INHBA

Inhibin, beta A

PDB rendering based on 1nys.
Identifiers
Symbols INHBA; EDF; FRP
External IDs OMIM147290 MGI96570 HomoloGene1653 GeneCards: INHBA Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 3624 16323
Ensembl ENSG00000122641 ENSMUSG00000041324
UniProt P08476 Q3UXL8
RefSeq (mRNA) NM_002192 NM_008380.1
RefSeq (protein) NP_002183 NP_032406.1
Location (UCSC) Chr 7:
41.72 – 41.74 Mb
Chr 13:
16.1 – 16.12 Mb
PubMed search [1] [2]

Inhibin, beta A, also known as INHBA, is a protein which in humans is encoded by the INHBA gene.[1] INHBA is a subunit of both activin and inhibin, two closely related glycoproteins with opposing biological effects.

Contents

[hide]

Function

The inhibin beta A subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-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. 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. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome.[2]

Interactions

INHBA has been shown to interact with ACVR2A.[3][4]

References

  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: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3624. 
  3. ^ 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. 
  4. ^ 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. 

Further reading