Special Issue Article
Glycosphingolipid Mediated Caveolin-1 OligomerizationLiming Shu and James A. Shayman*
Nephrology Division, Department of Internal Medicine, University of Michigan, 1150 West Medical Center Drive, Ann Arbor, Michigan 48109, USA
- *Corresponding Author:
- James A. Shayman
Department of Internal Medicine
1150 West Medical Center Drive
Ann Arbor, Michigan 48109-0676, USA
E-mail: [email protected]
Received date: January 21, 2012; Accepted date: February 16, 2012; Published date: February 18, 2012
Citation: Shu L, Shayman JA (2012) Glycosphingolipid Mediated Caveolin-1 Oligomerization. J Glycom Lipidom S2:003. doi: 10.4172/2153-0637.S2-003
Copyright: © 2012 Shu L, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
We have previously demonstrated an association between the accumulation of the glycosphingolipid globotriaosylceramide (Gb3) and the loss of high molecular weight oligomers in the aortas of α-galactosidase A-knockout mice, a model of Fabry disease. In the present study the molecular basis for the association between glycosphingolipids and caveolin-1 oligomerization was further investigated. Cellular glycosphingolipids were selectively depleted by treatment with a series of sphingolipid synthesis inhibitors, including D-threo-ethylenedioxyphenyl-2-palmitoylamino-3-pyrrolidinopropanol, fumonisin B1 and myriocin. The depletion of glycosphingolipids resulted in the loss of high molecular mass oligomers of caveolin-1 in plasma membranes of cultured ECV-304 cells as well as in the caveolar fractions of Hela cells as measured by immunoblotting. The disruption of caveolin-1 high molecular weight oligomer formation caused by changes of composition of glycosphingolipids may be directly involved in the interruption of cellular functions including caveolar stabilization, membrane trafficking and signal transduction. These results suggest a specific role for glycosphingolipidsin the caveolar co-localization and oligomerization of caveolin-1.