| Literature DB >> 23994228 |
Sonja Hartwig1, Silja Raschke2, Birgit Knebel1, Mika Scheler3, Martin Irmler3, Waltraud Passlack1, Stefan Muller4, Franz-Georg Hanisch4, Thomas Franz5, Xinping Li5, Hans-Dieter Dicken6, Kristin Eckardt2, Johannes Beckers7, Martin Hrabe de Angelis7, Cora Weigert8, Hans-Ulrich Häring8, Hadi Al-Hasani1, D Margriet Ouwens9, Jürgen Eckel2, Jorg Kotzka1, Stefan Lehr10.
Abstract
The skeletal muscle is a metabolically active tissue that secretes various proteins. These so-called myokines have been proposed to affect muscle physiology and to exert systemic effects on other tissues and organs. Yet, changes in the secretory profile may participate in the pathophysiology of metabolic diseases. The present study aimed at characterizing the secretome of differentiated primary human skeletal muscle cells (hSkMC) derived from healthy, adult donors combining three different mass spectrometry based non-targeted approaches as well as one antibody based method. This led to the identification of 548 non-redundant proteins in conditioned media from hSkmc. For 501 proteins, significant mRNA expression could be demonstrated. Applying stringent consecutive filtering using SignalP, SecretomeP and ER_retention signal databases, 305 proteins were assigned as potential myokines of which 12 proteins containing a secretory signal peptide were not previously described. This comprehensive profiling study of the human skeletal muscle secretome expands our knowledge of the composition of the human myokinome and may contribute to our understanding of the role of myokines in multiple biological processes. This article is part of a Special Issue entitled: Biomarkers: A Proteomic Challenge.Entities:
Keywords: Combined proteomic profiling; Mass spectrometry; Myokine; Two-dimensional gel electrophoresis
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Year: 2013 PMID: 23994228 DOI: 10.1016/j.bbapap.2013.08.004
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002