Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy

Cenni, Vittoria; Sabatelli, P.; Mattioli, E.; Marmiroli, Sandra; Capanni, C.; Ognibene, A.; Squarzoni, S.; Maraldi, Nm; Bonne, G.; Columbaro, M.; Merlini, L.; Lattanzi, G.

Background: Skeletal muscle disorders associated with mutations of lamin A/C gene include autosomal Emery-Dreifuss muscular dystrophy and limb girdle muscular dystrophy 1B. The pathogenic mechanism underlying these diseases is unknown. Recent data suggest an impairment of signalling mechanisms as a possible cause of muscle malfunction. A molecular complex in muscle cells formed by lamin A/C, emerin, and nuclear actin has been identified. The stability of this protein complex appears to be related to phosphorylation mechanisms.Objective: To analyse lamin A/C phosphorylation in control and laminopathic muscle cells.Methods: Lamin A/C N-terminal phosphorylation was determined in cultured mouse myoblasts using a specific antibody. Insulin treatment of serum starved myoblast cultures was carried out to evaluate involvement of insulin signalling in the phosphorylation pathway. Screening of four Emery-Dreifuss and one limb girdle muscular dystrophy 1B cases was undertaken to investigate lamin A/C phosphorylation in both cultured myoblasts and mature muscle fibres.Results: Phosphorylation of lamin A was observed during myoblast differentiation or proliferation, along with reduced lamin A/C phosphorylation in quiescent myoblasts. Lamin A N-terminus phosphorylation was induced by an insulin stimulus, which conversely did not affect lamin C phosphorylation. Lamin A/C was also hyperphosphorylated in mature muscle, mostly in regenerating fibres. Lamin A/C phosphorylation was strikingly reduced in laminopathic myoblasts and muscle fibres, while it was preserved in interstitial fibroblasts.Conclusions: Altered lamin A/C interplay with a muscle specific phosphorylation partner might be involved in the pathogenic mechanism of Emery-Dreifuss muscular dystrophy and limb girdle muscular dystrophy 1B.

Data di pubblicazione:	2005
Titolo:	Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy
Autore/i:	Cenni, Vittoria; P., Sabatelli; E., Mattioli; Marmiroli, Sandra; C., Capanni; A., Ognibene; S., Squarzoni; Nm, Maraldi; G., Bonne; M., Columbaro; L., Merlini; G., Lattanzi
Autore/i UNIMORE:	CENNI, Vittoria P. Sabatelli E. Mattioli MARMIROLI, Sandra C. Capanni A. Ognibene S. Squarzoni NM Maraldi G. Bonne M. Columbaro L. Merlini G. Lattanzi mostra contributor esterni nascondi contributor esterni
Rivista:	JOURNAL OF MEDICAL GENETICS
Volume:	42(3)
Pagina iniziale:	214
Pagina finale:	220
Codice identificativo ISI:	WOS:000227470300004
Codice identificativo Scopus:	2-s2.0-20144368040
Codice identificativo Pubmed:	15744034
Citazione:	Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy / Cenni, Vittoria; P., Sabatelli; E., Mattioli; Marmiroli, Sandra; C., Capanni; A., Ognibene; S., Squarzoni; Nm, Maraldi; G., Bonne; M., Columbaro; L., Merlini; G., Lattanzi. - In: JOURNAL OF MEDICAL GENETICS. - ISSN 0022-2593. - STAMPA. - 42(3)(2005), pp. 214-220.
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