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Reciprocal stimulating effects of bFGF and FSH on chicken primordial follicle activation through AKT and ERK pathway.

08:00 EDT 6th April 2019 | BioPortfolio

Summary of "Reciprocal stimulating effects of bFGF and FSH on chicken primordial follicle activation through AKT and ERK pathway."

Basic fibroblast growth factor (bFGF) and follicle-stimulating hormone (FSH) both play important roles in primordial follicle development. Here we investigated the reciprocal stimulation effects of a cytokine bFGF and FSH on primordial follicle development in the chicken and considered a possible signaling mechanism involving protein kinase B (AKT) and extracellular regulated protein kinase (ERK) pathways. 4-day-old chicken ovaries were treated with bFGF and FSH for 3 days in culture to investigate the effects of bFGF and FSH on primordial follicle development. Methods included HE staining, immunohistochemistry, quantitate real-time PCR, Western blot and immunofluorescence. A correlated change of bFGF receptor (FGFR1) mRNA expression and time course of primordial follicle activation was revealed in the early chick ovaries. A reciprocal stimulation effect on primordial follicle activation was demonstrated for bFGF and FSH, along with accelerated granulosa cells proliferation and decreased cell apoptosis. The promoting effect of bFGF was attenuated by the FGFR1 inhibitor SU5402 where the percentage of growing follicles had decreased. AKT and ERK signaling pathways mediated the action of bFGF and FSH in their promotion of primordial follicle activation. Cytokine bFGF and FSH imposed reciprocal stimulating effects on granulosa cell proliferation and anti-apoptosis to promote primordial follicle activation via the PI3K-AKT and ERK signaling pathways in early chick ovaries.

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This article was published in the following journal.

Name: Theriogenology
ISSN: 1879-3231
Pages: 27-35

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Medical and Biotech [MESH] Definitions

The beta subunit of follicle stimulating hormone. It is a 15-kDa glycopolypeptide. Full biological activity of FSH requires the non-covalently bound heterodimers of an alpha and a beta subunit. Mutation of the FSHB gene causes delayed puberty, or infertility.

Receptors with a 6-kDa protein on the surfaces of cells that secrete LUTEINIZING HORMONE or FOLLICLE STIMULATING HORMONE, usually in the adenohypophysis. LUTEINIZING HORMONE-RELEASING HORMONE binds to these receptors, is endocytosed with the receptor and, in the cell, triggers the release of LUTEINIZING HORMONE or FOLLICLE STIMULATING HORMONE by the cell. These receptors are also found in rat gonads. INHIBINS prevent the binding of GnRH to its receptors.

A major gonadotropin secreted by the adenohypophysis (PITUITARY GLAND, ANTERIOR). Follicle-stimulating hormone stimulates GAMETOGENESIS and the supporting cells such as the ovarian GRANULOSA CELLS, the testicular SERTOLI CELLS, and LEYDIG CELLS. FSH consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity.

A major gonadotropin secreted by the human adenohypophysis (PITUITARY GLAND, ANTERIOR). Follicle-stimulating hormone stimulates GAMETOGENESIS and the supporting cells such as the ovarian GRANULOSA CELLS, the testicular SERTOLI CELLS, and the LEYDIG CELLS. FSH consists of two noncovalently linked subunits, alpha and beta. The alpha subunit is common in the three human pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity.

Glycoproteins that inhibit pituitary FOLLICLE STIMULATING HORMONE secretion. Inhibins are secreted by the Sertoli cells of the testes, the granulosa cells of the ovarian follicles, the placenta, and other tissues. Inhibins and ACTIVINS are modulators of FOLLICLE STIMULATING HORMONE secretions; both groups belong to the TGF-beta superfamily, as the TRANSFORMING GROWTH FACTOR BETA. Inhibins consist of a disulfide-linked heterodimer with a unique alpha linked to either a beta A or a beta B subunit to form inhibin A or inhibin B, respectively

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