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Myofibrillar protein and gene expression in acute quadriplegic myopathy
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience. (neurofysiologi)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience. (neurofysiologi)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience. (neurofysiologi)
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2009 (English)In: Journal of the Neurological Sciences, ISSN 0022-510X, E-ISSN 1878-5883, Vol. 285, no 1-2, 28-38 p.Article in journal (Refereed) Published
Abstract [en]

The dramatic muscle wasting, preferential loss of myosin and impaired   muscle function in intensive care unit (ICU) patients with acute   quadriplegic myopathy (AQM) have traditionally been suggested to be the   result of proteolysis via specific proteolytic pathways. In this study   we aim to investigate the mechanisms underlying the preferential loss   of thick vs. thin filament proteins and the reassembly of the sarcomere   during the recovery process in muscle samples from ICU patients with   AQM. Quantitative and qualitative analyses of myofibrillar protein and   mRNA expression were analyzed using SDS-PAGE, confocal microscopy,   histochemistry and real-time PCR. The present results demonstrate that   the transcriptional regulation of myofibrillar protein synthesis plays   an important role in the loss of contractile proteins, as well as the   recovery of protein levels during clinical improvement, myosin in   particular, presumably in concert with proteolytic pathways, but the   mechanisms are specific to the different thick and thin filament   proteins studied.

Place, publisher, year, edition, pages
2009. Vol. 285, no 1-2, 28-38 p.
Keyword [en]
myosin, actin, myosin binding proteins, acute quadriplegic myopathy, mRNA
National Category
Medical and Health Sciences
Research subject
Clinical Neurophysiology
Identifiers
URN: urn:nbn:se:uu:diva-108256DOI: 10.1016/j.jns.2009.04.041ISI: 000270476400006OAI: oai:DiVA.org:uu-108256DiVA: diva2:234699
Available from: 2009-09-10 Created: 2009-09-10 Last updated: 2010-07-05Bibliographically approved

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