A clathrin-coated, Golgi-related compartment of the insulin secreting cell accumulates proinsulin in the presence of monensin |
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| Authors: | L Orci P Halban M Amherdt M Ravazzola J D Vassalli A Perrelet |
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| Institution: | 1. Institute of Histology and Embryology University of Geneva Medical School Geneva, Switzerland;2. Institute of Clinical Biochemistry University of Geneva Medical School Geneva, Switzerland |
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| Abstract: | When the intracellular transit of 3H-labeled (pro)-insulin polypeptides is perturbed by monensin in the pancreatic B-cell, proinsulin conversion is impaired and the radioactive peptides accumulate in a clathrin-coated membrane compartment related to the Golgi apparatus. Clathrin was demonstrated by immunocytochemistry using the postembedding protein A-gold technique. The coated compartment, which is dilated by monensin, comprises Golgi cisternae with condensing secretory material and newly formed secretory granules; under monensin block, the noncoated (storage) secretory granules do not become significantly labeled. These data suggest that an unperturbed passage through a Golgi-related, clathrin-coated membrane compartment which subsequently matures into noncoated secretory granules is needed for the normal processing of (pro)insulin polypeptides. |
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