Abstract
SDS-polyacrylamide gel electrophoresis followed by enzymography of a human testicular cell culture medium demonstrated that the molecular weight of plasminogen activator (PA) secreted was similar to that of human urokinase and it was also confirmed that follicle-stimulating hormone (FSH) stimulated PA secretion. To further investigate the correlation between spermatogenic impairment and secretory potential of PA in human testicular cells in vivo, the maximum increment in PA activity as a result of treatment with ovine FSH was measured for two groups of patients with different degrees of spermatogenic impairment. The mean value of maximum increment in PA activity in one group with severely impaired testes was remarkably lower than that in another group with slightly impaired testes. Protein biosynthesis in human testicular cells dependent on FSH appears to be impaired with the progression of spermatogenic impairment.
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