ABSTRACT
Although research into the purification of human gonadotrophins for clinical use began in the late 1940s, it was not until the early 1960s that human menopausal gonadotrophin (hMG), a urinary extract comprising a mixture of FSH and LH, was first made available to physicians from the laboratories of Serono. Subsequently, considerable improvements have facilitated separation of follicle stimulating hormone (FSH) from human luteinizing hormone (hLH), and then 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 FSH, and the need for posttranslational modification of the molecule by protein folding and glycosylation, made functional protein production impossible in prokaryotes. Thus, a eukaryotic cell culture system was employed with functional molecules being produced in Chinese hamster ovary (CHO) cells. The world’s first recombinant human FSH (rhFSH) preparation for clinical use was produced by Serono laboratories in 1988, and was licensed for marketing as Gonal-F® in 1995 (Fig 36.1). An rhFSH product was also licensed by Organon laboratories in 1996.
