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pH-independent and -dependent cleavage of proinsulin in the same secretory vesicle

Amherdt, M.
Ravazzola, M.
Anderson, R. G.
Published in The journal of cell biology. 1994, vol. 126, no. 5, p. 1149-1156
Abstract By quantitative immunoelectron microscopy and HPLC, we have studied the effect of disrupting pH gradients, by ammonium chloride, on proinsulin conversion in the insulin-producing B-cells of the islets of langerhans. Proinsulin content and pH in single secretory vesicles were measured on consecutive serial sections immunostained alternately with anti-proinsulin or anti-dinitrophenol (to reveal the pH-sensitive probe DAMP) antibodies. Radioactivity labeled proinsulin, proinsulin cleavage intermediates, and insulin were quantitated by HPLC analysis of extracts of islets treated in the same conditions. Cleavage at the C-peptide/A-chain junction is significantly less sensitive to pH gradient disruption than that of the B-chain/C-peptide junction, but the range of pH and proinsulin content in individual vesicles indicate that both cleavages occur in the same vesicle released from the TGN.
Keywords Ammonium Chloride/pharmacologyAnimalsCytoplasmic Granules/ metabolismGlucose/pharmacologyHydrogen-Ion ConcentrationIslets of Langerhans/ metabolismProinsulin/ metabolismProtein Processing, Post-Translational/drug effectsRatsRats, Sprague-Dawley
PMID: 8063854
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Other version: http://jcb.rupress.org/content/126/5/1149.full.pdf
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ORCI, Lelio et al. pH-independent and -dependent cleavage of proinsulin in the same secretory vesicle. In: The Journal of Cell Biology, 1994, vol. 126, n° 5, p. 1149-1156. doi: 10.1083/jcb.126.5.1149 https://archive-ouverte.unige.ch/unige:8946

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Deposited on : 2010-07-12

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