An Activin/Furin Regulatory Loop Modulates the Processing and Secretion of Inhibin α- and βB-Subunit Dimers in Pituitary Gonadotrope Cells

Antenos, Monica; Zhu, Jie; Jetly, Niti M.; Woodruff, Teresa K.

doi:10.1074/jbc.m804190200

Cited by 36 publications

(26 citation statements)

References 32 publications

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“…3b), and 56 kDa for free β B subunit and 27 kDa for mature β B subunit (Fig. 3c) were identified in the ovarian lysates, which is generally in accordance with previous reports [20][21][22]. It is noteworthy that the inhibin α antibody was able to detect only the precursor and that it could not detect the mature subunit as it did in other species [20].…”

Section: Expression Level Of Inhibin/activin Subunits Proteins In Wilsupporting

confidence: 76%

Immunohistochemical Localization of Inhibin/Activin Subunits in the Wild Ground Squirrel (<i>Citellus dauricus brandt</i>) Ovary

et al. 2012

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Abstract. The intraovarian function of gonadally produced inhibin and activin has been extensively studied in experimental models for decades, yet their presence and function have been rarely reported in wild rodents. With our seasonal breeding model, the wild ground squirrel, we aimed to investigate the possible roles of these peptides in the seasonal folliculogenesis. Immunohistochemical staining and Western blotting have been used to detect the cellular localization and expression patterns of inhibin/activin subunits (α, β A and β B ). In the breeding season ovary, all three subunits were present in granulosa cells, theca cells of antral follicles and interstitial cells, with the strongest immunostaining in granulosa cells. Following ovulation, the corpora lutea become a major site of inhibin/activin synthesis. In the nonbreeding season ovary, inhibin/activin α and β A subunits were weakly immunopositive in granulosa cells of early stage follicles, while β B subunit was undetectable. The expression level of inhibin/activin subunit proteins were generally higher in the ovaries of the breeding season, and then decreased to a relatively low level during the nonbreeding season. The dynamic expression of inhibin/activin subunits indicated that they might play important paracrine and/or autocrine roles during the seasonal folliculogenesis of the wild ground squirrel. Key words: Folliculogenesis, Immunohistochemistry, Inhibin/activin subunits, Ovary, Wild ground squirrel (J. Reprod. Dev. 58: [531][532][533][534][535][536] 2012) I nhibin and activin are prototypical members of the transforming growth factor β (TGFβ) superfamily of ligands and receptors, which are temporally and spatially widespread and functionally diverse [1][2][3]. Inhibin is composed of an α-subunit disulfide linked to a β subunit, and the particular isoform of inhibin is named for the β subunit present in that molecule (inhibin A, α/β A , and inhibin B, α/β B ). Activins are homodimers of the inhibin β subunits (activin A, β A /β A , activin B, β B /β B , and activin AB, β A /β B ) [4][5][6]. Biological roles for activin have been proposed in a number of reproductive organs including the gonads, pituitary, and uterus, where it regulates processes such as folliculogenesis, spermatogenesis, and pregnancy, while the primary role of inhibin appears to be antagonism of inhibin/ activin signaling in many cells, including pituitary gonadotrope FSH synthesis and ovarian theca and testicular Leydig cell androgen production [7][8][9]. In the ovary, inhibin and activin, mainly produced by granulosa cells, are thought to be involved in many intraovarian roles during folliculogenesis [10]. Activin and several other TGF-β superfamily ligands play key roles in germ cell survival, in primordial follicle assembly and in follicle growth from the preantral to midantral stages, and exert paracrine actions on theca cells to attenuate LH-dependent androgen production in small-to medium-sized antral follicles [11,12]. Changes in intrafollicular activins may contribu...

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Section: Expression Level Of Inhibin/activin Subunits Proteins In Wilsupporting

confidence: 76%

Immunohistochemical Localization of Inhibin/Activin Subunits in the Wild Ground Squirrel (<i>Citellus dauricus brandt</i>) Ovary

et al. 2012

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“…Dimerization of the bA or bB peptides with a inhibin (encoded by the Inha gene) followed by cleavage, results in heterodimeric inhibin A and inhibin B, respectively ( Fig. 1A) (Antenos et al 2008). After the pro-proteins are synthesized, the prodomains aid in folding and assembling of their mature peptides, by holding them in a dimerization-competent conformation (Gray and Mason 1990;Walton et al 2009Walton et al , 2012.…”

Section: Processing Of Ligandsmentioning

confidence: 98%

“…After the cleavage by convertases, the proand mature domains remain associated through noncovalent interactions (Antenos et al 2008(Antenos et al , 2011. Activins and inhibins are secreted from the cell in this fashion, protecting the nascent mature dimers from extracellular degradation ( Fig.…”

Section: Processing Of Ligandsmentioning

confidence: 98%

Activins and Inhibins: Roles in Development, Physiology, and Disease

Namwanje

Brown

2016

Cold Spring Harb Perspect Biol

207

175

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Since their original discovery as regulators of follicle-stimulating hormone (FSH) secretion and erythropoiesis, the TGF-β family members activin and inhibin have been shown to participate in a variety of biological processes, from the earliest stages of embryonic development to highly specialized functions in terminally differentiated cells and tissues. Herein, we present the history, structures, signaling mechanisms, regulation, and biological processes in which activins and inhibins participate, including several recently discovered biological activities and functional antagonists. The potential therapeutic relevance of these advances is also discussed.

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“…To reinforce this hypothesis, our results showed that, in the presence of FSH, exogenous activin-A down-regulates expression of inhibin ßA in cultured goat secondary follicles. In addition, ANTENOS et al (2008) demonstrated that activin-A reduces the levels of inhibin ßA and stimulates endogenous production of inhibin -and ßB-subunit mRNA in gonadotrope cells. Using PCR, inhibin-ßA mRNA expression was detected in the oocyte and somatic cells of rat secondary follicles (ZHAO et al 2001).…”

Section: Discussionmentioning

confidence: 99%

Goat ovarian follicles express different levels of mRNA for inhibin-ßA subunit and activin-A stimulates secondary follicle growth in vitro

et al. 2012

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An Activin/Furin Regulatory Loop Modulates the Processing and Secretion of Inhibin α- and βB-Subunit Dimers in Pituitary Gonadotrope Cells

Cited by 36 publications

References 32 publications

Immunohistochemical Localization of Inhibin/Activin Subunits in the Wild Ground Squirrel (<i>Citellus dauricus brandt</i>) Ovary

Immunohistochemical Localization of Inhibin/Activin Subunits in the Wild Ground Squirrel (<i>Citellus dauricus brandt</i>) Ovary

Activins and Inhibins: Roles in Development, Physiology, and Disease

Goat ovarian follicles express different levels of mRNA for inhibin-ßA subunit and activin-A stimulates secondary follicle growth in vitro

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