Staurosporine treatment and serum starvation promote the cleavage of emerin in cultured mouse myoblasts: involvement of a caspase‐dependent mechanism

FEBS Letters

Squarzoni, Stefano¹  Mattioli, Elisabetta³  Columbaro, Marta³  Rutigliano, Cristina²  Maraldi, Nadir Mario¹  Ognibene, Andrea²  Lattanzi, Giovanna¹ 

[1] Institute of Normal and Pathological Cytomorphology, CNR, c/o IOR, Via di Barbiano, 1/10, I-40136 Bologna, Italy;Laboratory of Cell Biology and Electron Microscopy, IOR, Bologna, Italy;Laboratory of Neuromuscular Pathology, IOR, Bologna, Italy

关键词: Emerin;    Apoptosis;    Myoblast;    Nuclear envelope;    Caspase 3;    Caspase 6;    LAP2;    lamina associated polypeptide 2;    LBR;    lamin B receptor;    PARP;    poly(ADP-ribose)polymerase;    EDMD;    Emery–Dreifuss muscular dystrophy;    FCS;    fetal calf serum;    TUNEL;    terminal transferase-mediated dUTP nick end-labeling;   

DOI  :  10.1016/S0014-5793(01)03203-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Emerin is a nuclear membrane-anchored protein which is absent or mutated in patients affected by Emery–Dreifuss muscular dystrophy. In this study, we induced apoptosis in cultured mouse myoblasts to evaluate emerin fate during the nuclear destabilization involved in programmed cell death. Emerin proteolysis was observed in myocytes during the apoptotic process. Myoblast apoptosis and emerin degradation were associated with chromatin compaction and detachment from the nuclear lamina, as detected by electron microscopy. In vivo specific inhibition of caspase 3 or caspase 6 activity completely abolished emerin proteolysis. These results show that the process of programmed cell death in muscle cells leads to emerin proteolysis, which appears to be related to caspase 6 activation and to cleavage of other nuclear envelope proteins, that share sequence homologies or functional features with emerin.

【 授权许可】

Unknown