Internalization and degradation of receptor-bound human choriogonadotropin in Leydig tumor cells. Fate of the hormone subunits.
The studies presented herein were aimed at characterizing the pathway involved in the internalization and degradation of human choriogonadotropin by cultured Leydig tumor cells. A quick biochemical method that differentiates between the surface-bound and internalized hormone was developed. Using this method and two hormone derivatives labeled exclusively (with 125I) in the alpha or beta subunits, it was possible to follow the fate of each hormone subunit during hormone binding, internalization, and degradation. The results show that the hormone is internalized in the intact form and that it reaches its place of degradation (presumably the lysosomes) in the intact form. The pathway for degradation of the internalized hormone is complex, and it appears to involve processing of one or both subunits of the intact hormone, followed by subunit dissociation and further degradation of the individual subunits. The alpha subunit is quickly degraded by the cells. The only detectable degradation products are extracellular amino acids. The beta subunit is degraded slower, and several intracellular degradation products are detectable before amino acids appear in the medium.
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D006063:Chorionic Gonadotropin / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007984:Leydig Cell Tumor / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011974:Receptors, LH
D006063:Chorionic Gonadotropin; D011956:Receptors, Cell Surface; D011974:Receptors, LH