
TY  - JOUR
A1  - Hedger, Mark P. 
A1  - Culler, Michael D. 
T1  - Comparison of LHRH-peptidase and plasminogen activator activity in rat testis extracts
JF  - Reproduction, Fertility and Development
JO  - Reprod. Fertil. Dev.
Y1  - 1998
VL  - 9
IS  - 7
SP  - 659
EP  - 664
KW  - gonadotrophin-releasing hormone associated peptide, angiotensins, prolyl endopeptidase, plasmin, plasminogen activator inhibitors.
UR  - https://doi.org/10.1071/R97062 
N2  - 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. 
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