ABSTRACT
Although research into the purification of human gonadotropins for clinical use began in the late 1940s, it was not until the early 1960s that human menopausal gonadotropin, a urinary extract comprising a mixture of follicle stimulating hormone (FSH) and luteinizing hormone (LH), was first made available to physicians from the laboratories of Serono in Rome. Subsequently, considerable improvements have facilitated both separation of FSH from human LH (hLH) and its production using recombinant technology. Early technology focused on the production of biological molecules in bacterial cells (usually Escherichia coli). However, the structural complexity of human gonadotropins such as FSH (Fig 42.1) and the need for posttranslational modification of the molecule by protein folding and glycosylation, made functional protein production impossible in prokaryotes. Thus, a mammalian cell culture system was employed with functional molecules being produced in Chinese hamster ovary (CHO) cells. The world’s first recombinant hFSH (rhFSH; follitropin α) preparation for clinical use was produced by Serono Laboratories in 1988, and was licensed for marketing in the European Union as Gonal-F® in 1995. An rhFSH (follitropin β) product was also licensed by Organon Laboratories in 1996.
