Progress and approaches in mapping the surfaces of human follicle-stimulating hormone: comparison with the other human pituitary glycoprotein hormones.

The pituitary glycoprotein hormones, including human follicle-stimulating hormone (hFSH), are involved in the physiologic functions of receptor binding, in subunit association during assembly and processing, and in untoward effects such as antibody formation during clinical intervention. These activities derive from specific macromolecular associations; a major research trend has been to map the surfaces of these glycoprotein hormones (hFSH, hLH, hCG, and hTSH) into discrete areas responsible for each activity by using a variety of biochemical approaches. Each surface domain or determinant of the hormone is likely to comprise discontinuous amino acid sequences, from one or both subunits, assembled into a precise, unique, macromolecular surface. The paradigm of antigen-antibody interaction may help to explain how the surfaces are assembled, how the common alpha-subunit combines with the unique beta-subunit of each, and how the receptor interacts with heterodimeric hormone.