Cargando…

Prelamin A causes aberrant myonuclear arrangement and results in muscle fiber weakness

Physiological and premature aging are frequently associated with an accumulation of prelamin A, a precursor of lamin A, in the nuclear envelope of various cell types. Here, we aimed to underpin the hitherto unknown mechanisms by which prelamin A alters myonuclear organization and muscle fiber functi...

Descripción completa

Detalles Bibliográficos
Autores principales: Levy, Yotam, Ross, Jacob A., Niglas, Marili, Snetkov, Vladimir A., Lynham, Steven, Liao, Chen-Yu, Puckelwartz, Megan J., Hsu, Yueh-Mei, McNally, Elizabeth M., Alsheimer, Manfred, Harridge, Stephen D.R., Young, Stephen G., Fong, Loren G., Español, Yaiza, Lopez-Otin, Carlos, Kennedy, Brian K., Lowe, Dawn A., Ochala, Julien
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Clinical Investigation 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6237469/
https://www.ncbi.nlm.nih.gov/pubmed/30282816
http://dx.doi.org/10.1172/jci.insight.120920
Descripción
Sumario:Physiological and premature aging are frequently associated with an accumulation of prelamin A, a precursor of lamin A, in the nuclear envelope of various cell types. Here, we aimed to underpin the hitherto unknown mechanisms by which prelamin A alters myonuclear organization and muscle fiber function. By experimentally studying membrane-permeabilized myofibers from various transgenic mouse lines, our results indicate that, in the presence of prelamin A, the abundance of nuclei and myosin content is markedly reduced within muscle fibers. This leads to a concept by which the remaining myonuclei are very distant from each other and are pushed to function beyond their maximum cytoplasmic capacity, ultimately inducing muscle fiber weakness.