Abstract
The proteolytic conversion of oxytocin and Arg8-vasopressin by purified rat thymocytes was studied at 37°C and physiological pH 7.4. The formed peptide fragments were isolated by high performance liquid chromatography and characterized by amino acid analysis. When oxytocin was incubated with rat thymocytes, oxytocin 1-8 and oxytocin 1–7 were isolated. In contrast, only Arg8-vasopressin 1–8 was found when Arg8-vasopressin was incubated with thymocytes. The formation of oxytocin 1-8, oxytocin 1–7 and Arg8-vasopressin 1–8 was prevented partially by 10–3M phenylmethylsulfonyl fluoride and iodoacetamide, and abolished by 0.5 × 10–3M Zn2+ and Hg2+ ions and 10–3M o-phenanthroline, but not by 10–5M leupeptin, lima bean trypsin inhibitor, trasylol, captopril and phosphoramidon. 0.5 × 10-3M EDTA was without effect on the formation of oxytocin 1–8 and Arg8-vasopressin 1-8 but increased by about 30% the formation of oxytocin 1–7. The results suggest that proteases capable of metabolizing oxytocin and Arg8-vasopressin are localized in the thymocyte surface membrane. Since oxytocin and vasopressin are synthetized by thymic epithelial cells and exert several actions on thymocytes, these proteases may play a physiological role in the inactivation of neurohypophyseal peptides at the thymocyte level.