Olivé, Montse and Engvall, Martin and Ravenscroft, Gianina and Cabrera-Serrano, Macarena and Jiao, Hong and Bortolotti, Carlo Augusto and Pignataro, Marcello and Lambrughi, Matteo and Jiang, Haibo and Forrest, Alistair R. R. and Benseny-Cases, Núria and Hofbauer, Stefan and Obinger, Christian and Battistuzzi, Gianantonio and Bellei, Marzia and Borsari, Marco and Di Rocco, Giulia and Viola, Helena M. and Hool, Livia C. and Cladera, Josep and Lagerstedt-Robinson, Kristina and Xiang, Fengqing and Wredenberg, Anna and Miralles, Francesc and Baiges, Juan José and Malfatti, Edoardo and Romero, Norma B. and Streichenberger, Nathalie and Vial, Christophe and Claeys, Kristl G. and Straathof, Chiara S. M. and Goris, An and Freyer, Christoph and Lammens, Martin and Bassez, Guillaume and Kere, Juha and Clemente, Paula and Sejersen, Thomas and Udd, Bjarne and Vidal, Noemí and Ferrer, Isidre and Edström, Lars and Wedell, Anna and Laing, Nigel G. (2019) Myoglobinopathy is an adult-onset autosomal dominant myopathy with characteristic sarcoplasmic inclusions. Nature Communications, 10 (1). p. 1396. ISSN 2041-1723
Full text not available from this repository.Abstract
Myoglobin, encoded by MB, is a small cytoplasmic globular hemoprotein highly expressed in cardiac myocytes and oxidative skeletal myofibers. Myoglobin binds O2, facilitates its intracellular transport and serves as a controller of nitric oxide and reactive oxygen species. Here, we identify a recurrent c.292C>T (p.His98Tyr) substitution in MB in fourteen members of six European families suffering from an autosomal dominant progressive myopathy with highly characteristic sarcoplasmic inclusions in skeletal and cardiac muscle. Myoglobinopathy manifests in adulthood with proximal and axial weakness that progresses to involve distal muscles and causes respiratory and cardiac failure. Biochemical characterization reveals that the mutant myoglobin has altered O2 binding, exhibits a faster heme dissociation rate and has a lower reduction potential compared to wild-type myoglobin. Preliminary studies show that mutant myoglobin may result in elevated superoxide levels at the cellular level. These data define a recognizable muscle disease associated with MB mutation.
| Item Type: | Article |
|---|---|
| Subjects: | R Medicine > R Medicine (General) |
| Depositing User: | Repository Administrator |
| Date Deposited: | 08 Apr 2019 03:54 |
| Last Modified: | 08 Apr 2019 03:54 |
| URI: | https://eprints.victorchang.edu.au/id/eprint/823 |
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