INHBB

Last updated
INHBB
Identifiers
Aliases INHBB , inhibin beta B subunit, inhibin subunit beta B
External IDs OMIM: 147390 MGI: 96571 HomoloGene: 1654 GeneCards: INHBB
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002193

NM_008381

RefSeq (protein)

NP_002184

NP_032407

Location (UCSC) Chr 2: 120.35 – 120.35 Mb Chr 1: 119.34 – 119.35 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Inhibin, beta B, also known as INHBB, is a protein which in humans is encoded by the INHBB gene. [5] [6] INHBB is a subunit of both activin and inhibin, two closely related glycoproteins with opposing biological effects.

Contents

Function

Inhibin

Inhibins are heterodimeric glycoproteins composed of an α subunit (INHA) and one of two homologous, but distinct, β subunits (βA or βB, this protein). mRNA for the two subunits has been demonstrated in the testes of adult rats. [7] Inhibin can bind specifically to testicular interstitial cells throughout development and may be an important regulator of Leydig cell testosterone production or interstitial cell function. [8]

The inhibin beta B subunit joins the α 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. 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.

Activin

Furthermore, the beta B subunit forms a homodimer, activin B, and also joins with the beta A subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. [6]

Tissue distribution

Sections of testicular tissue from rat revealed positive immunoreactivity against anti-inhibin intensely appeared in Leydig cells. [9] In adult animals, binding of 125I inhibin was localized primarily to the interstitial compartment of the testis. [8] Also, Jin et al., (2001) reported that Leydig cells showed strong positive staining for the inhibin βA subunit in pigs testis. [10]

Receptors

In situ ligand binding studies have shown that 125I inhibin βA binds specifically to Leydig cells throughout rat testis development. These results suggest that inhibin has been considered as a regulator of Leydig cell differentiated function. [11] [12] Recently, additional inhibin specific binding proteins were identified in inhibin target tissues, including pituitary and Leydig cells. [13] [14] From these receptors betaglycan (the TGF-β type III receptor) and InhBP/p120 (a membrane-tethered proteoglycan) were identified as putative inhibin receptors and they are all present in Leydig cells. However, a faint positive reaction was detected in Leydig cell cytoplasm in rats treated with anise oil. [9] This may be related to the damaged Leydig cells, as a result of the decreasing of inhibin expression. This may be related to its content of safrole.

Cancer

INHBB gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. [15] For this reason, INHBB is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression. [15]

Related Research Articles

<span class="mw-page-title-main">Follicle-stimulating hormone</span> Gonadotropin that regulates the development of reproductive processes

Follicle-stimulating hormone (FSH) is a gonadotropin, a glycoprotein polypeptide hormone. FSH is synthesized and secreted by the gonadotropic cells of the anterior pituitary gland and regulates the development, growth, pubertal maturation, and reproductive processes of the body. FSH and luteinizing hormone (LH) work together in the reproductive system.

<span class="mw-page-title-main">Luteinizing hormone/choriogonadotropin receptor</span> Transmembrane receptor found in humans

The luteinizing hormone/choriogonadotropin receptor (LHCGR), also lutropin/choriogonadotropin receptor (LCGR) or luteinizing hormone receptor (LHR), is a transmembrane receptor found predominantly in the ovary and testis, but also many extragonadal organs such as the uterus and breasts. The receptor interacts with both luteinizing hormone (LH) and chorionic gonadotropins and represents a G protein-coupled receptor (GPCR). Its activation is necessary for the hormonal functioning during reproduction.

<span class="mw-page-title-main">Follistatin</span> Mammalian protein found in Homo sapiens

Follistatin, also known as activin-binding protein, is a protein that in humans is encoded by the FST gene. Follistatin is an autocrine glycoprotein that is expressed in nearly all tissues of higher animals.

<span class="mw-page-title-main">ACVR1B</span> Protein-coding gene in humans

Activin receptor type-1B is a protein that in humans is encoded by the ACVR1B gene.

<span class="mw-page-title-main">ACVR2A</span> Protein-coding gene in the species Homo sapiens

Activin receptor type-2A is a protein that in humans is encoded by the ACVR2A gene. ACVR2A is an activin type 2 receptor.

The activin type 2 receptors belong to a larger TGF-beta receptor family and modulate signals for transforming growth factor beta ligands. These receptors are involved in a host of physiological processes including, growth, cell differentiation, homeostasis, osteogenesis, apoptosis and many other functions. There are two activin type two receptors: ACVR2A and ACVR2B.

<span class="mw-page-title-main">ACVR2B</span> Protein-coding gene in the species Homo sapiens

Activin receptor type-2B is a protein that in humans is encoded by the ACVR2B gene. ACVR2B is an activin type 2 receptor.

<span class="mw-page-title-main">Steroidogenic factor 1</span> Protein-coding gene in humans

The steroidogenic factor 1 (SF-1) protein is a transcription factor involved in sex determination by controlling the activity of genes related to the reproductive glands or gonads and adrenal glands. This protein is encoded by the NR5A1 gene, a member of the nuclear receptor subfamily, located on the long arm of chromosome 9 at position 33.3. It was originally identified as a regulator of genes encoding cytochrome P450 steroid hydroxylases, however, further roles in endocrine function have since been discovered.

<span class="mw-page-title-main">INHBA</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">Thyroid hormone receptor beta</span> Protein-coding gene in the species Homo sapiens

Thyroid hormone receptor beta (TR-beta) also known as nuclear receptor subfamily 1, group A, member 2 (NR1A2), is a nuclear receptor protein that in humans is encoded by the THRB gene.

<span class="mw-page-title-main">INHA</span> Protein and coding gene in humans

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

<span class="mw-page-title-main">Relaxin/insulin-like family peptide receptor 2</span> Protein-coding gene in the species Homo sapiens

Relaxin/insulin-like family peptide receptor 2, also known as RXFP2, is a human G-protein coupled receptor.

<span class="mw-page-title-main">FSHB</span> Protein-coding gene in the species Homo sapiens

Follitropin subunit beta also known as follicle-stimulating hormone beta subunit (FSH-B) is a protein that in humans is encoded by the FSHB gene. Alternative splicing results in two transcript variants encoding the same protein.

<span class="mw-page-title-main">FSTL3</span> Protein-coding gene in the species Homo sapiens

Follistatin-related protein 3 is a protein that in humans is encoded by the FSTL3 gene.

Testicular Immunology is the study of the immune system within the testis. It includes an investigation of the effects of infection, inflammation and immune factors on testicular function. Two unique characteristics of testicular immunology are evident: (1) the testis is described as an immunologically privileged site, where suppression of immune responses occurs; and, (2) some factors which normally lead to inflammation are present at high levels in the testis, where they regulate the development of sperm instead of promoting inflammation.

<span class="mw-page-title-main">INHBC</span> Protein-coding gene in the species Homo sapiens

Inhibin beta C chain is a protein that in humans is encoded by the INHBC gene.

<span class="mw-page-title-main">Luteinizing hormone beta polypeptide</span> Protein-coding gene in the species Homo sapiens

Luteinizing hormone subunit beta also known as lutropin subunit beta or LHβ is a polypeptide that in association with an alpha subunit common to all gonadotropin hormones forms the reproductive signaling molecule luteinizing hormone. In humans it is encoded by the LHB gene.

<span class="mw-page-title-main">TSHB</span> Protein-coding gene in the species Homo sapiens

Thyroid stimulating hormone, beta also known as TSHB is a protein which in humans is encoded by the TSHB gene.

<span class="mw-page-title-main">Activin and inhibin</span> Regulators of feedback on FSH-production

Activin and inhibin are two closely related protein complexes that have almost directly opposite biological effects. Identified in 1986, activin enhances FSH biosynthesis and secretion, and participates in the regulation of the menstrual cycle. Many other functions have been found to be exerted by activin, including roles in cell proliferation, differentiation, apoptosis, metabolism, homeostasis, immune response, wound repair, and endocrine function. Conversely, inhibin downregulates FSH synthesis and inhibits FSH secretion. The existence of inhibin was hypothesized as early as 1916; however, it was not demonstrated to exist until Neena Schwartz and Cornelia Channing's work in the mid-1970s, after which both proteins were molecularly characterized ten years later.

<span class="mw-page-title-main">3β-Androstanediol</span> Chemical compound

3β-Androstanediol, also known as 5α-androstane-3β,17β-diol, and sometimes shortened in the literature to 3β-diol, is an endogenous steroid hormone and a metabolite of androgens like dehydroepiandrosterone (DHEA) and dihydrotestosterone (DHT).

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000163083 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000037035 - 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. 1 2 "Entrez Gene: INHBB inhibin, beta B (activin AB beta polypeptide)".
  7. Feng ZM, Bardin CW, Chen CL (June 1989). "Characterization and regulation of testicular inhibin beta-subunit mRNA". Mol. Endocrinol. 3 (6): 939–48. doi: 10.1210/mend-3-6-939 . PMID   2739657.
  8. 1 2 Krummen LA, Moore A, Woodruff TK, Covello R, Taylor R, Working P, Mather JP (April 1994). "Localization of inhibin and activin binding sites in the testis during development by in situ ligand binding". Biol. Reprod. 50 (4): 734–44. doi: 10.1095/biolreprod50.4.734 . PMID   8199254.
  9. 1 2 Ibrahim A (2008). "Correlation between fennel-or anise-oil administration and damage to the testis of adult rats". Egyptian Journal of Biology. 10: 62–76.
  10. Jin W, Arai KY, Herath CB, Kondo M, Ishi H, Tanioka Y, Watanabe G, Groome NP, Taya K (2001). "Inhibins in the male Göttingen miniature pig: Leydig cells are the predominant source of inhibin B". J. Androl. 22 (6): 953–60. doi: 10.1002/j.1939-4640.2001.tb03435.x . PMID   11700859.
  11. Lejeune H, Chuzel F, Sanchez P, Durand P, Mather JP, Saez JM (November 1997). "Stimulating effect of both human recombinant inhibin A and activin A on immature porcine Leydig cell functions in vitro". Endocrinology. 138 (11): 4783–91. doi: 10.1210/endo.138.11.5542 . PMID   9348206.
  12. Pierson TM, Wang Y, DeMayo FJ, Matzuk MM, Tsai SY, Omalley BW (July 2000). "Regulable expression of inhibin A in wild-type and inhibin alpha null mice". Mol. Endocrinol. 14 (7): 1075–85. doi: 10.1210/mend.14.7.0478 . PMID   10894156. S2CID   86195240.
  13. Chong H, Pangas SA, Bernard DJ, Wang E, Gitch J, Chen W, Draper LB, Cox ET, Woodruff TK (July 2000). "Structure and expression of a membrane component of the inhibin receptor system". Endocrinology. 141 (7): 2600–7. doi: 10.1210/endo.141.7.7540 . PMID   10875264.
  14. Bernard DJ, Chapman SC, Woodruff TK (February 2002). "Inhibin binding protein (InhBP/p120), betaglycan, and the continuing search for the inhibin receptor". Mol. Endocrinol. 16 (2): 207–12. doi: 10.1210/mend.16.2.0783 . PMID   11818494.
  15. 1 2 Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes". J Cell Physiol. 230 (4): 802–812. doi:10.1002/jcp.24808. hdl: 11392/2066612 . PMID   25205602. S2CID   24986454.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.