|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 277, Issue 14, 11788-11794, April 5, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Unidad de Biofísica (Centro Mixto Consejo Superior
de Investigaciones Científicas/Universidad del
País Vasco/Euskal Herriko Unibertsitatea) and
the Departamento de Bioquímica, Universidad del País
Vasco, Aptdo. 644, 48080 Bilbao, Spain
The capacity of ceramides to modify the
permeability barrier of cell membranes has been explored. Membrane
efflux induced either by in situ generated ceramides
(through enzymatic cleavage of sphingomyelin) or by addition of
ceramides to preformed membranes has been studied. Large unilamellar
vesicles composed of different phospholipids and cholesterol, and
containing entrapped fluorescent molecules, have been used as a system
to assay ceramide-dependent efflux. Small proportions of
ceramide (10 mol % of total lipid) that may exist under physiological
conditions of ceramide-dependent signaling have been used
in most experiments. When long chain (egg-derived) ceramides are used,
both externally added or enzymatically produced ceramides induce
release of vesicle contents. However, the same proportion of ceramides
generated by sphingomyelinase induce faster and more extensive efflux
than when added in organic solution to the preformed vesicles. Under
our conditions 10 mol % of N-acetylsphingosine
(C2-ceramide) did not induce any efflux. On the other hand,
sphingomyelinase treatment of bilayers containing 50 mol % sphingomyelin gave rise to release of fluorescein-derivatised dextrans
of molecular mass
Membrane Restructuring via Ceramide Results in Enhanced
Solute Efflux*
,
20 kDa, i.e. larger than
cytochrome c. These results have been discussed in the
light of our own previous data (Ruiz-Argüello, M. B.,
Basañez, G., Goñi, F. M., and Alonso, A. (1996)
J. Biol. Chem. 271, 26616-26621) and of the
observations by Siskind and Colombini (Siskind, L. J., and
Colombini, M. (2000) J. Biol. Chem. 275, 38640-38644). Our spectroscopic observations appear to be in good
agreement with the electrophysiological studies of the latter authors.
Furthermore, some experiments in this paper have been designed to
explore the mechanism of ceramide-induced efflux. Two properties of
ceramide, namely its capacity to induce negative monolayer curvature
and its tendency to segregate into ceramide-rich domains, appear to be
important in the membrane restructuring process.
*
This work was supported in part by grants from
Dirección General de Investigación Científica y
Técnica (Grant PB 96/0171), the Basque Government (Grant PI
99/7), and the University of the Basque Country (Grant UPV 13552/2001).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a predoctoral grant from the Basque Government.
§
Supported by a grant from the Spanish Ministerio de Educación
y Ciencia.
¶
To whom correspondence should be addressed. Tel.:
34-94-601-26-25; Fax: 34-94-464-85-00; E-mail:
gbpaliza@lg.ehu.es.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  S. A. Novgorodov, T. I. Gudz, and L. M. Obeid Long-chain Ceramide Is a Potent Inhibitor of the Mitochondrial Permeability Transition Pore J. Biol. Chem., September 5, 2008; 283(36): 24707 - 24717. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Rogasevskaia and J. R. Coorssen Sphingomyelin-enriched microdomains define the efficiency of native Ca2+-triggered membrane fusion J. Cell Sci., July 1, 2006; 119(13): 2688 - 2694. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. A. Rotolo, J. Zhang, M. Donepudi, H. Lee, Z. Fuks, and R. Kolesnick Caspase-dependent and -independent Activation of Acid Sphingomyelinase Signaling J. Biol. Chem., July 15, 2005; 280(28): 26425 - 26434. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
I. Lopez-Montero, N. Rodriguez, S. Cribier, A. Pohl, M. Velez, and P. F. Devaux Rapid Transbilayer Movement of Ceramides in Phospholipid Vesicles and in Human Erythrocytes J. Biol. Chem., July 8, 2005; 280(27): 25811 - 25819. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F.-X. Contreras, A.-V. Villar, A. Alonso, R. N. Kolesnick, and F. M. Goni Sphingomyelinase Activity Causes Transbilayer Lipid Translocation in Model and Cell Membranes J. Biol. Chem., September 26, 2003; 278(39): 37169 - 37174. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. F. Epand, J.-C. Martinou, M. Fornallaz-Mulhauser, D. W. Hughes, and R. M. Epand The Apoptotic Protein tBid Promotes Leakage by Altering Membrane Curvature J. Biol. Chem., August 30, 2002; 277(36): 32632 - 32639. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. J. Siskind, R. N. Kolesnick, and M. Colombini Ceramide Channels Increase the Permeability of the Mitochondrial Outer Membrane to Small Proteins J. Biol. Chem., July 19, 2002; 277(30): 26796 - 26803. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |