Cargando…

Nonconverted, amino acid analog-modified proinsulin stays in a Golgi- derived clathrin-coated membrane compartment

The secretion of insulin by the pancreatic B-cell involves a passage of the newly synthetized (pro)insulin polypeptides across the Golgi apparatus, at the trans pole of which secretory proteins are released as a population of secretory granules characterized by a clathrinlike coat on segments of the...

Descripción completa

Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1984
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113534/
https://www.ncbi.nlm.nih.gov/pubmed/6389572
_version_ 1782140207831711744
collection PubMed
description The secretion of insulin by the pancreatic B-cell involves a passage of the newly synthetized (pro)insulin polypeptides across the Golgi apparatus, at the trans pole of which secretory proteins are released as a population of secretory granules characterized by a clathrinlike coat on segments of their limiting membrane. When the conversion of radiolabeled proinsulin to insulin was inhibited by replacing arginine and lysine with the aminoacid analogs, canavanine and thialysine, the nonconverted radioactive material remained associated with Golgi- derived, coated secretory granules. The coat was characterized as clathrin-containing by immunocytochemistry. Under analog treatment, the noncoated, storage secretory granules did not become markedly labeled during the pulse-chase experiment. These data are compatible with the hypothesis that in normal conditions, the maturation of the coated compartment into noncoated granules is linked to the effective conversion of the prohormone.
format Text
id pubmed-2113534
institution National Center for Biotechnology Information
language English
publishDate 1984
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-21135342008-05-01 Nonconverted, amino acid analog-modified proinsulin stays in a Golgi- derived clathrin-coated membrane compartment J Cell Biol Articles The secretion of insulin by the pancreatic B-cell involves a passage of the newly synthetized (pro)insulin polypeptides across the Golgi apparatus, at the trans pole of which secretory proteins are released as a population of secretory granules characterized by a clathrinlike coat on segments of their limiting membrane. When the conversion of radiolabeled proinsulin to insulin was inhibited by replacing arginine and lysine with the aminoacid analogs, canavanine and thialysine, the nonconverted radioactive material remained associated with Golgi- derived, coated secretory granules. The coat was characterized as clathrin-containing by immunocytochemistry. Under analog treatment, the noncoated, storage secretory granules did not become markedly labeled during the pulse-chase experiment. These data are compatible with the hypothesis that in normal conditions, the maturation of the coated compartment into noncoated granules is linked to the effective conversion of the prohormone. The Rockefeller University Press 1984-12-01 /pmc/articles/PMC2113534/ /pubmed/6389572 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Nonconverted, amino acid analog-modified proinsulin stays in a Golgi- derived clathrin-coated membrane compartment
title Nonconverted, amino acid analog-modified proinsulin stays in a Golgi- derived clathrin-coated membrane compartment
title_full Nonconverted, amino acid analog-modified proinsulin stays in a Golgi- derived clathrin-coated membrane compartment
title_fullStr Nonconverted, amino acid analog-modified proinsulin stays in a Golgi- derived clathrin-coated membrane compartment
title_full_unstemmed Nonconverted, amino acid analog-modified proinsulin stays in a Golgi- derived clathrin-coated membrane compartment
title_short Nonconverted, amino acid analog-modified proinsulin stays in a Golgi- derived clathrin-coated membrane compartment
title_sort nonconverted, amino acid analog-modified proinsulin stays in a golgi- derived clathrin-coated membrane compartment
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113534/
https://www.ncbi.nlm.nih.gov/pubmed/6389572