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Defective myogenic differentiation of human rhabdomyosarcoma cells is characterized by sialidase Neu2 loss of expression
Author(s) -
Stoppani Elena,
Rossi Stefania,
Marchesini Sergio,
Preti Augusto,
Fanzani Alessandro
Publication year - 2009
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2009.06.005
Subject(s) - rhabdomyosarcoma , biology , follistatin , embryonal rhabdomyosarcoma , myf5 , alveolar rhabdomyosarcoma , sialidase , pax3 , myocyte , microbiology and biotechnology , myogenesis , medicine , genetics , enzyme , myod , gene , sarcoma , biochemistry , pathology , transcription factor , neuraminidase
Sialidase Neu2 is a glycohydrolytic enzyme whose tissue distribution has been detected principally in differentiated skeletal muscle. In this study we show that Neu2 expression is absent in different embryonal and alveolar human tumor rhabdomyosarcoma (RMS) cells, which are genetically committed myoblasts characterized by delayed differentiation. Forced myogenic differentiation of an embryonal RMS cell line, as obtained via pharmacological and genetic p38 activation or via follistatin overexpression, was characterized by Neu2 loss of expression despite the significant rise of different muscle‐specific markers, suggesting therefore that the defective myogenic program of RMS cells is accompanied by Neu2 suppression.