INHA

Protein and coding gene in humans
INHA
Identifiers
AliasesINHA, inhibin alpha subunit, inhibin subunit alpha
External IDsOMIM: 147380 MGI: 96569 HomoloGene: 1652 GeneCards: INHA
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for INHA
Genomic location for INHA
Band2q35Start219,569,162 bp[1]
End219,575,711 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for INHA
Genomic location for INHA
Band1 C4|1 39.16 cMStart75,483,721 bp[2]
End75,487,010 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right adrenal gland

  • left adrenal gland

  • placenta

  • nucleus accumbens

  • body of pancreas

  • anterior pituitary

  • caudate nucleus

  • putamen

  • stromal cell of endometrium

  • right lobe of thyroid gland
Top expressed in
  • cumulus cell

  • ovary

  • testicle

  • seminiferous tubule

  • superior frontal gyrus

  • spermatocyte

  • adrenal gland

  • islet of Langerhans

  • cerebellar cortex

  • uterine tube
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • cytokine activity
  • hormone activity
  • protein binding
  • protein heterodimerization activity
  • transforming growth factor beta receptor binding
  • growth factor activity
  • signaling receptor binding
  • inhibin binding
Cellular component
  • cytoplasm
  • inhibin-betaglycan-ActRII complex
  • photoreceptor inner segment
  • photoreceptor outer segment
  • extracellular region
  • neuronal cell body
  • inhibin A complex
  • inhibin B complex
  • extracellular space
Biological process
  • regulation of apoptotic process
  • skeletal system development
  • cell differentiation
  • male gonad development
  • regulation of MAPK cascade
  • SMAD protein signal transduction
  • cell development
  • negative regulation of macrophage differentiation
  • cell-cell signaling
  • positive regulation of pathway-restricted SMAD protein phosphorylation
  • negative regulation of cell cycle
  • positive regulation of follicle-stimulating hormone secretion
  • regulation of cell cycle
  • cell surface receptor signaling pathway
  • regulation of cell population proliferation
  • hemoglobin biosynthetic process
  • negative regulation of B cell differentiation
  • ovarian follicle development
  • erythrocyte differentiation
  • negative regulation of follicle-stimulating hormone secretion
  • negative regulation of phosphorylation
  • signal transduction
  • BMP signaling pathway
  • regulation of signaling receptor activity
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3623

16322

Ensembl

ENSG00000123999

ENSMUSG00000032968

UniProt

P05111

Q04997

RefSeq (mRNA)

NM_002191

NM_010564
NM_001329843

RefSeq (protein)

NP_002182

NP_001316772
NP_034694

Location (UCSC)Chr 2: 219.57 – 219.58 MbChr 1: 75.48 – 75.49 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Inhibin, alpha, also known as INHA, is a protein which in humans is encoded by the INHA gene.[5]

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.[6]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000123999 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032968 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ "Entrez Gene: INHA inhibin, alpha".

Further reading

  • Mellor SL, Richards MG, Pedersen JS, Robertson DM, Risbridger GP (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/jcem.83.3.4640. PMID 9506758.
  • Munz B, Hübner G, Tretter Y, Alzheimer C, Werner S (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. doi:10.1177/153537020222700905. PMID 12324653. S2CID 19795772.
  • 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. S2CID 36242096.
  • Shao L, Frigon NL, Young AL, Yu AL, Mathews LS, Vaughan J, et al. (1992). "Effect of activin A on globin gene expression in purified human erythroid progenitors". Blood. 79 (3): 773–81. doi:10.1182/blood.V79.3.773.bloodjournal793773. PMID 1310063.
  • Vannelli GB, Barni T, Forti G, Negro-Vilar A, Vale W, Serio M, 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, Hsueh AJ, Bradley A (1992). "Alpha-inhibin is a tumour-suppressor gene with gonadal specificity in mice". Nature. 360 (6402): 313–9. Bibcode:1992Natur.360..313M. doi:10.1038/360313a0. PMID 1448148. S2CID 4327163.
  • 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, Seeburg P, Francke U (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, Bangah M, Krans M, De Bruijn HW (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, Rivier J, Rosenfeld MG, Evans RM, et al. (1986). "Inhibin A-subunit cDNAs from porcine ovary and human placenta". Proc. Natl. Acad. Sci. U.S.A. 83 (16): 5849–53. Bibcode:1986PNAS...83.5849M. 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. Bibcode:1987PNAS...84.3595R. doi:10.1073/pnas.84.11.3595. PMC 304921. PMID 3035540.
  • Murata M, Eto Y, Shibai H, Sakai M, Muramatsu M (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. Bibcode:1988PNAS...85.2434M. 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, Crowther C, Forage R (1986). "Human inhibin genes. Genomic characterisation and sequencing". FEBS Lett. 206 (2): 329–34. doi:10.1016/0014-5793(86)81006-7. PMID 3758355. S2CID 21261385.
  • 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/mend.10.9.8885240. PMID 8885240.
  • v
  • t
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TGFβ receptor superfamily modulators
Type I
ALK1 (ACVRL1)
  • Kinase inhibitors: K-02288
  • ML-347 (LDN-193719, VU0469381)
  • Other inhibitors: Disitertide
ALK2 (ACVR1A)
  • Kinase inhibitors: DMH-1
  • DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
  • ML-347 (LDN-193719, VU0469381)
ALK3 (BMPR1A)
  • Kinase inhibitors: DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
ALK4 (ACVR1B)
  • Kinase inhibitors: A 83-01
  • SB-431542
  • SB-505124
ALK5 (TGFβR1)
ALK6 (BMPR1B)
  • Kinase inhibitors: DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
ALK7 (ACVR1C)
  • Antagonists: Lefty (1, 2)
  • Kinase inhibitors: A 83-01
  • SB-431542
  • SB-505124
Type II
TGFβR2
  • Kinase inhibitors: DMH-2
  • LY-364947
BMPR2
ACVR2A (ACVR2)
ACVR2B
  • Decoy receptors: Ramatercept
AMHR2 (AMHR)
Type III
TGFβR3 (β-glycan)
Unsorted


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