Clathrin-coated, Golgi-related compartment of the insulin secreting cell accumulates proinsulin in the presence of monensin

Journal Article · Wed Oct 31 23:00:00 EST 1984 · Cell; (United States)

DOI:https://doi.org/10.1016/0092-8674(84)90189-2· OSTI ID:6006660

Orci, L; Halban, P; Amherdt, M; Ravazzola, M; Vassalli, J D; Perrelet, A

When the intracellular transit of /sup 3/H-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.

• Research Organization: Univ. of Geneva Medical School, Switzerland
• OSTI ID: 6006660
• Journal Information: Cell; (United States), Journal Name: Cell; (United States) Vol. 39:1; ISSN CELLB
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AUTORADIOGRAPHY
BIOCHEMISTRY
CELL CONSTITUENTS
CELL MEMBRANES
CHEMISTRY
HORMONES
INSULIN
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
MEMBRANES
ORGANIC COMPOUNDS
ORGANOIDS
PEPTIDE HORMONES
PEPTIDES
POLYPEPTIDES
PROTEINS
TRACER TECHNIQUES
TRITIUM COMPOUNDS