UNIGE document Scientific Article
previous document  unige:9235  next document
add to browser collection
Title

Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles

Authors
Ravazzola, M.
Storch, M. J.
Anderson, R. G.
Perrelet, A.
Published in Cell. 1987, vol. 49, no. 6, p. 865-868
Abstract The direct identification of the intracellular site where proinsulin is proteolytically processed into insulin has been achieved by immunocytochemistry using an insulin-specific monoclonal antibody. Insulin immunoreactivity is absent from the Golgi stack of pancreatic B-cells and first becomes detectable in clathrin-coated secretory vesicles released from the trans Golgi pole. Clathrin-coated secretory vesicles transform into mature noncoated secretory granules which contain the highest concentration of insulin immunoreactive sites. Maturation of clathrin-coated secretory vesicles is accompanied by a progressive acidification of the vesicular milieu, as evidenced by a cytochemical probe that accumulates in acidic compartments whereupon it can be revealed by immunocytochemistry. Thus packaging of the prohormone in secretory vesicles, and acidification of this compartment, are critical steps in the proper proteolytic maturation of insulin.
Keywords Antibodies, Monoclonal/diagnostic useCell CompartmentationClathrin/physiologyCytoplasmic Granules/ physiologyGold/diagnostic useHydrogen-Ion ConcentrationInsulin/immunology/ metabolismMicroscopy, ElectronPeptide Hydrolases/metabolismProinsulin/ metabolismProtein Processing, Post-Translational
Identifiers
PMID: 3555846
Full text
Structures
Citation
(ISO format)
ORCI, Lelio et al. Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles. In: Cell, 1987, vol. 49, n° 6, p. 865-868. https://archive-ouverte.unige.ch/unige:9235

203 hits

0 download

Update

Deposited on : 2010-07-12

Export document
Format :
Citation style :