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Ectopic localizations of Golgi glycosyltransferases


Berger, E G (2002). Ectopic localizations of Golgi glycosyltransferases. Glycobiology, 12(2):29R-36R.

Abstract

Glycosyltransferases involved in N- and O-glycan chain elongation and termination are localized in the Golgi apparatus. Early evidence in support of this rule was based on fractionation techniques and was corroborated by numerous immunocytochemical studies. Usually these studies were confined to cultured cell lines exhibiting little differentiation features, such as HeLa cells. However, localization studies conducted in primary cell cultures (e.g.,human umbilical vein endothelial cells), cells obtained ex vivo (e.g., sperm cells), and tissue sections (e.g., intestinal, renal, or hepatic tissue) often reveal ectopic localizations of glycosyltransferases usually at post-Golgi sites, including the plasma membrane. Hence, extracellular cues resulting from specific adhesion sites may influence post-Golgi trafficking routes, which may be reflected by ectopic localization of Golgi enzymes

Abstract

Glycosyltransferases involved in N- and O-glycan chain elongation and termination are localized in the Golgi apparatus. Early evidence in support of this rule was based on fractionation techniques and was corroborated by numerous immunocytochemical studies. Usually these studies were confined to cultured cell lines exhibiting little differentiation features, such as HeLa cells. However, localization studies conducted in primary cell cultures (e.g.,human umbilical vein endothelial cells), cells obtained ex vivo (e.g., sperm cells), and tissue sections (e.g., intestinal, renal, or hepatic tissue) often reveal ectopic localizations of glycosyltransferases usually at post-Golgi sites, including the plasma membrane. Hence, extracellular cues resulting from specific adhesion sites may influence post-Golgi trafficking routes, which may be reflected by ectopic localization of Golgi enzymes

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Item Type:Journal Article, refereed, original work
Communities & Collections:National licences > 142-005
Dewey Decimal Classification:610 Medicine & health
Scopus Subject Areas:Life Sciences > Biochemistry
Language:English
Date:1 February 2002
Deposited On:25 Sep 2018 10:28
Last Modified:31 Jul 2020 22:14
Publisher:Oxford University Press
ISSN:0959-6658
OA Status:Hybrid
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1093/glycob/12.2.29r
Related URLs:https://www.swissbib.ch/Search/Results?lookfor=nationallicenceoxford101093glycob12229R (Library Catalogue)

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