
Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
INHA
Introduction
Inhibin, alpha, also known as INHA, is a protein which in humans is encoded by the INHA gene.[1]
Function
Function
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.[2]
References
References
- ↑ Burger HG, Igarashi M (April 1988). “Inhibin: definition and nomenclature, including related substances”. Endocrinology. 122 (4): 1701–2. doi:10.1210/endo-122-4-1701. PMID 3345731.
- ↑ “Entrez Gene: INHA inhibin, alpha”.
Further reading
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. doi:10.1210/jc.83.3.969. 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. doi:10.1677/joe.0.1610187. 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. doi:10.1634/stemcells.20-6-493. 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. doi:10.1007/bf00319612. 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. doi:10.1210/endo-128-6-3313. 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. doi:10.1210/mend-3-9-1352. 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. doi:10.1016/0888-7543(89)90091-8. 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. doi:10.1056/NEJM198909213211204. 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. doi:10.1073/pnas.83.16.5849. PMC 386393. 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. doi:10.1073/pnas.84.11.3595. PMC 304921. 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. doi:10.1073/pnas.85.8.2434. PMC 280011. PMID 3267209.
- Burger HG, Igarashi M (1988). “Inhibin: definition and nomenclature, including related substances”. Endocrinology. 122 (4): 1701–2. doi:10.1210/endo-122-4-1701. PMID 3345731.
- Mason AJ, Niall HD, Seeburg PH (1986). “Structure of two human ovarian inhibins”. Biochem. Biophys. Res. Commun. 135 (3): 957–64. doi:10.1016/0006-291X(86)91021-1. PMID 3754442.
- Stewart AG, Milborrow HM, Ring JM, et al. (1986). “Human inhibin genes. Genomic characterisation and sequencing”. FEBS Lett. 206 (2): 329–34. doi:10.1016/0014-5793(86)81006-7. 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. doi:10.1074/jbc.270.11.6308. 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. doi:10.1210/me.10.9.1055. PMID 8885240.
