| Literature DB >> 32875355 |
Sophie Mouillet-Richard1, Fatima Djouadi2, Fatima-Zohra Boufroura3, Céline Tomkiewicz-Raulet4, Virginie Poindessous3, Johan Castille5, Jean-Luc Vilotte5, Jean Bastin3.
Abstract
Inherited fatty acid oxidation diseases in their mild forms often present as metabolic myopathies. Carnitine Palmitoyl Transferase 2 (CPT2) deficiency, one such prototypical disorder is associated with compromised myotube differentiation. Here, we show that CPT2-deficient myotubes exhibit defects in focal adhesions and redox balance, exemplified by increased SOD2 expression. We document unprecedented alterations in the cellular prion protein PrPC, which directly arise from the failure in CPT2 enzymatic activity. We also demonstrate that the loss of PrPC function in normal myotubes recapitulates the defects in focal adhesion, redox balance and differentiation hallmarks monitored in CPT2-deficient cells. These results are further corroborated by studies performed in muscles from Prnp-/- mice. Altogether, our results unveil a molecular scenario, whereby PrPC dysfunction governed by faulty CPT2 activity may drive aberrant focal adhesion turnover and hinder proper myotube differentiation. Our study adds a novel facet to the involvement of PrPC in diverse physiopathological situations.Entities:
Keywords: Cellular prion protein; Focal adhesions; Inherited fatty acid oxidation disorders; Inherited metabolic myopathy; Muscle differentiation; Redox balance
Year: 2020 PMID: 32875355 DOI: 10.1007/s00018-020-03624-6
Source DB: PubMed Journal: Cell Mol Life Sci ISSN: 1420-682X Impact factor: 9.261