Androgen-binding protein

Last updated
Androgen-binding protein, Sex hormone-binding globulin
Identifiers
SymbolSHBG
Alt. symbolsABP
NCBI gene 6462
HGNC 10839
OMIM 182205
RefSeq NM_001040
UniProt P04278
Other data
Locus Chr. 17 p13-p12

Androgen-binding protein (ABP) is a glycoprotein (beta-globulin) produced by the Sertoli cells [1] in the seminiferous tubules [2] of the testis that binds specifically to testosterone (T), dihydrotestosterone (DHT), and 17-beta-estradiol.

Contents

Because ABP binds to T and DHT, these hormones are made less lipophilic and become concentrated within the luminal fluid of the seminiferous tubules. The higher levels of these hormones enable spermatogenesis in the seminiferous tubules and sperm maturation in the epididymis.

ABP has the same amino acid sequence as sex hormone-binding globulin (SHBG); the difference is the site of production and the addition of different sugar moieties. ABP contains 403 amino acids, resulting in a molecular weight of 44,533. Its gene is located on chromosome 17.

ABP’s production is regulated under the influence of FSH [2] on Sertoli cells, enhanced by insulin, retinol, and testosterone.

The human ABP is not to be confused with a mouse secretoglobin of the same name, which is produced in the saliva.

See also

Related Research Articles

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7α-Thioprogesterone

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Peritubular myoid cell Smooth muscle cell found in testis

A peritubular myoid (PTM) cell is one of the smooth muscle cells which surround the seminiferous tubules in the testis. These cells are present in all mammals but their organization and abundance varies between species. The exact role of PTM cells is still somewhat uncertain and further work into this is needed. However, a number of functions of these cells have been established. They are contractile cells which contain actin filaments and are primarily involved in transport of spermatozoa through the tubules. They provide structural integrity to the tubules through their involvement in laying down the basement membrane. This has also been shown to affect Sertoli cell function and PTM cells also communicate with Sertoli cells through the secretion of growth factors and ECM components. Studies have shown PTM cells to be critical in achieving normal spermatogenesis. Overall, PTM cells have a role in both maintaining the structure of the tubules and regulating spermatogenesis through cellular interaction.

5α-Dihydroethisterone

5α-Dihydroethisterone is an active metabolite of the formerly clinically used but now-discontinued progestin ethisterone and the experimental and never-marketed hormonal antineoplastic agent ethynylandrostanediol (HE-3235). Its formation from its parent drugs is catalyzed by 5α-reductase in tissues that express the enzyme in high amounts like the liver, skin, hair follicles, and prostate gland. 5α-DHET has significant affinity for steroid hormone receptors and may contribute importantly to the activities of its parent drugs.

References

  1. Bardin CW, Musto N, Gunsalus G, Kotite N, Cheng SL, Larrea F, Becker R (1981). "Extracellular androgen binding proteins". Annual Review of Physiology. 43: 189–98. doi:10.1146/annurev.ph.43.030181.001201. PMID   7011179.
  2. 1 2 Hansson V, Weddington SC, French FS, McLean W, Smith A, Nayfeh SN, Ritzén EM, Hagenäs L (September 1976). "Secretion and role of androgen-binding proteins in the testis and epididymis". Journal of Reproduction and Fertility. Supplement (24 suppl): 17–33. PMID   1069850.