Recycling glycoproteins do not return to the cis-Golgi

Recycling of a number of glycoproteins along the site of action of mannosidase I (the distal endoplasmic reticulum/cis-Golgi) was followed in several different cell lines. Treatment of cells with 1- deoxymannojirimycin (dMM) produced high mannose oligosaccharides at positions otherwise occupied by c...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1988
Materias:
Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115183/
https://www.ncbi.nlm.nih.gov/pubmed/2839522
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description Recycling of a number of glycoproteins along the site of action of mannosidase I (the distal endoplasmic reticulum/cis-Golgi) was followed in several different cell lines. Treatment of cells with 1- deoxymannojirimycin (dMM) produced high mannose oligosaccharides at positions otherwise occupied by complex-type oligosaccharides in these glycoproteins. Conversion of high-mannose-type oligosaccharides to complex oligosaccharides of proteins initially synthesized in the presence of dMM was used as a marker for recycling of glycoproteins along the site of action of dMM. In contrast to findings reported by Snider and Rogers (Snider, M. D., and O. C. Rogers. 1986. J. Cell Biol. 103:265-275), removal of dMM did not result in reconversion of high- mannose oligosaccharides to complex-type sugars, even after prolonged periods of culture. We conclude that surface glycoproteins do not recycle through the cis-medial Golgi elements.
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spelling pubmed-21151832008-05-01 Recycling glycoproteins do not return to the cis-Golgi J Cell Biol Articles Recycling of a number of glycoproteins along the site of action of mannosidase I (the distal endoplasmic reticulum/cis-Golgi) was followed in several different cell lines. Treatment of cells with 1- deoxymannojirimycin (dMM) produced high mannose oligosaccharides at positions otherwise occupied by complex-type oligosaccharides in these glycoproteins. Conversion of high-mannose-type oligosaccharides to complex oligosaccharides of proteins initially synthesized in the presence of dMM was used as a marker for recycling of glycoproteins along the site of action of dMM. In contrast to findings reported by Snider and Rogers (Snider, M. D., and O. C. Rogers. 1986. J. Cell Biol. 103:265-275), removal of dMM did not result in reconversion of high- mannose oligosaccharides to complex-type sugars, even after prolonged periods of culture. We conclude that surface glycoproteins do not recycle through the cis-medial Golgi elements. The Rockefeller University Press 1988-07-01 /pmc/articles/PMC2115183/ /pubmed/2839522 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
Recycling glycoproteins do not return to the cis-Golgi
title Recycling glycoproteins do not return to the cis-Golgi
title_full Recycling glycoproteins do not return to the cis-Golgi
title_fullStr Recycling glycoproteins do not return to the cis-Golgi
title_full_unstemmed Recycling glycoproteins do not return to the cis-Golgi
title_short Recycling glycoproteins do not return to the cis-Golgi
title_sort recycling glycoproteins do not return to the cis-golgi
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115183/
https://www.ncbi.nlm.nih.gov/pubmed/2839522

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