Identification of calcitonin receptors in human spermatozoa

Abstract

Calcitonin (CT) is a powerful hypocalcemic hormone which regulates calcium balance in cells. The presence of CT and CT receptors has been demonstrated in many extrathyroidal tissues, including the male genital tract. CT immunoreactivity has also been found in human seminal fluid, and an inhibitory effect of salmon CT on human sperm motility in vitro was recently reported. In this study the presence of specific binding sites for synthetic salmon CT in intact human spermatozoa was investigated using [125I]salmon CT. Binding experiments demonstrated a CT-sperm interaction involving a receptor-mediated mechanism. The binding was very rapid and minimally reversible, with the maximal site saturation occurring at approximately 2 nM labeled peptide. The dissociation of the CT-receptor complex was only slightly influenced by the addition of unlabeled hormone. Increasing concentrations of unlabeled salmon, eel, and human CT produced a dose-dependent inhibition of [125I]salmon CT binding. These data fulfill the major criteria for demonstration of specific receptors for salmon CT in human spermatozoa. Owing to the key role of calcium ions in regulating sperm motility and the onset of the acrosomal reaction, CT receptors could be important in male gamete physiology.