Neutral ceramidase secreted by endothelial cells is released in part associated with caveolin-1

Elena Romiti, Elisabetta Meacci, Chiara Donati, Lucia Formigli, Sandra Zecchi-Orlandini, Marta Farnararo, Makoto Ito, Paola Bruni

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16 Citations (Scopus)


Neutral ceramidase (CDase) is a key enzyme of sphingomyelin (SM) metabolism implicated in cell signaling triggered by a variety of extracellular ligands. Previously it was shown that in murine endothelial cells a portion of neutral CDase is localized in detergent-resistant light membranes. In this study subcellular distribution of neutral CDase was further investigated. In accordance with the previous finding, the enzyme was identified in caveolae. Moreover, the same protein was detected in medium-speed supernatant of cell-conditioned medium, accounting for CDase activity measurable in the medium at neutral pH. Notably, these cells released also the caveolae-scaffolding protein caveolin-1 (cav-1). Interestingly, secreted neutral CDase and cav-1 coimmunoprecipitated. In addition, acid sphingomyelinase (SMase) activity was detectable in cav-1 immunocomplexes. These findings are consistent with the view that neutral CDase is released, in part, in association with cav-1 together with acid SMase. It remains to be established whether the here-identified secreted cav-1-enriched complex acts as platform to facilitate extracellular metabolism of SM.

Original languageEnglish
Pages (from-to)27-33
Number of pages7
JournalArchives of Biochemistry and Biophysics
Issue number1
Publication statusPublished - Sept 1 2003

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology


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