Isolation and Analysis of Detergent-Resistant Membrane Fractions

2016 ◽  
pp. 107-131 ◽  
Author(s):  
Massimo Aureli ◽  
Sara Grassi ◽  
Sandro Sonnino ◽  
Alessandro Prinetti
Keyword(s):  
Detergent Resistant Membrane

Comparative lipid analysis and structure of detergent-resistant membrane raft fractions isolated from human and ruminant erythrocytes

2005 ◽  
Vol 434 (1) ◽  
pp. 150-158 ◽  
Author(s):  
Kamen S. Koumanov ◽  
Cedric Tessier ◽  
Albena B. Momchilova ◽  
Dominique Rainteau ◽  
Claude Wolf ◽  
...  
Keyword(s):  
Lipid Analysis ◽  
Membrane Raft ◽  
Detergent Resistant Membrane

Fatty acid synthase drives the synthesis of phospholipids partitioning into detergent-resistant membrane microdomains

2003 ◽  
Vol 302 (4) ◽  
pp. 898-903 ◽  
Author(s):  
Johannes V Swinnen ◽  
Paul P Van Veldhoven ◽  
Leen Timmermans ◽  
Ellen De Schrijver ◽  
Koen Brusselmans ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Membrane Microdomains ◽  
Detergent Resistant Membrane

scholarly journals Detergent-Resistant Membrane Microdomains Facilitate Ib Oligomer Formation and Biological Activity of Clostridium perfringens Iota-Toxin

2004 ◽  
Vol 72 (4) ◽  
pp. 2186-2193 ◽  
Author(s):  
Martha L. Hale ◽  
Jean-Christophe Marvaud ◽  
Michel R. Popoff ◽  
Bradley G. Stiles
Keyword(s):  
Clostridium Perfringens ◽  
Cell Types ◽  
Cell Receptor ◽  
Vero Cells ◽  
Membrane Microdomains ◽  
Oligomer Formation ◽  
A Cell ◽  
Clostridium Perfringens Iota Toxin ◽  
Detergent Resistant Membrane ◽  
Soluble Fractions

ABSTRACT Clostridium perfringens iota-toxin consists of two separate proteins identified as a cell binding protein, iota b (Ib), which forms high-molecular-weight complexes on cells generating Na+/K+-permeable pores through which iota a (Ia), an ADP-ribosyltransferase, presumably enters the cytosol. Identity of the cell receptor and membrane domains involved in Ib binding, oligomer formation, and internalization is currently unknown. In this study, Vero (toxin-sensitive) and MRC-5 (toxin-resistant) cells were incubated with Ib, after which detergent-resistant membrane microdomains (DRMs) were extracted with cold Triton X-100. Western blotting revealed that Ib oligomers localized in DRMs extracted from Vero, but not MRC-5, cells while monomeric Ib was detected in the detergent-soluble fractions of both cell types. The Ib protoxin, previously shown to bind Vero cells but not form oligomers or induce cytotoxicity, was detected only in the soluble fractions. Vero cells pretreated with phosphatidylinositol-specific phospholipase C before addition of Ib indicated that glycosylphosphatidyl inositol-anchored proteins were minimally involved in Ib binding or oligomer formation. While pretreatment of Vero cells with filipin (which sequesters cholesterol) had no effect, methyl-β-cyclodextrin (which extracts cholesterol) reduced Ib binding and oligomer formation and delayed iota-toxin cytotoxicity. These studies showed that iota-toxin exploits DRMs for oligomer formation to intoxicate cells.

scholarly journals Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions

2018 ◽  
Vol 19 (10) ◽  
pp. 2876 ◽  
Author(s):  
Sabine Lüthje ◽  
Teresa Martinez-Cortes
Keyword(s):  
Plasma Membranes ◽  
Secretory Pathway ◽  
In Silico Analysis ◽  
Class Iii ◽  
Membrane Repair ◽  
Protein Protein Interaction ◽  
Thale Cress ◽  
Membrane Bound ◽  
Class Iii Peroxidases ◽  
Detergent Resistant Membrane

Class III peroxidases are heme-containing proteins of the secretory pathway with a high redundance and versatile functions. Many soluble peroxidases have been characterized in great detail, whereas only a few studies exist on membrane-bound isoenzymes. Membrane localization of class III peroxidases has been demonstrated for tonoplast, plasma membrane and detergent resistant membrane fractions of different plant species. In silico analysis revealed transmembrane domains for about half of the class III peroxidases that are encoded by the maize (Zea mays) genome. Similar results have been found for other species like thale-cress (Arabidopsis thaliana), barrel medic (Medicago truncatula) and rice (Oryza sativa). Besides this, soluble peroxidases interact with tonoplast and plasma membranes by protein–protein interaction. The topology, spatiotemporal organization, molecular and biological functions of membrane-bound class III peroxidases are discussed. Besides a function in membrane protection and/or membrane repair, additional functions have been supported by experimental data and phylogenetics.

scholarly journals Proteomic Analysis of Detergent Resistant Membrane Domains during Early Interaction of Macrophages with Rough and Smooth Brucella melitensis

PLoS ONE ◽  
2014 ◽  
Vol 9 (3) ◽  
pp. e91706 ◽  
Author(s):  
Sabine A. Lauer ◽  
Srinivas Iyer ◽  
Timothy Sanchez ◽  
Christian V. Forst ◽  
Brent Bowden ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Brucella Melitensis ◽  
Membrane Domains ◽  
Early Interaction ◽  
Detergent Resistant Membrane

Tritrichomonas foetus Displays Classical Detergent-resistant Membrane Microdomains on its Cell Surface

Protist ◽  
2014 ◽  
Vol 165 (3) ◽  
pp. 293-304 ◽  
Author(s):  
Ivone de Andrade Rosa ◽  
Georgia Atella ◽  
Marlene Benchimol
Keyword(s):  
Cell Surface ◽  
Membrane Microdomains ◽  
Tritrichomonas Foetus ◽  
Detergent Resistant Membrane
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