Chemical and Biological Characterization of the Inhibin Family of Protein Hormones

Vale, Wylie; Rivier, Catherine; Hsueh, Aaron J. W.; Campen, Carolyn A.; Meunier, Hélène; Bicsak, Thomas A.; Vaughan, Joan; Corrigan, A; Bardin, W.; Sawchenko, Paul E.

doi:10.1016/b978-0-12-571144-9.50005-3

Cited by 277 publications

(219 citation statements)

References 115 publications

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“…Inhibin is the only known endocrine hormone in the TGF␤ superfamily and plays an essential role in the negative feedback between the gonads and the pituitary gland that is necessary for the regulation of reproductive function (41)(42)(43)(44). In the pituitary, FSH is stimulated by locally produced activin, and ovarianderived inhibin antagonizes activin (17,42,(45)(46)(47).…”

Section: Discussionmentioning

confidence: 99%

Inhibin α-Subunit N Terminus Interacts with Activin Type IB Receptor to Disrupt Activin Signaling

Zhu

Lin

Zou

et al. 2012

Journal of Biological Chemistry

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Background:The inhibin ␤-subunit interacts with activin type II receptor to antagonize activin signaling. Results: The inhibin ␣-subunit N terminus binds ALK4 to antagonize activin signaling. Conclusion: Inhibin ␣-subunit binding to ALK4 supports potent antagonism of constitutive activin-stimulated FSH production in pituitary cells. Significance: Understanding the mechanisms underlying control of pituitary FSH synthesis may provide treatment approaches to reproductive endocrine disorders.

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Section: Discussionmentioning

confidence: 99%

Inhibin α-Subunit N Terminus Interacts with Activin Type IB Receptor to Disrupt Activin Signaling

Zhu

Lin

Zou

et al. 2012

Journal of Biological Chemistry

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“…They exert their effects through both endocrine and local (autocrine/paracrine) mechanisms [18]. Inhibins and activins are structurally related dimeric gonadal proteins with the ability to regulate follicle-stimulating hormone (FSH) secretion from the pituitary glands [26,27]. They are dimeric glycoproteins formed by two of three different subunits (α,  A and  B ).…”

mentioning

confidence: 99%

Immunolocalization of Inhibin/Activin Subunit Proteins During the Breeding Season in Testes and Scented Glands of Muskrats (Ondatra zibethicus)

Zhang

Weng

et al. 2011

J. Vet. Med. Sci.

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ABSTRACT. The objective of this study was to investigate the cellular immunolocalization of inhibin  and inhibin/activin ( A and  B ) subunits in the muskrat testes and scented glands during the breeding season. Inhibin  and inhibin/activin ( A and  B ) subunits were expressed in Sertoli cells and Leydig cells of testes and glandular cells of scented glands, respectively. Also, positive signals of inhibin  and inhibin/activin ( A and  B ) subunits by Western blotting were both observed in testicular and scented glandular tissues. These results suggested that the testes and scented glands of the muskrats had the ability to synthesize inhibins and activins and that activins and inhibins might play an important role in testicular and scented glandular function in muskrats.

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“…On the other hand, inhibin, a heterodimeric molecule composed of one of the activin ␤A or ␤B subunits linked to a distantly related ␣ subunit to produce inhibin A or B, respectively, was originally discovered as an endocrine regulator of follicle-stimulating hormone biosynthesis, being synthesized primarily in gonadal tissues and acting on pituitary gonadotrophs (reviewed in Ref. 10). Specific assays for human dimeric inhibins A and B indicate that they are differentially produced during the menstrual cycle and that alterations of inhibin concentrations are inversely associated with changes in folliclestimulating hormone concentrations in a variety of fertility abnormalities in both men and women (reviewed in Ref.…”

mentioning

confidence: 99%

Reconstitution and Analysis of Soluble Inhibin and Activin Receptor Complexes in a Cell-free System

Re¹,

Sidis

Fabrizio³

et al. 2004

Journal of Biological Chemistry

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Activins and inhibins compose a heterogeneous subfamily within the transforming growth factor-␤ (TGF-␤) superfamily of growth and differentiation factors with critical biological activities in embryos and adults. They signal through a heteromeric complex of type II, type I, and for inhibin, type III receptors. To characterize the affinity, specificity, and activity of these receptors (alone and in combination) for the inhibin/activin subfamily, we developed a cell-free assay system using soluble receptor-Fc fusion proteins. The soluble activin type II receptor (sActRII)-Fc fusion protein had a 7-fold higher affinity for activin A compared with sActRIIB-Fc, whereas both receptors had a marked preference for activin A over activin B. Although inhibin A and B binding was 20-fold lower compared with activin binding to either type II receptor alone, the mixture of either type II receptor with soluble TGF-␤ type III receptor (T␤RIII; betaglycan)-Fc reconstituted a soluble high affinity inhibin receptor. In contrast, mixing either soluble activin type II receptor with soluble activin type I receptors did not substantially enhance activin binding. Our results support a cooperative model of binding for the inhibin receptor (ActRII⅐sT␤RIII complex) but not for activin receptors (type II ؉ type I) and demonstrate that a complex composed of activin type II receptors and T␤RIII is both necessary and sufficient for high affinity inhibin binding. This study also illustrates the utility of this cell-free system for investigating hypotheses of receptor complex mechanisms resulting from crystal structure analyses.

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Chemical and Biological Characterization of the Inhibin Family of Protein Hormones

Cited by 277 publications

References 115 publications

Inhibin α-Subunit N Terminus Interacts with Activin Type IB Receptor to Disrupt Activin Signaling

Inhibin α-Subunit N Terminus Interacts with Activin Type IB Receptor to Disrupt Activin Signaling

Immunolocalization of Inhibin/Activin Subunit Proteins During the Breeding Season in Testes and Scented Glands of Muskrats (Ondatra zibethicus)

Reconstitution and Analysis of Soluble Inhibin and Activin Receptor Complexes in a Cell-free System

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