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• W2006503883 abstract "Abstract The lysosomal acid protease, cathepsin D, is considered to be the primary enzyme within the thyroid which is responsible for the hydrolysis of thyroglobulin and release of active thyroid hormones. Pepstatin has been shown to be a potent inhibitor of cathepsin D in various organs. Therefore, pepstatin may play a therapeutic role in certain disease states. The purpose of our study was to determine the effect of pepstatin on the release of cathepsin D from incubated slices of thyroid tissue. This thyroid tissue was also measured for cyclic AMP concentration. When thyrotropin (TSH) and a phosphodiesterase inhibitor, methylxanthine (MIX), were added to the medium of incubated thyroid tissue, 819 ± 77 U/g cathepsin D was found in the medium compared to 47 ± 7 U/g when no additional agents were added. The addition of 1.43 m M pepstatin to the medium prior to incubation resulted in 100% inhibition of cathepsin D. Pepstatin did not, however, inhibit another thyroid lysosomal enzyme, β-glucuronidase. TSH + MIX-Stimulated thyroid tissue also showed an elevation in tissue cyclic AMP concentrations after incubation as compared to nonstimulated tissue (6.43 ± 0.58 pmol/whole thyroid vs 1.18 ± 0.23 pmol/whole thyroid). When pepstatin was added to the TSH + MIX-stimulated tissue, there was a slight reduction in cyclic AMP concentration (3.6 ± 0.67 pmol/whole thyroid). However, this concentration was still significantly greater than in nonstimulated tissue. The effect of chlorpromazine was also studied. This agent inhibited the increase in cyclic AMP in TSH + MIX-stimulated tissue, but had no appreciable effect on cathepsin D or β-glucuronidase release. This study showed that pepstatin specifically inhibits thyroid cathepsin D during incubation of thyroid tissue. However, pepstatin does not inhibit β-glucuronidase or TSH + MIX-stimulated tissue cyclic AMP elevations. Further studies with pepstatin using an in vivo model are warranted." @default.
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• W2006503883 title "Inhibition of thyroid cathepsin D activity by pepstatin" @default.
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• W2006503883 doi "https://doi.org/10.1016/0022-4804(80)90075-x" @default.
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