INHBA

From Wikipedia, the free encyclopedia

Inhibin, beta A (activin A, activin AB alpha polypeptide)

PDB rendering based on 1nys.

Available structures: 1nys, 1nyu, 1s4y, 2arp, 2arv, 2b0u, 2p6a

Identifiers

Symbol(s)

INHBA; EDF; FRP

External IDs

OMIM: 147290 MGI: 96570 HomoloGene: 1653

Gene ontology
Molecular Function:	• cytokine activity • transforming growth factor beta receptor binding • hormone activity • growth factor activity • activin inhibitor activity • identical protein binding • follistatin binding
Cellular Component:	• extracellular region • activin A complex • inhibin A complex
Biological Process:	• G1/S transition of mitotic cell cycle • skeletal development • ovarian follicle development • induction of apoptosis • defense response • cell cycle arrest • cell surface receptor linked signal transduction • cell-cell signaling • nervous system development • mesoderm development • response to external stimulus • cell differentiation • erythrocyte differentiation • negative regulation of cell growth • growth • negative regulation of phosphorylation • hemoglobin biosynthetic process • negative regulation of interferon-gamma biosynthetic process • negative regulation of B cell differentiation • positive regulation of erythrocyte differentiation • negative regulation of macrophage differentiation • positive regulation of transcription from RNA polymerase II promoter • positive regulation of follicle-stimulating hormone secretion • negative regulation of follicle-stimulating hormone secretion

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002192 (mRNA)
NP_002183 (protein)

NM_008380 (mRNA)
NP_032406 (protein)

Location

Chr 7: 41.7 - 41.71 Mb

Chr 13: 15.81 - 15.82 Mb

Pubmed search

[1]

[2]

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]

[edit] References

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

[edit] 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.