INHBA

Inhibin, beta A
	; PDB prikaz baziran na 1nys.
Dostupne strukture
	1NYS, 1NYU, 1S4Y, 2ARP, 2ARV, 2B0U, 2P6A, 3B4V
Identifikatori
Simboli	INHBA; EDF; FRP
Vanjski ID	OMIM: 147290 MGI: 96570 HomoloGene: 1653 GeneCards: INHBA Gene
Ontologija gena
Molekularna funkcija	• citokinska aktivnost; • hormonska aktivnost; • proteinsko vezivanje;
Celularna komponenta	• ekstracelularni region; • aktivin A kompleks; • inhibin A kompleks;
Biološki proces	• G1/S promena mitotičkog ćelijskog ciklusa; • razvoj folikula jajnika; • razvoj folikula kose;
Pregled RNK izražavanja
	podaci
Ortolozi

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Inhibin, beta A (INHBA) je protein koji je kod ljudi kodiran INHBA genom.^[1] INHBA is a subunit of both activin and inhibin, two closely related glycoproteins with opposing biological effects.

Funkcija[uredi | uredi kod]

Inhibin beta A subunit zajedno sa alfa podjedinicom formira hipofizni FSH sekretorni inhibitor. Inhibin negativno reguliše proliferaciju gonadalnih stromalnih ćelija i ima supresivno dejstvo na tumour. Serumski nivoi inhibina odražavaju veličinu granulosa-ćelija tumora i mogu se koristiti kao marker za primarnu kao i rekurentnu bolest. Kod kancera prostate, izražavanje gena inhibin alfa-podjedinice je potisnuto i ne može se detektovati kod slabo diferenciranih ćelija tumora.^[2]

Interakcije[uredi | uredi kod]

INHBA formira interakcije sa ACVR2A.^[3]^[4]

Reference[uredi | uredi kod]

↑ 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: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)”.
↑ Lewis, K A; Gray P C, Blount A L, MacConell L A, Wiater E, Bilezikjian L M, Vale W (March 2000). „Betaglycan binds inhibin and can mediate functional antagonism of activin signalling”. Nature (ENGLAND) 404 (6776): 411–4. DOI:10.1038/35006129. ISSN 0028-0836. PMID 10746731.
↑ Martens, J W; de Winter J P, Timmerman M A, McLuskey A, van Schaik R H, Themmen A P, de Jong F H (July 1997). „Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells”. Endocrinology (UNITED STATES) 138 (7): 2928–36. DOI:10.1210/en.138.7.2928. ISSN 0013-7227. PMID 9202237.

Literatura[uredi | uredi kod]

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.
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. DOI:10.1016/0092-8674(91)90549-E. 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. DOI:10.3109/10425179109039678. 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. 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.
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.
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. DOI:10.1074/jbc.270.11.6308. PMID 7890768.
Mason AJ (1994). „Functional analysis of the cysteine residues of activin A”. Mol. Endocrinol. 8 (3): 325–32. DOI:10.1210/me.8.3.325. 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. DOI:10.1016/0378-1119(94)90802-8. 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. DOI:10.1074/jbc.271.51.32760. PMID 8955111.