Further evidence for distinction between sex hormone-binding globulin and an androgen-binding protein in hydatidiform mole serum.
We further studied the androgen-binding protein (ABP) that we recently evidenced in the serum from two patients with hydatidiform mole [Ref. 4]. This protein was further shown to be distinct from the sex hormone-binding globulin (SHBG) by concanavalin A and ion-exchange chromatographies, as well as spectrophotometric and kinetic studies. However, the ABP was shown to have a molecular weight and relative affinities for several steroids, similar to those of SHBG. Our results lead us to suppose that the ABP previously evidenced in molar vesicles and fluid [Ref. 5] is secreted in the serum. It is, however, likely that the secretion process alters the binding affinity of this protein. The presence of this additional binding component in the serum of patients with such trophoblastic tumours, may reduce severely the free 17 beta-hydroxyandrogens levels, as well as may help create a release gradient in the serum steroids buffer stores.
D000727:Androgen-Binding Protein / Q000097:blood*; D002352:Carrier Proteins / Q000097:blood*; D002845:Chromatography; D003208:Concanavalin A; D013196:Dihydrotestosterone / Q000378:metabolism; D005260:Female; D012739:Gonadal Steroid Hormones / Q000378:metabolism; D006801:Humans; D006828:Hydatidiform Mole / Q000097:blood*; D011247:Pregnancy; D011374:Progesterone / Q000378:metabolism; D012738:Sex Hormone-Binding Globulin / Q000378:metabolism*; D013053:Spectrophotometry; D014594:Uterine Neoplasms / Q000097:blood*
D000727:Androgen-Binding Protein; D002352:Carrier Proteins; D012739:Gonadal Steroid Hormones; D012738:Sex Hormone-Binding Globulin; D013196:Dihydrotestosterone; D003208:Concanavalin A; D011374:Progesterone