Expression of multiple nebulin isoforms in human skeletal muscle and brain
| Autor: | Petri Auvinen, Joni Keto, J. Laitila, Peter Hackman, Sari Hujanen, Carina Wallgren-Pettersson, Anders Paetau, Panu Somervuo, Mubashir Hanif, Sanna Huovinen, Katarina Pelin, Bjarne Udd |
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| Rok vydání: | 2012 |
| Předmět: |
Gene isoform
0303 health sciences Pathology medicine.medical_specialty biology Physiology Skeletal muscle medicine.disease Sarcomere 03 medical and health sciences Cellular and Molecular Neuroscience Nebulin 0302 clinical medicine medicine.anatomical_structure Nemaline myopathy Physiology (medical) medicine biology.protein Neurology (clinical) Neuron medicine.symptom Myopathy 030217 neurology & neurosurgery Actin 030304 developmental biology |
| Zdroj: | Muscle & Nerve. 46:730-737 |
| ISSN: | 0148-639X |
| DOI: | 10.1002/mus.23380 |
| Popis: | Department of Neurology, University Hospital and University of Tampere, Tampere, FinlandAccepted 6 March 2012ABSTRACT: Introduction: Nebulin is a large actin-bindingprotein of the skeletal muscle sarcomere. Multiple isoforms ofnebulin are produced from the 183-exon–containing nebulingene (NEB). Mutations in NEB cause nemaline myopathy, distalmyopathy, and core-rod myopathy. Methods: Nebulin mRNAexpression was assessed by microarrays and RT-PCR in 21human leg muscle and 2 brain samples. Protein expressionwas assessed by immunohistochemistry in 5 regions of 1 brainsample. Results: Nebulin isoform diversity is as high in brainas in skeletal muscle. Isoforms with more than 22 super repeatsseem to be more common than previously anticipated. Immuno-histochemistry showed nebulin expression predominantly in thecytoplasm of pyramidal neurons but also in the cytoplasm ofmainly subcortical endothelial cells. Conclusions: Nebulin, asin skeletal muscle, may have a role as an actin filament stabi-lizer or length regulator in neurons of the human brain, althoughpatients with NEB mutations usually have normal cognition. |
| Databáze: | OpenAIRE |
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