Polypeptide hormone receptors: characteristics and applications.
Major developments in the area of polypeptide hormone receptors have been reviewed. Receptors are high affinity, high specificity binding sites which appear to be located largely, if not entirely, on the plasma membrane of cells. Receptors are proteins intimately associated with and influenced by lipids. Receptor sites and degrading sites appear to be readily distinguishable entities. The binding of hormone to receptor is distinct and has been dissociated from subsequent steps leading to hormonal response. There is no direct relationship between receptor occupancy and the magnitude of target response to hormone. So called 'spare' receptors can be viewed thermodynamically as enhancing target tissue sensitivity to hormone. The binding of hormone to receptor appears to be a point at which regulation of tissue sensitivity can be influenced either through altering the affinity for hormone or the number of receptors. One factor apparently involved in the regulation of receptor levels is the hormone itself. Receptors have been used to develop assay procedures which have significantly complemented the bioassay and radioimmunoassay. Finally, the measurement of receptor levels in disease has provided new insights into pathophysiology.
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D013006:Growth Hormone / Q000378:metabolism; D006728:Hormones / Q000378:metabolism*; D007328:Insulin / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D009928:Organ Specificity; D010455:Peptides / Q000378:metabolism*; D011388:Prolactin / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000032:analysis*; D051381:Rats; D011956:Receptors, Cell Surface
D006728:Hormones; D007328:Insulin; D010455:Peptides; D011506:Proteins; D011956:Receptors, Cell Surface; D011388:Prolactin; D013006:Growth Hormone