JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on November 15, 2002
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
277/47/44731    most recent
M204604200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Crespo, P. M.
Right arrow Articles by Daniotti, J. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Crespo, P. M.
Right arrow Articles by Daniotti, J. L.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print September 16, 2002
J. Biol. Chem, 10.1074/jbc.M204604200
Submitted on May 10, 2002
Revised on September 16, 2002
Accepted on September 13, 2002

Effect of gangliosides on the distribution of a glycosylphosphatidylinositol-anchored protein in plasma membrane from CHO-K1 Cells

Pilar Maria Crespo, Adolfo Ramon Zurita, and Jose Luis Daniotti

CIQUIBIC-Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Córdoba, Córdoba 5000

Corresponding Author: daniotti{at}dqb.fcq.unc.edu.ar

Glycosylphosphatidylinositol (GPI)-anchored proteins are mainly clustered in sphingolipid-cholesterol microdomains of the plasma membrane. The distribution of a GPI-anchored fusion protein (GPI-YFP) in the plasma membrane of CHO-K1 cells with different glycolipid compositions was investigated. Cells depleted of glycosphingolipids by inhibiting glucosylceramide synthase activity, or cell lines expressing different gangliosides due to stable transfection of appropriate ganglioside glycosyltransferases, or exposed to exogenous GM1, were transfected with GPI-YFP cDNA. The distribution of GPI-YFP fusion protein expressed at the plasma membrane was studied using the membrane-impermeable crosslinking agent bis(sulphosuccinimidyl)suberate (BS3). Results indicate that GPI-YFP form clusters at the surface of cells expressing GM3, or cells depleted of glycolipids, or transfected cells expressing mainly GD3 and GT3, or GM1 and GD1a, or mostly GM2, or highly expressing GM1. However, no significant changes in membrane microdomains of GPI-YFP were detected in the different glycolipid environment provided by the membranes of the cell lines under study. On the other hand, wild type CHO-K1 cells exposed to 100 mu M of GM1 before crosslinking with BS3 showed a dramatic reduction in the amount of GPI-YFP clusters. These finding clearly indicate that manipulating the glycolipid content of cellular membrane, just by changing the ganglioside biosynthetic activity of the cell, did not significantly affect the association of GPI-YFP on the cell surface of CHO-K1 cells. The effect of exogenous GM1 gangliosides on GPI-YFP plasma membrane distribution might be a consequence of ganglioside level reached in plasma membrane and/or the effect of particular ganglioside species (micelles) that leads to membrane architecture and/or dynamic modifications.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
A. S. Uliana, P. M. Crespo, J. A. Martina, J. L. Daniotti, and H. J. F. Maccioni
Modulation of GalT1 and SialT1 Sub-Golgi Localization by SialT2 Expression Reveals an Organellar Level of Glycolipid Synthesis Control
J. Biol. Chem., October 27, 2006; 281(43): 32852 - 32860.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. A. Gomez and J. L. Daniotti
H-Ras Dynamically Interacts with Recycling Endosomes in CHO-K1 Cells: INVOLVEMENT OF Rab5 AND Rab11 IN THE TRAFFICKING OF H-Ras TO THIS PERICENTRIOLAR ENDOCYTIC COMPARTMENT
J. Biol. Chem., October 14, 2005; 280(41): 34997 - 35010.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. P. West, B. A. Dancho, and S. B. Mizel
Gangliosides Inhibit Flagellin Signaling in the Absence of an Effect on Flagellin Binding to Toll-like Receptor 5
J. Biol. Chem., March 11, 2005; 280(10): 9482 - 9488.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. M. Crespo, R. Iglesias-Bartolome, and J. L. Daniotti
Ganglioside GD3 Traffics from the trans-Golgi Network to Plasma Membrane by a Rab11-independent and Brefeldin A-insensitive Exocytic Pathway
J. Biol. Chem., November 12, 2004; 279(46): 47610 - 47618.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Nagafuku, K. Kabayama, D. Oka, A. Kato, S. Tani-ichi, Y. Shimada, Y. Ohno-Iwashita, S. Yamasaki, T. Saito, K. Iwabuchi, et al.
Reduction of Glycosphingolipid Levels in Lipid Rafts Affects the Expression State and Function of Glycosylphosphatidylinositol-anchored Proteins but Does Not Impair Signal Transduction via the T Cell Receptor
J. Biol. Chem., December 19, 2003; 278(51): 51920 - 51927.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.