Localization of neutral ceramidase in caveolin-enriched light membranes of murine endothelial cells

Elena Romiti, Elisabetta Meacci, Giuditta Tanzi, Laura Becciolini, Susumu Mitsutake, Marta Farnararo, Makoto Ito, Paola Bruni

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19 Citations (Scopus)

Abstract

Sphingomyelinase (SMase) and ceramidase (CDase) activities participate in sphingomyelin (SM) metabolism and have a role in the signal transduction of a variety of ligands. In this study evidence is presented that caveolin-enriched light membranes (CELMs) of murine endothelial cells, characterized by high SM, ceramide (Cer) and cholesterol content, bear acid and neutral SMase as well as neutral CDase activities. Localization of neutral CDase in CELMs was confirmed by Western analysis. Notably, cell treatment with cyclodextrin, which depleted cell cholesterol, did not affect acid or neutral SMase activities but significantly enhanced neutral CDase activity in CELMs, indicating a negative role for cholesterol in CDase regulation. These findings suggest that neutral CDase is implicated, together with SMase activities, in the control of caveolar Cer content that may be critical for caveola dynamics.

Original languageEnglish
Pages (from-to)163-168
Number of pages6
JournalFEBS Letters
Volume506
Issue number2
DOIs
Publication statusPublished - Oct 5 2001

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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    Romiti, E., Meacci, E., Tanzi, G., Becciolini, L., Mitsutake, S., Farnararo, M., Ito, M., & Bruni, P. (2001). Localization of neutral ceramidase in caveolin-enriched light membranes of murine endothelial cells. FEBS Letters, 506(2), 163-168. https://doi.org/10.1016/S0014-5793(01)02878-2