INHBA

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Inhibin, beta A (activin A, activin AB alpha polypeptide)
File:PBB Protein INHBA image.jpg
PDB rendering based on 1nys.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols INHBA ; EDF; FRP
External IDs Template:OMIM5 Template:MGI HomoloGene1653
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Inhibin, beta A (activin A, activin AB alpha polypeptide), also known as INHBA, is a human gene.

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 severalfold 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.[1]

References

  1. "Entrez Gene: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)".

Further reading

  • Munz B, Hübner G, Tretter Y; et al. (1999). "A novel role of activin in inflammation and repair". J. Endocrinol. 161 (2): 187–93. PMID 10320815.
  • Welt C, Sidis Y, Keutmann H, Schneyer A (2002). "Activins, inhibins, and follistatins: from endocrinology to signaling. A paradigm for the new millennium". Exp. Biol. Med. (Maywood). 227 (9): 724–52. PMID 12324653.
  • Shav-Tal Y, Zipori D (2003). "The role of activin a in regulation of hemopoiesis". Stem Cells. 20 (6): 493–500. PMID 12456957.
  • Reis FM, Luisi S, Carneiro MM; et al. (2005). "Activin, inhibin and the human breast". Mol. Cell. Endocrinol. 225 (1–2): 77–82. doi:10.1016/j.mce.2004.02.016. PMID 15451571.
  • Shao L, Frigon NL, Young AL; et al. (1992). "Effect of activin A on globin gene expression in purified human erythroid progenitors". Blood. 79 (3): 773–81. PMID 1310063.
  • Mathews LS, Vale WW (1991). "Expression cloning of an activin receptor, a predicted transmembrane serine kinase". Cell. 65 (6): 973–82. PMID 1646080.
  • Tanimoto K, Handa S, Ueno N; et al. (1992). "Structure and sequence analysis of the human activin beta A subunit gene". DNA Seq. 2 (2): 103–10. PMID 1777673.
  • Mason AJ, Berkemeier LM, Schmelzer CH, Schwall RH (1990). "Activin B: precursor sequences, genomic structure and in vitro activities". Mol. Endocrinol. 3 (9): 1352–8. PMID 2575216.
  • Barton DE, Yang-Feng TL, Mason AJ; et al. (1989). "Mapping of genes for inhibin subunits alpha, beta A, and beta B on human and mouse chromosomes and studies of jsd mice". Genomics. 5 (1): 91–9. PMID 2767687.
  • Murata M, Eto Y, Shibai H; et al. (1988). "Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain". Proc. Natl. Acad. Sci. U.S.A. 85 (8): 2434–8. PMID 3267209.
  • Burger HG, Igarashi M (1988). "Inhibin: definition and nomenclature, including related substances". Endocrinology. 122 (4): 1701–2. PMID 3345731.
  • Mason AJ, Niall HD, Seeburg PH (1986). "Structure of two human ovarian inhibins". Biochem. Biophys. Res. Commun. 135 (3): 957–64. PMID 3754442.
  • Stewart AG, Milborrow HM, Ring JM; et al. (1986). "Human inhibin genes. Genomic characterisation and sequencing". FEBS Lett. 206 (2): 329–34. PMID 3758355.
  • Sumitomo S, Inouye S, Liu XJ; et al. (1995). "The heparin binding site of follistatin is involved in its interaction with activin". Biochem. Biophys. Res. Commun. 208 (1): 1–9. doi:10.1006/bbrc.1995.1297. PMID 7887917.
  • Xu J, McKeehan K, Matsuzaki K, McKeehan WL (1995). "Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism". J. Biol. Chem. 270 (11): 6308–13. PMID 7890768.
  • Mason AJ (1994). "Functional analysis of the cysteine residues of activin A.". Mol. Endocrinol. 8 (3): 325–32. PMID 8015550.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Nishihara T, Okahashi N, Ueda N (1994). "Activin A induces apoptotic cell death". Biochem. Biophys. Res. Commun. 197 (2): 985–91. doi:10.1006/bbrc.1993.2576. PMID 8267637.
  • ten Dijke P, Ichijo H, Franzén P; et al. (1993). "Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity". Oncogene. 8 (10): 2879–87. PMID 8397373.
  • Tanimoto K, Yoshida E, Mita S; et al. (1997). "Human activin betaA gene. Identification of novel 5' exon, functional promoter, and enhancers". J. Biol. Chem. 271 (51): 32760–9. PMID 8955111.

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