INHA

From Wikipedia, the free encyclopedia

Inhibin, alpha

Identifiers

External IDs

OMIM: 147380 MGI: 96569 HomoloGene: 1652

Gene ontology
Molecular Function:	• cytokine activity • hormone activity • growth factor activity • activin inhibitor activity
Cellular Component:	• extracellular region • inhibin A complex
Biological Process:	• skeletal development • ovarian follicle development • induction of apoptosis • cell cycle arrest • cell surface receptor linked signal transduction • cell-cell signaling • nervous system development • response to external stimulus • cell differentiation • erythrocyte differentiation • regulation of cell proliferation • negative regulation of phosphorylation • hemoglobin biosynthetic process • negative regulation of interferon-gamma biosynthetic process • negative regulation of B cell differentiation • negative regulation of macrophage differentiation • positive regulation of follicle-stimulating hormone secretion • negative regulation of follicle-stimulating hormone secretion • regulation of cell cycle

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002191 (mRNA)
NP_002182 (protein)

NM_010564 (mRNA)
NP_034694 (protein)

Location

Chr 2: 220.15 - 220.15 Mb

Chr 1: 75.39 - 75.39 Mb

Pubmed search

[1]

[2]

Inhibin, alpha, also known as INHA, is a human gene.

The inhibin alpha subunit joins either the beta A or beta B subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumour-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. However, in prostate cancer, expression of the inhibin alpha-subunit gene was suppressed and was not detectable in poorly differentiated tumor cells. Furthermore, 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.^[1]

[edit] See also

Inhibin

[edit] References

^ Entrez Gene: INHA inhibin, alpha.

[edit] Further reading

Mellor SL, Richards MG, Pedersen JS, et al. (1998). "Loss of the expression and localization of inhibin alpha-subunit in high grade prostate cancer.". J. Clin. Endocrinol. Metab. 83 (3): 969–75. PMID 9506758.
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.
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.
Vannelli GB, Barni T, Forti G, et al. (1992). "Immunolocalization of inhibin alpha-subunit in the human testis. A light- and electron-microscopy study.". Cell Tissue Res. 269 (2): 221–7. PMID 1423490.
Matzuk MM, Finegold MJ, Su JG, et al. (1992). "Alpha-inhibin is a tumour-suppressor gene with gonadal specificity in mice.". Nature 360 (6402): 313–9. doi:10.1038/360313a0. PMID 1448148.
Shimonaka M, Inouye S, Shimasaki S, Ling N (1991). "Follistatin binds to both activin and inhibin through the common subunit.". Endocrinology 128 (6): 3313–5. PMID 2036994.
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.
Lappöhn RE, Burger HG, Bouma J, et al. (1989). "Inhibin as a marker for granulosa-cell tumors.". N. Engl. J. Med. 321 (12): 790–3. PMID 2770810.
Mayo KE, Cerelli GM, Spiess J, et al. (1986). "Inhibin A-subunit cDNAs from porcine ovary and human placenta.". Proc. Natl. Acad. Sci. U.S.A. 83 (16): 5849–53. PMID 3016724.
Ramasharma K, Li CH (1987). "Characteristics of binding of human seminal alpha-inhibin-92 to human pituitary membranes.". Proc. Natl. Acad. Sci. U.S.A. 84 (11): 3595–8. PMID 3035540.
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.
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.
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.
Mason AJ, Farnworth PG, Sullivan J (1997). "Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A.". Mol. Endocrinol. 10 (9): 1055–65. PMID 8885240.