Title: The propeptide of preprosomatostatin mediates intracellular transport and secretion of alpha-globin from mammalian cells Document date: 1989_5_1
ID: kjid2e3q_46
Snippet: Similar to observations for several native prohormones (7, 25, 29, 31) proteolytic processing of PRO-GLO required an acidic environment; cleavage was quantitatively inhibited even at low concentrations (25 gM) of chloroquine. High concentrations of chloroquine may be toxic to some cells, however, at the concentrations used in these experiments (25-100/~M) we observed no inhibition of total protein synthesis. Thus, although chloroquine was reporte.....
Document: Similar to observations for several native prohormones (7, 25, 29, 31) proteolytic processing of PRO-GLO required an acidic environment; cleavage was quantitatively inhibited even at low concentrations (25 gM) of chloroquine. High concentrations of chloroquine may be toxic to some cells, however, at the concentrations used in these experiments (25-100/~M) we observed no inhibition of total protein synthesis. Thus, although chloroquine was reported to not affect processing of proopiomelanocortin in pituitary AtT-20 cells (20) , we observed processing inhibition at all chloroquine concentrations and the concomitant enhanced secretion of unprocessed PRO-GLO. Similar results were observed for native proSRIF (41a). We interpret our results to suggest that PRO-GLO was transported to the distal elements of the Golgi apparatus/TGN and packaged into acid vesicles where proteolytic processing was initiated.
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