Plasminogen activator and protease inhibitor activities in isolated rat thymocytes

✍ Scribed by Michael Mayer; Zvezdana Finci; Jamil Kanaany; Nurit Kaiser

• Publisher: Springer
• Year: 1985
• Tongue: English
• Weight: 572 KB
• Volume: 66
• Category: Article
• ISSN: 0300-8177
• DOI: 10.1007/bf00220781

✦ Synopsis

Plasminogen Activator (PA) and its response to glucocorticoids and androgens was studied in viable rat thymocytes in suspension. PA was measured by its ability to convert plasminogen to plasmin, and the formed plasmin determined by cleavage of 14C-labeled globin. Using this functional assay, PA was found to be associated with the outer surface of thymic cells, and only negligible activity recovered from the incubation medium. Rat thymocytes also contain cytoplasmic and nuclear inhibitor(s) of the serine proteases plasmin, trypsin, chymotrypsin and thymic PA. Release of these inhibitors prevented determination of thymic PA activity in presence of lysed cells. The specific activity of PA in thymocytes isolated from adrenalectomized-castrated rats did not differ significantly from the specific activity associated with cells from intact animals. Furthermore, treatment of adrenalectomized-castrated rats with 0.1 mg of dexamethasone/kg for 2 days induced thymic involution without affecting thymic PA activity. These observations suggest that PA activity of thymocytes is not involved in glucocorticoid-mediated thymic involution.