Relative cellular distribution of particulate androgen binding between Sertoli and germ cells in rat testis.
An androgen binding activity with characteristics similar to ABP is present in a particulate fraction (105,000 g pellet) obtained by differential centrifugation of seminiferous tubules, impure Sertoli cells and impure germ cells homogenates. Purification of germ cells through albumin gradients, results in almost a complete loss of androgen binding activity in the purified germ cell suspensions. Furthermore, Sertoli cell enriched testes from 22-, 32- and 40-day old rats showed increases in particulate androgen binding, when compared to matched controls, parallel to increments in the activity of a Sertoli cell marker enzyme (beta-glucuronidase). These results suggest that particulate androgen binding activity is only present in Sertoli cells and this protein may play a role in the compartmentalization of androgens in the testis.
D000727:Androgen-Binding Protein / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D013196:Dihydrotestosterone / Q000378:metabolism; D005854:Germ Cells / Q000378:metabolism; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D012708:Sertoli Cells / Q000378:metabolism*; D013347:Subcellular Fractions / Q000378:metabolism; D013737:Testis / Q000378:metabolism*
D000727:Androgen-Binding Protein; D002352:Carrier Proteins; D013196:Dihydrotestosterone