinase C system may cause down regulation of LH receptors in the large cells.

scholarly journals Purification, Morphology, and Progesterone Production and Content of Three Cell Types Isolated from the Corpus Luteum of the Sheep

1982 ◽  
Vol 35 (4) ◽  
pp. 441 ◽  
Author(s):  
RJ Rodgers ◽  
JD O'Shea
Keyword(s):  
Endothelial Cells ◽  
Smooth Muscle ◽  
Corpus Luteum ◽  
Cell Types ◽  
Cellular Composition ◽  
Isolation And Purification ◽  
Luteal Cells ◽  
Ficoll Gradient ◽  
Luteal Tissue ◽  
Cell Fractions

A method is presented for the isolation and purification of three cell types, endothelial cells, small luteal cells and large luteal cells, from the ovine corpus luteum. The method involves enzymatic dispersion of luteal tissue followed by centrifugation of separated cells on a Ficoll gradient. The three purified cell types and others, particularly fibrocytes and smooth muscle cells, that were removed during purification, were identified by their morphology. The cell yield, the cellular composition and cellular progesterone content of each fraction from the Ficoll gradient were measured. The endothelial cell fractions were relatively free of contamination by other cell types and had negligible progesterone. Fractions of small luteal cells and those of large luteal cells contained endothelial cells but were relatively free of other cell types. Large luteal cells contained significantly more progesterone, produced more progesterone when incubated in culture, but were less responsive to luteinizing hormone than small luteal cells.

Does prostacyclin (PGI2) support porcine corpus luteum function? – data from in vitro study

2016 ◽  
Vol 62 (5) ◽  
pp. 49
Author(s):  
Magdalena Julia Szymańska ◽  
Agnieszka Blitek
Keyword(s):  
Endothelial Cells ◽  
Mrna Expression ◽  
Corpus Luteum ◽  
Estrous Cycle ◽  
In Vitro Study ◽  
Luteal Cells ◽  
Enzymatic Isolation ◽  
Effective Doses ◽  
And Function

Background. Prostacyclin (PGI2) of luteal origin is involved in the control of corpus luteum (CL) development and function in cattle. PGI2 may regulate the process of angiogenesis and may stimulate progesterone (P4) secretion by luteal cells via its specific receptors, PTGIR. In contrast to cattle, the role of PGI2 in the pig CL has not yet been described.Aim. The present study aimed to investigate the effect of PGI2 on 1) P4 secretion by luteal cells, and 2) the expression of angiogenesis-related genes in endothelial cells of the porcine CL.Methods. CL collected from gilts on day 5-7 of the estrous cycle were used for enzymatic isolation of luteal (Experiment 1) and endothelial (Experiment 2) cells. In Exp. 1, cultured luteal cells were incubated with increasing (0, 0.01, 0.1, 1, 5 µM) doses of PGI2 analogues: iloprost (ILO) and carbaprostacyclin (cPGI2) for 8 h. To determine the effective doses of PGI2 analogues, P4 concentration in culture medium was examined by RIA. Thereafter, luteal cells were treated with ILO and cPGI2 at the concentration of 1 and 5 µM in the presence or absence of PTGIR antagonist (CAY10441). After 8 h of incubation the medium was collected for P4 determination. In Exp. 2, isolated endothelial cells were treated for 24 h with ILO and cPGI2 at doses of 1 and 5 µM. Then, cells were collected for analysis of Ang-1 and -2 mRNA expression using qPCR.Results. Both, ILO and cPGI2 affected P4 secretion by luteal cells. Elevated levels of P4 were observed in medium after treatment of luteal cells with 1 µM of ILO and 0.1, 1 and 5 µM of cPGI2 compared with control values (p<0.05). The addition of CAY10441 inhibited the stimulatory effect of ILO on P4 secretion, while did not change P4 production by luteal cells incubated with cPGI2. Moreover, PGI2 analogues differentially affected (p<0.05) the expression of proangiogenic factors. ILO stimulated Ang-2, whereas cPGI2 positively affected Ang-1 mRNA expression in endothelial cells at concentrations of 1 µM and 5 µM, respectively.Conclusion. PGI2 affects P4 secretion during luteal phase of the estrous cycle and may regulate the process of angiogenesis in the porcine CL.

Expression of protein kinase C isoforms in various steroidogenic cell types

1991 ◽  
Vol 75 (2) ◽  
pp. 149-155 ◽  
Author(s):  
Jean-Marc Pelosin ◽  
Annie Ricouart ◽  
Christian Sergheraert ◽  
Mohamed Benahmed ◽  
Edmond M. Chambaz
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Types ◽  
Kinase C ◽  
Steroidogenic Cell ◽  
Protein Kinase C Isoforms

scholarly journals PKA and AMPK Signaling Pathways Differentially Regulate Luteal Steroidogenesis

Endocrinology ◽  
2021 ◽  
Vol 162 (4) ◽  
Author(s):  
Emilia Przygrodzka ◽  
Xiaoying Hou ◽  
Pan Zhang ◽  
Michele R Plewes ◽  
Rodrigo Franco ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Corpus Luteum ◽  
Posttranslational Modifications ◽  
Enzyme Activation ◽  
Hormone Sensitive Lipase ◽  
Negative Effects ◽  
Luteal Cells ◽  
Ampk Signaling ◽  
Progesterone Synthesis ◽  
Amp Activated Protein Kinase

Abstract Luteinizing hormone (LH) via protein kinase A (PKA) triggers ovulation and formation of the corpus luteum, which arises from the differentiation of follicular granulosa and theca cells into large and small luteal cells, respectively. The small and large luteal cells produce progesterone, a steroid hormone required for establishment and maintenance of pregnancy. We recently reported on the importance of hormone-sensitive lipase (HSL, also known as LIPE) and lipid droplets for appropriate secretory function of the corpus luteum. These lipid-rich intracellular organelles store cholesteryl esters, which can be hydrolyzed by HSL to provide cholesterol, the main substrate necessary for progesterone synthesis. In the present study, we analyzed dynamic posttranslational modifications of HSL mediated by PKA and AMP-activated protein kinase (AMPK) as well as their effects on steroidogenesis in luteal cells. Our results revealed that AMPK acutely inhibits the stimulatory effects of LH/PKA on progesterone production without reducing levels of STAR, CYP11A1, and HSD3B proteins. Exogenous cholesterol reversed the negative effects of AMPK on LH-stimulated steroidogenesis, suggesting that AMPK regulates cholesterol availability in luteal cells. AMPK evoked inhibitory phosphorylation of HSL (Ser565). In contrast, LH/PKA decreased phosphorylation of AMPK at Thr172, a residue required for its activation. Additionally, LH/PKA increased phosphorylation of HSL at Ser563, which is crucial for enzyme activation, and decreased inhibitory phosphorylation of HSL at Ser565. The findings indicate that LH and AMPK exert opposite posttranslational modifications of HSL, presumptively regulating cholesterol availability for steroidogenesis.

Expression and role of resistin on steroid secretion in the porcine corpus luteum

Reproduction ◽  
2021 ◽  
Author(s):  
Patrycja Kurowska ◽  
Monika Sroka ◽  
Monika Dawid ◽  
Ewa Mlyczyńska ◽  
Natalia Respekta ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Corpus Luteum ◽  
Luteal Phase ◽  
Cell Function ◽  
Orphan Receptor ◽  
Mitogen Activated Protein Kinase ◽  
Luteal Cell ◽  
Steroid Synthesis ◽  
Steroid Secretion ◽  
Luteal Cells

Resistin plays an important role in adipogenesis, obesity, insulin resistance and reproduction. Previous studies showed resistin action on ovarian follicular cells; however, whether resistin regulates steroid secretion in luteal cells is still unknown. Our aim was first to determine the expression of resistin and its potential receptors (tyrosine kinase-like orphan receptor 1 [ROR1] and Toll-like receptor 4 [TLR4]) in the porcine corpus luteum (CL), regulation of its expression, effect on kinases phosphorylation and luteal steroidogenesis. Our results showed that the expression of resistin and its receptors was dependent on the luteal phase and this was at the mRNA level higher in the late compared with the early and middle luteal phase. At the opposite, resistin protein expression was higher in the middle and late compared with the early luteal phase, while ROR1 and TLR4 expression was highest in the early luteal phase. Additionally, we observed cytoplasmic localisation of resistin, ROR1 and TLR4 in small and large luteal cells. We found that luteinising hormone, progesterone (P4), insulin and insulin-like growth factor 1 regulated the protein level of resistin, ROR1 and TLR4. Resistin decreased P4 and increased oestradiol (E2) secretion via changing in steroidogenic enzymes expression and via the activation of protein kinase A (PKA) and mitogen-activated protein kinase (MAP3/1), increased the expression of receptors LHCGR and ESR2 and decreased the expression of PGR. Moreover, resistin decreased PKA phosphorylation and enhanced MAP3/1 phosphorylation. Taken together, resistin could act directly on steroid synthesis and serve as an important factor in in vivo luteal cell function.

scholarly journals Immunoisolation and partial characterization of endothelial plasmalemmal vesicles (caveolae).

1997 ◽  
Vol 8 (4) ◽  
pp. 595-605 ◽  
Author(s):  
R V Stan ◽  
W G Roberts ◽  
D Predescu ◽  
K Ihida ◽  
L Saucan ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Silica Coating ◽  
Cell Types ◽  
Magnetic Microspheres ◽  
Physical Parameters ◽  
Cell Fractionation ◽  
Plasmalemmal Vesicles ◽  
Kinase C ◽  
And Function

Plasmalemmal vesicles (PVs) or caveolae are plasma membrane invaginations and associated vesicles of regular size and shape found in most mammalian cell types. They are particularly numerous in the continuous endothelium of certain microvascular beds (e.g., heart, lung, and muscles) in which they have been identified as transcytotic vesicular carriers. Their chemistry and function have been extensively studied in the last years by various means, including several attempts to isolate them by cell fractionation from different cell types. The methods so far used rely on nonspecific physical parameters of the caveolae and their membrane (e.g., size-specific gravity and solubility in detergents) which do not rule out contamination from other membrane sources, especially the plasmalemma proper. We report here a different method for the isolation of PVs from plasmalemmal fragments obtained by a silica-coating procedure from the rat lung vasculature. The method includes sonication and flotation of a mixed vesicle fraction, as the first step, followed by specific immunoisolation of PVs on anticaveolin-coated magnetic microspheres, as the second step. The mixed vesicle fraction, is thereby resolved into a bound subfraction (B), which consists primarily of PVs or caveolae, and a nonbound subfraction (NB) enriched in vesicles derived from the plasmalemma proper. The results so far obtained indicate that some specific endothelial membrane proteins (e.g., thrombomodulin, functional thrombin receptor) are distributed about evenly between the B and NB subfractions, whereas others are restricted to the NB subfraction (e.g., angiotensin converting enzyme, podocalyxin). Glycoproteins distribute unevenly between the two subfractions and antigens involved in signal transduction [e.g., annexin II, protein kinase C alpha, the G alpha subunits of heterotrimeric G proteins (alpha s, alpha q, alpha i2, alpha i3), small GTP-binding proteins, endothelial nitric oxide synthase, and nonreceptor protein kinase c-src] are concentrated in the NB (plasmalemma proper-enriched) subfraction rather than in the caveolae of the B subfraction. Additional work should show whether discrepancies between our findings and those already recorded in the literature represent inadequate fractionation techniques or are accounted for by chemical differentiation of caveolae from one cell type to another.

Primary Cilia Mediate Intracellular cAMP Responses in Bone Cells Exposed to Dynamic Fluid Flow

2008 ◽  
Author(s):  
Ronald Y. Kwon ◽  
Sara Temiyasathit ◽  
Padmaja Tummala ◽  
Clarence Quah ◽  
Christopher R. Jacobs
Keyword(s):  
Fluid Flow ◽  
Primary Cilia ◽  
Bone Structure ◽  
Bone Cells ◽  
Cyclic Adenosine Monophosphate ◽  
Second Messenger ◽  
Adenosine Monophosphate ◽  
Cell Types ◽  
Intracellular Camp ◽  
And Function

It is well accepted that fluid flow is an important mechanical signal in regulating bone structure and function. Primary cilia, which are non-motile, microtubule based organelles that extend from the centrosome and project into extracellular space in many cell types, have recently been shown to mediate fluid flow-induced osteogenic responses in MLO-Y4 osteocyte-like cells [1]. However, primary cilia did not mediate increases in intracellular Ca2+ concentration, and the second messenger system(s) involved in primary cilia-mediated mechanosensing has yet to be elucidated. In this study, our goals were to (1) determine whether exposing bone cells to oscillatory fluid flow modulates intracellular levels of cyclic adenosine monophosphate (cAMP), another ubiquitous second messenger molecule, and (2) investigate whether this modulation may be mediated by primary cilia.

Production and regulation of progesterone in bovine corpus luteum and placenta in mid and late gestation: a personal review

1990 ◽  
Vol 2 (2) ◽  
pp. 129 ◽  
Author(s):  
M Shemesh
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Corpus Luteum ◽  
Cyclic Nucleotide ◽  
Secretory Activity ◽  
Late Pregnancy ◽  
Second Messenger ◽  
Late Gestation ◽  
Kinase C ◽  
Bovine Corpus Luteum

In late pregnancy the secretory activity of the corpus luteum of the cow is markedly diminished. This reduced secretion is due to a decline in the number of viable luteal cells as well as reduction in the secretory activity and responsiveness of the cells to trophic agents. The principal extra-ovarian source of progesterone in late gestation appears to be the placenta, especially the fetal cotyledon, which was shown to produce progesterone throughout gestation. Uniquely, this progesterone biosynthesis is cyclic-nucleotide independent, but Ca2+ dependent. It therefore appears that the Ca2(+)-second messenger and protein kinase C systems are responsible for regulation of sterol biosynthesis in the cow placenta.

Sign in / Sign up

Export Citation Format

Share Document