Document Detail

The acidic environment of the Golgi is critical for glycosylation and transport.
MedLine Citation:
PMID:  20816224     Owner:  NLM     Status:  MEDLINE    
Proteins and glycolipids are modified by various modes of glycosylation in the endoplasmic reticulum (ER) and the Golgi apparatus. It is well known that the lumen of the Golgi is acidic and compromising acidification by chemical compounds causes impaired glycosylation and transport of proteins (Axelsson et al., 2001; Chapman and Munro, 1994; Palokangas et al., 1994; Presley et al., 1997; Puri et al., 2002; Reaves and Banting, 1994; Rivinoja et al., 2006; Tartakoff et al., 1978). The mechanisms by which glycosylation and transport are regulated by an acidic pH remain largely unknown. Recent findings that the impaired regulation of an acidic environment may be implicated in the pathology of several diseases emphasize the importance of pH regulation (Jentsch, 2007; Kasper et al., 2005; Kornak et al., 2001; Kornak et al., 2008; Piwon et al., 2000; Stobrawa et al., 2001; Teichgraber et al., 2008). We recently established a mutant cell line in which Golgi acidification was selectively impaired and the raised luminal Golgi pH caused impaired transport and glycosylation of proteins and altered Golgi morphology (Maeda et al., 2008). As alkalinizing compounds nonselectively affect all acidic organelles including lysosomes, endosomes, and the Golgi, the mutant cell is thought to be useful in analyzing how the acidic environment of the Golgi regulates glycosylation. In this chapter, we have introduced how we established mutant cells with impaired Golgi acidification and methods for measuring Golgi pH.
Yusuke Maeda; Taroh Kinoshita
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Methods in enzymology     Volume:  480     ISSN:  1557-7988     ISO Abbreviation:  Meth. Enzymol.     Publication Date:  2010  
Date Detail:
Created Date:  2010-09-06     Completed Date:  2010-12-14     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0212271     Medline TA:  Methods Enzymol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  495-510     Citation Subset:  IM    
Copyright Information:
Copyright (c) 2010 Elsevier Inc. All rights reserved.
Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan.
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MeSH Terms
Acids / pharmacology*
Cell Culture Techniques
Genes, Reporter
Genetic Techniques
Glycosylation / drug effects
Golgi Apparatus / chemistry,  drug effects*,  metabolism*
Hydrogen-Ion Concentration
Models, Biological
Mutagenesis / physiology
Protein Processing, Post-Translational / drug effects,  genetics
Protein Transport / drug effects,  genetics
Proteins / genetics,  metabolism*
Staining and Labeling / methods
Reg. No./Substance:
0/Acids; 0/Proteins

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