INHA

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Inhibin, alfa
Identifikatori
SimbolINHA
Vanjski IDOMIM: 147380 MGI: 96569 HomoloGene: 1652 GeneCards: INHA Gene
Ontologija gena
Molekularna funkcija receptorsko vezivanje
citokinska aktivnost
hormonska aktivnost
Celularna komponenta fotoreceptorski spoljašnji segment
fotoreceptorski unutrašnji segment
ekstracelularni region
Biološki proces razviće skeletalnog sistema
razviće folikula jajnika
indukcija apoptoze
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez362316322
EnsemblENSG00000123999ENSMUSG00000032968
UniProtP05111Q04997
RefSeq (mRNA)NM_002191.3NM_010564.4
RefSeq (protein)NP_002182.1NP_034694.3
Lokacija (UCSC)Chr 2:
220.43 - 220.44 Mb
Chr 1:
75.51 - 75.51 Mb
PubMed pretraga[1][2]

Inhibin, alfa (INHA) je protein koji je kod ljudi kodiran INHA genom.[1]

Funkcija

Inhibin alfa podjedinica zajedno sa još jednom beta A ili beta B 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]

Reference

  1. 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. 
  2. „Entrez Gene: INHA inhibin, alpha”. 

Literatura

  • Mellor SL, Richards MG, Pedersen JS i dr.. (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 i dr.. (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 i dr.. (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 i dr.. (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 i dr.. (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 i dr.. (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 i dr.. (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 i dr.. (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 i dr.. (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 i dr.. (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. 

Povezano

  • p
  • r
  • u
Endokrine
žlezde
Hipotalamusno-
hipofizni
Druge endokrine
žlezde
Neendokrine
žlezde

M: END

anat/phys/devp/horm/cell

noco(d)/cong/tumr, sysi/epon

proc, lek (A10/H1/H2/H3/H5)