Prelamin A is involved in early steps of muscle differentiation |
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Authors: | Capanni Cristina Del Coco Rosalba Squarzoni Stefano Columbaro Marta Mattioli Elisabetta Camozzi Daria Rocchi Anna Scotlandi Katia Maraldi Nadir Foisner Roland Lattanzi Giovanna |
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Institution: | a IGM-CNR, Unit of Bologna, c/o IOR, Via di Barbiano 1/10 I-40136 Bologna, Italy b Laboratory of Cell Biology Istituto Ortopedico Rizzoli, Bologna, Italy c Laboratory of Oncological Research, Istituto Ortopedico Rizzoli, Bologna, Italy d Max F. Perutz Laboratories, Medical University of Vienna, Vienna, Austria |
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Abstract: | Lamin A is a nuclear lamina constituent implicated in a number of human disorders including Emery-Dreifuss muscular dystrophy. Since increasing evidence suggests a role of the lamin A precursor in nuclear functions, we investigated the processing of prelamin A during differentiation of C2C12 mouse myoblasts. We show that both protein levels and cellular localization of prelamin A are modulated during myoblast activation. Similar changes of lamin A-binding proteins emerin and LAP2α were observed. Furthermore, prelamin A was found in a complex with LAP2α in differentiating myoblasts. Prelamin A accumulation in cycling myoblasts by expressing unprocessable mutants affected LAP2α and PCNA amount and increased caveolin 3 mRNA and protein levels, while accumulation of prelamin A in differentiated muscle cells following treatment with a farnesyl transferase inhibitor appeared to inhibit caveolin 3 expression. Our data provide evidence for a critical role of the lamin A precursor in the early steps of muscle cell differentiation. |
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Keywords: | Prelamin A LAP2 alpha Myoblast differentiation Caveolin 3 |
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