1. NEU3 Sialidase Strictly Modulates GM3 Levels in Skeletal Myoblasts C2C12 Thus Favoring Their Differentiation and Protecting Them from Apoptosis
- Author
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Eugenio Monti, Guido Tettamanti, Maurilio Sampaolesi, Marco Piccoli, Nadia Papini, Cristina Tringali, Luigi Anastasia, Bruno Venerando, Francesca Colazzo, Erika Conforti, Giacomo Palazzolo, Clementina Sitzia, L. Dileo, Anastasia, L., Papini, N., Colazzo, F., Palazzolo, G., Tringali, C., Dileo, L., Piccoli, M., Conforti, E., Sitzia, C., Monti, E., Sampaolesi, M., Tettamanti, G., and Venerando, B.
- Subjects
Down-Regulation ,Neuraminidase ,Glycobiology and Extracellular Matrices ,Biology ,Sialidase ,Biochemistry ,Cell Line ,Cell membrane ,Mice ,SKELETAL MYOBLASTS ,DIFFERENTIATION ,APOPTOSIS ,medicine ,Animals ,G(M3) Ganglioside ,Myocyte ,Gene Silencing ,Epidermal growth factor receptor ,skeletal muscle ,Muscle, Skeletal ,Molecular Biology ,ganglioside GM3 ,Sphingolipids ,Ganglioside ,Epidermal Growth Factor ,Hydrolysis ,Skeletal muscle ,C2V12 ,Cell Biology ,sialidase NEU3 ,cell differentiation ,Cell biology ,ErbB Receptors ,medicine.anatomical_structure ,Models, Chemical ,Cancer cell ,biology.protein ,C2C12 - Abstract
Membrane-bound sialidase NEU3, often referred to as the "ganglioside sialidase", has a critical regulatory function on the sialoglycosphingolipid pattern of the cell membrane, with an anti-apoptotic function, especially in cancer cells. Although other sialidases have been shown to be involved in skeletal muscle differentiation, the role of NEU3 had yet to be disclosed. Herein we report that NEU3 plays a key role in skeletal muscle differentiation by strictly modulating the ganglioside content of adjacent cells, with special regards to GM3. Induced down-regulation of NEU3 in murine myoblasts C2C12, even when partial, totally inhibits their capability to differentiate by increasing GM3 level above a critical point, that causes EGFR inhibition (and ultimately its down-regulation), and an higher responsiveness of myoblasts to the apoptotic stimuli. ispartof: Journal of Biological Chemistry vol:283 issue:52 pages:36265-36271 ispartof: location:United States status: published
- Published
- 2008