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Nerve influence on myosin light chain phosphorylation in slow and fast skeletal muscles.
FEBS J. 2005 Nov; 272(22):5771-85.FJ

Abstract

Neural stimulation controls the contractile properties of skeletal muscle fibres through transcriptional regulation of a number of proteins, including myosin isoforms. To study whether neural stimulation is also involved in the control of post-translational modifications of myosin, we analysed the phosphorylation of alkali myosin light chains (MLC1) and regulatory myosin light chains (MLC2) in rat slow (soleus) and fast (extensor digitorum longus EDL) muscles using 2D-gel electrophoresis and mass spectrometry. In control rats, soleus and EDL muscles differed in the proportion of the fast and slow isoforms of MLC1 and MLC2 that they contained, and also in the distribution of the variants with distinct isoelectric points identified on 2D gels. Denervation induced a slow-to-fast transition in myosin isoforms and increased MLC2 phosphorylation in soleus, whereas the opposite changes in myosin isoform expression and MLC2 phosphorylation were observed in EDL. Chronic low-frequency stimulation of EDL, with a pattern mimicking that of soleus, induced a fast-to-slow transition in myosin isoforms, accompanied by a decreased MLC2 phosphorylation. Chronic administration (10 mg x kg(-1) x d(-1) intraperitoneally) of cyclosporin A, a known inhibitor of calcineurin, did not change significantly the distribution of fast and slow MLC2 isoforms or the phosphorylation of MLC2. All changes in MLC2 phosphorylation were paralleled by changes in MLC kinase expression without any variation of the phosphatase subunit, PP1. No variation in MLC1 phosphorylation was detectable after denervation or cyclosporin A administration. These results suggest that the low-frequency neural discharge, typical of soleus, determines low levels of MLC2 phosphorylation together with expression of slow myosin, and that MLC2 phosphorylation is regulated by controlling MLC kinase expression through calcineurin-independent pathways.

Authors+Show Affiliations

Department of Anatomy and Physiology, University of Padova, Italy.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16279942

Citation

Bozzo, Cyril, et al. "Nerve Influence On Myosin Light Chain Phosphorylation in Slow and Fast Skeletal Muscles." The FEBS Journal, vol. 272, no. 22, 2005, pp. 5771-85.
Bozzo C, Spolaore B, Toniolo L, et al. Nerve influence on myosin light chain phosphorylation in slow and fast skeletal muscles. FEBS J. 2005;272(22):5771-85.
Bozzo, C., Spolaore, B., Toniolo, L., Stevens, L., Bastide, B., Cieniewski-Bernard, C., Fontana, A., Mounier, Y., & Reggiani, C. (2005). Nerve influence on myosin light chain phosphorylation in slow and fast skeletal muscles. The FEBS Journal, 272(22), 5771-85.
Bozzo C, et al. Nerve Influence On Myosin Light Chain Phosphorylation in Slow and Fast Skeletal Muscles. FEBS J. 2005;272(22):5771-85. PubMed PMID: 16279942.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Nerve influence on myosin light chain phosphorylation in slow and fast skeletal muscles. AU - Bozzo,Cyril, AU - Spolaore,Barbara, AU - Toniolo,Luana, AU - Stevens,Laurence, AU - Bastide,Bruno, AU - Cieniewski-Bernard,Caroline, AU - Fontana,Angelo, AU - Mounier,Yvonne, AU - Reggiani,Carlo, PY - 2005/11/11/pubmed PY - 2005/12/31/medline PY - 2005/11/11/entrez SP - 5771 EP - 85 JF - The FEBS journal JO - FEBS J VL - 272 IS - 22 N2 - Neural stimulation controls the contractile properties of skeletal muscle fibres through transcriptional regulation of a number of proteins, including myosin isoforms. To study whether neural stimulation is also involved in the control of post-translational modifications of myosin, we analysed the phosphorylation of alkali myosin light chains (MLC1) and regulatory myosin light chains (MLC2) in rat slow (soleus) and fast (extensor digitorum longus EDL) muscles using 2D-gel electrophoresis and mass spectrometry. In control rats, soleus and EDL muscles differed in the proportion of the fast and slow isoforms of MLC1 and MLC2 that they contained, and also in the distribution of the variants with distinct isoelectric points identified on 2D gels. Denervation induced a slow-to-fast transition in myosin isoforms and increased MLC2 phosphorylation in soleus, whereas the opposite changes in myosin isoform expression and MLC2 phosphorylation were observed in EDL. Chronic low-frequency stimulation of EDL, with a pattern mimicking that of soleus, induced a fast-to-slow transition in myosin isoforms, accompanied by a decreased MLC2 phosphorylation. Chronic administration (10 mg x kg(-1) x d(-1) intraperitoneally) of cyclosporin A, a known inhibitor of calcineurin, did not change significantly the distribution of fast and slow MLC2 isoforms or the phosphorylation of MLC2. All changes in MLC2 phosphorylation were paralleled by changes in MLC kinase expression without any variation of the phosphatase subunit, PP1. No variation in MLC1 phosphorylation was detectable after denervation or cyclosporin A administration. These results suggest that the low-frequency neural discharge, typical of soleus, determines low levels of MLC2 phosphorylation together with expression of slow myosin, and that MLC2 phosphorylation is regulated by controlling MLC kinase expression through calcineurin-independent pathways. SN - 1742-464X UR - https://www.unboundmedicine.com/medline/citation/16279942/Nerve_influence_on_myosin_light_chain_phosphorylation_in_slow_and_fast_skeletal_muscles_ L2 - https://doi.org/10.1111/j.1742-4658.2005.04965.x DB - PRIME DP - Unbound Medicine ER -