Indian Journal of Experimental Biology
Ability of a glycoprotein hormone to fold and assemble correctly is an essential requirement for the attainment of its biological activity . Cells have a quality control system to assure that when proteins of the endoplasmic reticulum mi sfold or fail to assemble correctly they do not exit the cell. But human chorionic gonadotropin (hCG) is an exception to this rule as is illustrated by the following observations. First, both hCG subunits are secreted efficiently as unassembled monomers. Second, some mis(un)folded forms of hCG-β can be efficiently secreted from cells that do not facilitate the secretion of other misfolded proteins. Third, the efficient secretion of an assembly incompetent α-subunit occurs in spite of lacking both of its non-cystine knot disulphide bonds. And fourth, hCG heterodimers that contain misfolded α-subunits as a result of lack ing cystine knot disulphides are also secreted. In this report, we review direct ex perimental evidence demonstrating that the structural requirements necessary for the secretion of hCG subunits differ from the structural requirements necessary for hCG assembly by using disulphide bond formation as an index with which to monitor the folding, assembly, and secretion of hCG and its α - and β-subunits .
This work is licensed under a Creative Commons Attribution Non-Commercial, NoDerivatives 2.5 License. Creative Commons Attribution Non-Commerical-NoDerivatives 2.5 India
Bedows, E., Darling, R. J., Wilken, J. A., & Sherman, S. A. (2002). Role of disulphide bond formation in folding, secretion, and assembly of human chorionic gonadotropin subunits. Indian Journal of Experimental Biology, 40(4), 467-476. http://nopr.niscair.res.in/handle/123456789/17350