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S100B protein in myoblasts modulates myogenic differentiation via NF-kappaB-dependent inhibition of MyoD expression.
J Cell Physiol. 2010 Apr; 223(1):270-82.JC

Abstract

S100B, a Ca(2+)-binding protein of the EF-hand type, is expressed in myoblasts, the precursors of skeletal myofibers, and muscle satellite cells (this work). S100B has been shown to participate in the regulation of several intracellular processes including cell cycle progression and differentiation. We investigated regulatory activities of S100B within myoblasts by stable overexpression of S100B and by inhibition of S100B expression. Overexpression of S100B in myoblast cell lines and primary myoblasts resulted in inhibition of myogenic differentiation, evidenced by lack of expression of myogenin and myosin heavy chain (MyHC) and absence of myotube formation. S100B-overexpressing myoblasts showed reduced MyoD expression levels and unchanged Myf5 expression levels, compared with control myoblasts, and transient transfection of S100B-overexpressing myoblasts with MyoD, but not Myf5, restored differentiation and fusion in part. The transcriptional activity of NF-kappaB, a negative regulator of MyoD expression, was enhanced in S100B-overexpressing myoblasts, and blocking NF-kappaB activity resulted in reversal of S100B's inhibitory effects. Yin Yang1, a transcriptional repressor that is induced by NF-kappaB (p65) and mediates NF-kappaB inhibitory effects on several myofibrillary genes, also was upregulated in S100B-overexpressing myoblasts. Conversely, silencing S100B expression in myoblast cell lines by RNA interference resulted in reduced NF-kappaB activity and enhanced MyoD, myogenin and MyHC expression and myotube formation. Thus, intracellular S100B might modulate myoblast differentiation by interfering with MyoD expression in an NF-kappaB-dependent manner.

Authors+Show Affiliations

Department of Experimental Medicine and Biochemical Sciences, University of Perugia, Perugia, Italy.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

20069545

Citation

Tubaro, Claudia, et al. "S100B Protein in Myoblasts Modulates Myogenic Differentiation Via NF-kappaB-dependent Inhibition of MyoD Expression." Journal of Cellular Physiology, vol. 223, no. 1, 2010, pp. 270-82.
Tubaro C, Arcuri C, Giambanco I, et al. S100B protein in myoblasts modulates myogenic differentiation via NF-kappaB-dependent inhibition of MyoD expression. J Cell Physiol. 2010;223(1):270-82.
Tubaro, C., Arcuri, C., Giambanco, I., & Donato, R. (2010). S100B protein in myoblasts modulates myogenic differentiation via NF-kappaB-dependent inhibition of MyoD expression. Journal of Cellular Physiology, 223(1), 270-82. https://doi.org/10.1002/jcp.22035
Tubaro C, et al. S100B Protein in Myoblasts Modulates Myogenic Differentiation Via NF-kappaB-dependent Inhibition of MyoD Expression. J Cell Physiol. 2010;223(1):270-82. PubMed PMID: 20069545.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - S100B protein in myoblasts modulates myogenic differentiation via NF-kappaB-dependent inhibition of MyoD expression. AU - Tubaro,Claudia, AU - Arcuri,Cataldo, AU - Giambanco,Ileana, AU - Donato,Rosario, PY - 2010/1/14/entrez PY - 2010/1/14/pubmed PY - 2010/3/10/medline SP - 270 EP - 82 JF - Journal of cellular physiology JO - J Cell Physiol VL - 223 IS - 1 N2 - S100B, a Ca(2+)-binding protein of the EF-hand type, is expressed in myoblasts, the precursors of skeletal myofibers, and muscle satellite cells (this work). S100B has been shown to participate in the regulation of several intracellular processes including cell cycle progression and differentiation. We investigated regulatory activities of S100B within myoblasts by stable overexpression of S100B and by inhibition of S100B expression. Overexpression of S100B in myoblast cell lines and primary myoblasts resulted in inhibition of myogenic differentiation, evidenced by lack of expression of myogenin and myosin heavy chain (MyHC) and absence of myotube formation. S100B-overexpressing myoblasts showed reduced MyoD expression levels and unchanged Myf5 expression levels, compared with control myoblasts, and transient transfection of S100B-overexpressing myoblasts with MyoD, but not Myf5, restored differentiation and fusion in part. The transcriptional activity of NF-kappaB, a negative regulator of MyoD expression, was enhanced in S100B-overexpressing myoblasts, and blocking NF-kappaB activity resulted in reversal of S100B's inhibitory effects. Yin Yang1, a transcriptional repressor that is induced by NF-kappaB (p65) and mediates NF-kappaB inhibitory effects on several myofibrillary genes, also was upregulated in S100B-overexpressing myoblasts. Conversely, silencing S100B expression in myoblast cell lines by RNA interference resulted in reduced NF-kappaB activity and enhanced MyoD, myogenin and MyHC expression and myotube formation. Thus, intracellular S100B might modulate myoblast differentiation by interfering with MyoD expression in an NF-kappaB-dependent manner. SN - 1097-4652 UR - https://www.unboundmedicine.com/medline/citation/20069545/S100B_protein_in_myoblasts_modulates_myogenic_differentiation_via_NF_kappaB_dependent_inhibition_of_MyoD_expression_ L2 - https://doi.org/10.1002/jcp.22035 DB - PRIME DP - Unbound Medicine ER -