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

Journal Article · Thu Nov 01 00:00:00 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), Vol. 39:1
• Country of Publication: United States
• Language: English

Related Subjects

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