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Retrograde transport from the Golgi region to the endoplasmic reticulum is sensitive to GTP gamma S
The involvement of GTP-binding proteins in the intracellular transport of the secretory glycoprotein alpha 1-antitrypsin was investigated in streptolysin O-permeabilized HepG2 cells. This permeabilization procedure allows ready access to the intracellular milieu of the membrane-impermeant, nonhydrol...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1992
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289374/ https://www.ncbi.nlm.nih.gov/pubmed/1541633 |
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collection | PubMed |
description | The involvement of GTP-binding proteins in the intracellular transport of the secretory glycoprotein alpha 1-antitrypsin was investigated in streptolysin O-permeabilized HepG2 cells. This permeabilization procedure allows ready access to the intracellular milieu of the membrane-impermeant, nonhydrolyzable GTP analog GTP gamma S. In streptolysin O-permeabilized HepG2 cells, the constitutive secretory pathway remains functional and is sensitive to GTP gamma S. Exposure of HepG2 cells to brefeldin A resulted in redistribution of Golgi-resident glycosyltransferases (including both alpha 2----3 and alpha 2----6 sialyltransferases) to the ER. This redistribution was sensitive to GTP gamma S. Our results suggest that GTP-binding proteins are involved in the regulation not only of the anterograde, but also of the retrograde, pathway. |
format | Text |
id | pubmed-2289374 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1992 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22893742008-05-01 Retrograde transport from the Golgi region to the endoplasmic reticulum is sensitive to GTP gamma S J Cell Biol Articles The involvement of GTP-binding proteins in the intracellular transport of the secretory glycoprotein alpha 1-antitrypsin was investigated in streptolysin O-permeabilized HepG2 cells. This permeabilization procedure allows ready access to the intracellular milieu of the membrane-impermeant, nonhydrolyzable GTP analog GTP gamma S. In streptolysin O-permeabilized HepG2 cells, the constitutive secretory pathway remains functional and is sensitive to GTP gamma S. Exposure of HepG2 cells to brefeldin A resulted in redistribution of Golgi-resident glycosyltransferases (including both alpha 2----3 and alpha 2----6 sialyltransferases) to the ER. This redistribution was sensitive to GTP gamma S. Our results suggest that GTP-binding proteins are involved in the regulation not only of the anterograde, but also of the retrograde, pathway. The Rockefeller University Press 1992-03-02 /pmc/articles/PMC2289374/ /pubmed/1541633 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 Retrograde transport from the Golgi region to the endoplasmic reticulum is sensitive to GTP gamma S |
title | Retrograde transport from the Golgi region to the endoplasmic reticulum is sensitive to GTP gamma S |
title_full | Retrograde transport from the Golgi region to the endoplasmic reticulum is sensitive to GTP gamma S |
title_fullStr | Retrograde transport from the Golgi region to the endoplasmic reticulum is sensitive to GTP gamma S |
title_full_unstemmed | Retrograde transport from the Golgi region to the endoplasmic reticulum is sensitive to GTP gamma S |
title_short | Retrograde transport from the Golgi region to the endoplasmic reticulum is sensitive to GTP gamma S |
title_sort | retrograde transport from the golgi region to the endoplasmic reticulum is sensitive to gtp gamma s |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289374/ https://www.ncbi.nlm.nih.gov/pubmed/1541633 |