Epidermal growth factor stimulates production of insulin-like growth factor-binding protein-1 in human granulosa-luteal cells

Angervo, Maarit; Koistinen, R; Seppälä, Matti

doi:10.1677/joe.0.1340127

Cited by 21 publications

(7 citation statements)

References 17 publications

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“…Thus, IGFBP-1 may play an important role in cell replication. In support of such a role, it has been shown that IGFBP-1 is the most highly induced early growth response gene expressed in regenerating liver (Mohn et al, 1990;Ghahary et al, 1992) and EGF, which is believed to play a role in liver regeneration, increases IGFBP-1 synthesis in human hepatoma cells (Angervo et al, 1992). All of these studies indicate the importance of accounting for these parameters in studies of IGFBP-1 regulation and emphasise the complexity of the mechanisms controlling IGFBP-1.…”

Section: Discussionmentioning

confidence: 96%

Interaction of insulin, glucocorticoids, and protein kinase C in the regulation of insulin-like growth factor-binding protein-1 production by H4IIE rat hepatoma cells

Lewitt¹,

Saunders²,

Baxter³

1996

J. Cell. Physiol.

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A sensitive RIA was used to examine regulation of IGFBP-1 in H4IIE rat hepatoma cells. IGFBP-1 was stimulated up to tenfold by dexamethasone and corticosterone, and this stimulation was abolished by RU486. The effect of dexamethasone increased with time in culture. Phorbol 12-myristate 13-acetate (PMA) stimulated IGFBP-1 up to fourfold with a maximal effect in short-term culture. Dexamethasone and PMA were additive in stimulating IGFBP-1. Under basal conditions IGFBP-1 production was linearly related to cell density: however, stimulation by dexamethasone was greatest in confluent cells, and PMA had a greater effect in sparse cultures. Insulin inhibited IGFBP-1 up to 80%, and this effect diminished with time in culture but was unaffected by cell density. Dexamethasone was stimulatory in the presence of a maximal inhibitory concentration of insulin, and insulin was inhibitory in the presence of maximal dexamethasone from 3-48 h in culture, regardless of cell density. PMA abolished the inhibitory action of insulin on IGFBP-1 secretion and mRNA expression during incubation periods of less than 4 h and not during longer incubations. PMA did not influence the stability of IGFBP-1 mRNA. We conclude that, in rat H4IIE cells, dexamethasone and PMA stimulate IGFBP-1 by independent mechanisms and speculate that when protein kinase C is activated the inhibitory action of insulin is blocked.

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Section: Discussionmentioning

confidence: 96%

Interaction of insulin, glucocorticoids, and protein kinase C in the regulation of insulin-like growth factor-binding protein-1 production by H4IIE rat hepatoma cells

Lewitt¹,

Saunders²,

Baxter³

1996

J. Cell. Physiol.

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“…The oocytes present in the milieu of FF, which is rich in hormones such as progesterone, FSH and luteinizing hormone (LH), are associated with follicular maturation and oocyte development [17]. Epidermal growth factor (EGF) [2], insulin-like growth factor (IGF) and transforming growth factor (TGF) [6] have been detected in follicular fluid.…”

Section: Discussionmentioning

confidence: 99%

“…However, a limitation of this study is that we are unable to attribute fertilization to oocyte quality only, although we Fig. 2 Spectral counts of heparan sulfate proteoglycan perlecan in the follicular fluids containing fertilized oocytes (fFF) and non-fertilized oocytes (nfFF) in each patient (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12) tried to minimize the influence of sperm quality using ICSI. An increased number of samples would enable the use of a proteomics analysis to identify distinctive biomarkers.…”

Section: Discussionmentioning

confidence: 99%

A proteomic analysis of human follicular fluid: comparison between fertilized oocytes and non-fertilized oocytes in the same patient

Bayasula

Iwase

Kobayashi

et al. 2013

J Assist Reprod Genet

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Purpose Human follicular fluid constitutes the microenvironment of follicles and includes various biological active proteins that can affect follicle growth and oocyte fertilization. Conducting proteomic evaluations of human follicular fluid may be helpful for identifying potential biomarkers possibly possessing a predictive value for oocyte quality and the success of in vitro fertilization. Method We performed proteomic profiling of human follicular fluids containing oocytes that were fertilized and resulted in pregnancy and follicular fluids containing oocytes that were not fertilized in the same patients undergoing intracytoplasmic sperm injection using the LTQ Orbitrap coupled with liquid chromatography-tandem mass spectrometry (LC/MS/MS) analyses. ResultsWe identified a total of 503 proteins in human follicular fluids containing fertilized and non-fertilized oocytes obtained from 12 patients. We also found that 53 proteins exhibited significantly different spectral counts between the two groups, including heparan sulfate proteoglycan perlecan, which showed significant upregulation in the follicular fluids containing fertilized oocytes in comparison with that observed in the follicular fluids containing non-fertilized oocytes. Conclusion Our results suggest a possibility that proteins identified by LC/MS/MS in follicular fluid might not only be involved in folliculogenesis, but also function as biomarkers possessing predictive potential for oocyte maturation and the success of IVF when their expression levels are significantly different between fertilized and non-fertilized oocytes, although no distinctive biomarkers were identified in the current study.

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“…EGF has been reported to exhibit luteotropic effects on cultured human GL cells by augmenting basal and hCG-and PGE 2 -stimulated progesterone production [56]. It also stimulates IGFBP-1 production in these cells [57]. As immunoreactive EGF protein has been localized to the human preovulatory follicles [58] and CL [59], it may have a physiological role in regulating the formation of the CL and FS production in the human ovary.…”

Section: Discussionmentioning

confidence: 99%

Regulation of the Activin-Binding Protein Follistatin in Cultured Human Luteinizing Granulosa Cells: Characterization of the Effects of Follicle Stimulating Hormone, Prostaglandin E2, and Different Growth Factors1

Tuuri

Ritvos

1995

Biology of Reproduction

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Regulation of the activin-binding protein follistatin (FS) by recombinant human (rh) FSH, prostaglandin E2 (PGE2), and several polypeptide growth factors was examined in cultures of human granulosa-luteal (GL) cells obtained from in-vitro fertilization patients at oocyte retrieval. Northern and dot blot hybridization analyses demonstrated that both rhFSH and PGE2 caused stimulatory effects on FS mRNA levels in a culture stage-, time-, and concentration-dependent manner. An 8-h stimulation with rhFSH (100 ng/ml) significantly increased FS mRNA levels on Days 5 and 7 of culture and PGE2 (10(-6)M) on Days 2, 4, and 7. The stimulatory effect of rhFSH and PGE2 on FS mRNA levels were rapid and transient. Maximal inductions occurred 8 h after stimulation, whereas weak or no stimulatory effects were seen at 24 or 48 h. PGF2 alpha did not affect FS mRNA levels at any time point studied. Treatment of the cells with the protein synthesis inhibitor cycloheximide prior to rhFSH stimulation did not inhibit the rapid induction of FS mRNAs, but it prevented the decline at 24 h. Both rhFSH and PGE2 clearly also increased the levels of secreted FS proteins are detected by immunoprecipitation studies with a specific antibody. The effects of the polypeptide growth factors epidermal growth factor (EGF); transforming growth factor beta 1 (TGF beta 1), and activin A on FS mRNA levels were also examined. TGF beta 1 and activin A had no effect on basal FS expression at any concentration or time point studied. An 8-h stimulation with EGF increased FS mRNA levels, but the effect was weaker than those caused by rhFSH and PGE2. We conclude that rhFSH and PGE2 induce FS mRNA and protein in human cultured GL cells. EGF is able to induce FS mRNA to a lesser extent than are rhFSH and PGE2, whereas PGF2 alpha, TGF beta 1, and activin A do not affect basal FS mRNA levels in human cultured GL cells. This study together with our previous report on the stimulatory effect of hCG on FS levels suggest that in the luteal phase of the human menstrual cycle, FS expression in granulosa cells is likely to be positively controlled by luteotropic factors such as gonadotropins and PGE2. Consequently, elevated FS levels may support the survival of the human CL since FS is known to prevent the antisteroidogenic effects of activin in human GL cells.

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Epidermal growth factor stimulates production of insulin-like growth factor-binding protein-1 in human granulosa-luteal cells

Cited by 21 publications

References 17 publications

Interaction of insulin, glucocorticoids, and protein kinase C in the regulation of insulin-like growth factor-binding protein-1 production by H4IIE rat hepatoma cells

Interaction of insulin, glucocorticoids, and protein kinase C in the regulation of insulin-like growth factor-binding protein-1 production by H4IIE rat hepatoma cells

A proteomic analysis of human follicular fluid: comparison between fertilized oocytes and non-fertilized oocytes in the same patient

Regulation of the Activin-Binding Protein Follistatin in Cultured Human Luteinizing Granulosa Cells: Characterization of the Effects of Follicle Stimulating Hormone, Prostaglandin E2, and Different Growth Factors1

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