INHBA

The inhibin beta A subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary several fold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome.{{cite web | title = Entrez Gene: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3624}}

INHBA has been shown to interact with ACVR2A.{{cite journal |last=Lewis |first=K A |author2=Gray P C |author3=Blount A L |author4=MacConell L A |author5=Wiater E |author6=Bilezikjian L M |author7=Vale W |date=March 2000|title=Betaglycan binds inhibin and can mediate functional antagonism of activin signalling |journal=Nature |volume=404 |issue=6776 |pages=411–4 |location = ENGLAND| issn = 0028-0836| pmid = 10746731 |doi = 10.1038/35006129 |bibcode=2000Natur.404..411L |s2cid=4393629 }}{{cite journal |last=Martens |first=J W |author2=de Winter J P |author3=Timmerman M A |author4=McLuskey A |author5=van Schaik R H |author6=Themmen A P |author7=de Jong F H |date=July 1997|title=Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells |journal=Endocrinology |volume=138 |issue=7 |pages=2928–36 |location = UNITED STATES| issn = 0013-7227| pmid = 9202237 |doi=10.1210/endo.138.7.5250 |url=https://repub.eur.nl/pub/8700/9202237.pdf |doi-access=free }}

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• {{cite journal |vauthors=Welt C, Sidis Y, Keutmann H, Schneyer A |title=Activins, inhibins, and follistatins: from endocrinology to signaling. A paradigm for the new millennium. |journal=Exp. Biol. Med. (Maywood) |volume=227 |issue= 9 |pages= 724–52 |year= 2002 |pmid= 12324653 |doi= 10.1177/153537020222700905|s2cid=19795772 }}
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• {{cite journal |vauthors=Barton DE, Yang-Feng TL, Mason AJ, etal |title=Mapping of genes for inhibin subunits alpha, beta A, and beta B on human and mouse chromosomes and studies of jsd mice |journal=Genomics |volume=5 |issue= 1 |pages= 91–9 |year= 1989 |pmid= 2767687 |doi=10.1016/0888-7543(89)90091-8 |doi-access=free }}
• {{cite journal |vauthors=Murata M, Eto Y, Shibai H, etal |title=Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 8 |pages= 2434–8 |year= 1988 |pmid= 3267209 |doi=10.1073/pnas.85.8.2434 | pmc=280011 |bibcode=1988PNAS...85.2434M |doi-access=free }}
• {{cite journal |vauthors=Burger HG, Igarashi M |title=Inhibin: definition and nomenclature, including related substances |journal=Endocrinology |volume=122 |issue= 4 |pages= 1701–2 |year= 1988 |pmid= 3345731 |doi=10.1210/endo-122-4-1701 }}
• {{cite journal |vauthors=Mason AJ, Niall HD, Seeburg PH |title=Structure of two human ovarian inhibins |journal=Biochem. Biophys. Res. Commun. |volume=135 |issue= 3 |pages= 957–64 |year= 1986 |pmid= 3754442 |doi=10.1016/0006-291X(86)91021-1 }}
• {{cite journal |vauthors=Stewart AG, Milborrow HM, Ring JM, etal |title=Human inhibin genes. Genomic characterisation and sequencing |journal=FEBS Lett. |volume=206 |issue= 2 |pages= 329–34 |year= 1986 |pmid= 3758355 |doi=10.1016/0014-5793(86)81006-7 |s2cid=21261385 |doi-access=free }}
• {{cite journal |vauthors=Sumitomo S, Inouye S, Liu XJ, etal |title=The heparin binding site of follistatin is involved in its interaction with activin |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 1 |pages= 1–9 |year= 1995 |pmid= 7887917 |doi= 10.1006/bbrc.1995.1297 }}
• {{cite journal |vauthors=Xu J, McKeehan K, Matsuzaki K, McKeehan WL |title=Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism |journal=J. Biol. Chem. |volume=270 |issue= 11 |pages= 6308–6313 |year= 1995 |pmid= 7890768 |doi=10.1074/jbc.270.11.6308 |doi-access=free }}
• {{cite journal | author=Mason AJ |title=Functional analysis of the cysteine residues of activin A |journal=Mol. Endocrinol. |volume=8 |issue= 3 |pages= 325–32 |year= 1994 |doi=10.1210/mend.8.3.8015550 |pmid= 8015550 |s2cid=7615672 |doi-access=free }}
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• {{cite journal |vauthors=Nishihara T, Okahashi N, Ueda N |title=Activin A induces apoptotic cell death |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 2 |pages= 985–91 |year= 1994 |pmid= 8267637 |doi= 10.1006/bbrc.1993.2576 }}
• {{cite journal |vauthors=ten Dijke P, Ichijo H, Franzén P, etal |title=Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity |journal=Oncogene |volume=8 |issue= 10 |pages= 2879–87 |year= 1993 |pmid= 8397373 }}
• {{cite journal |vauthors=Tanimoto K, Yoshida E, Mita S, etal |title=Human activin betaA gene. Identification of novel 5' exon, functional promoter, and enhancers |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 32760–9 |year= 1997 |pmid= 8955111 |doi=10.1074/jbc.271.51.32760 |doi-access=free }}

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{{TGFβ receptor superfamily modulators}}

{{PDB Gallery|geneid=3624}}

sr:INHBB