
%0 Journal Article
%A Hedger, Mark P. 
%A Culler, Michael D. 
%T Comparison of LHRH-peptidase and plasminogen activator activity in rat testis extracts
%J Reproduction, Fertility and Development
%D 1998/04/23
%V 9
%N 7
%P 659-664
%K gonadotrophin-releasing hormone associated peptide, angiotensins, prolyl endopeptidase, plasmin, plasminogen activator inhibitors.
%R https://doi.org/10.1071/R97062
%U https://www.publish.csiro.au/paper/R97062 
%X Testicular LHRH-peptidase and testicular urokinase-type plasminogen activator are Sertoli cell-secreted proteases which display similar molecular properties. However, there is relatively little information regarding the substrate specificity and potential cross-reactivity of these enzymes. Testicular extracts were prepared from homogenates of whole rat testes and assessed by LHRH-peptidase assay, and by radial caseinolysis assays for plasminogen activator and plasmin-like activity. Following partial purification of the protease activities in testicular extracts by gel filtration and ion-exchange chromatography, it was conrmed that testicular LHRH-peptidase and plasminogen activator are clearly separable. There was no detectable plasmin-like activity in the testicular extracts; however, the extracts were found to contain an inhibitor, or inhibitors, of both plasminogen activator and plasmin activity. In addition to LHRH and Gly 6 -substituted LHRH analogues, the partially purified LHRH-peptidase degraded both angiotensins I and II, but not the gonadotrophin-releasing-hormone-associated peptide derived from the LHRH precursor molecule. These properties of the LHRH-peptidase provide further evidence that it is a testis-specific prolyl endopeptidase, involved in regulating and/or limiting peptide activity in the testis. 
