| Literature DB >> 15978589 |
Christoph S Clemen1, Dirk Fischer, Udo Roth, Stéphanie Simon, Patrick Vicart, Kanefusa Kato, Anna M Kaminska, Matthias Vorgerd, Lev G Goldfarb, Bruno Eymard, Norma B Romero, Bertrand Goudeau, Thomas Eggermann, Klaus Zerres, Angelika A Noegel, Rolf Schröder.
Abstract
Small heat shock proteins prevent abnormal protein folding and accumulation. We analyzed the expression of hsp27 and alphaB-crystallin in skeletal muscle specimens of patients with desminopathies, plectinopathies, myotilinopathy, and other myofibrillar myopathies by means of differential centrifugation, 2D-gel electrophoresis, Western blotting, and mass spectrometry. Hsp27-P82 and -P15 as well as alphaB-crystallin-P59 and -P45 are the major serine phosphorylation isoforms in normal and diseased human skeletal muscle. 2D-gel-electrophoresis revealed spots of hsp27 in a range of pH 5.3-6.4 in samples of all skeletal muscle specimens, except for the seven desminopathies. They indicated a shift of the main hsp27-spot to alkaline pH degrees, which may help to differentiate primary desminopathies from other myopathies with structural pathology of the desmin cytoskeleton.Entities:
Mesh：
Substances：
Year: 2005 PMID： 15978589 DOI： 10.1016/j.febslet.2005.05.051
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124