This Article Full Text Full Text (PDF) Purchase Article View Shopping Cart Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Scicchitano, B. M. Articles by Nervi, C. Search for Related Content PubMed PubMed Citation Articles by Scicchitano, B. M. Articles by Nervi, C.

AVP Induces Myogenesis through the Transcriptional Activation of the Myocyte Enhancer Factor 2

Department of Histology and Medical Embryology, University of Rome "La Sapienza," 00161 Roma, Italy

Address all correspondence and requests for reprints to: Clara Nervi, M.D., Ph.D., Department of Histology and Medical Embryology, University of Roma "La Sapienza," Via A. Borelli 50, 00161 Rome, Italy. E-mail: clara.nervi{at}uniroma1.it.

The neurohypophyseal nonapeptide Arg⁸ vasopressin (AVP) promotes differentiation of cultured L6 and L5 myogenic cell lines and mouse primary satellite cells. Here, we investigated the molecular mechanism involved in the induction of the myogenic program by AVP. In L6 cells, AVP treatment rapidly induces Myf-5, myogenin, and myocyte enhancer factor 2 (MEF2) mRNAs, without affecting the expression of known myogenic growth factors such as IGF-I, IGF-II, or their receptors. In the presence of cycloheximide, AVP up-regulates the expression of MEF2, but not of myogenin, indicating that the synthesis of a protein intermediate is not necessary for MEF2 induction. Notably, AVP treatment activates a calcium/calmodulin kinase signaling pathway that induces cytosolic compartmentalization of the histone deacetylase 4, a mechanism related to the transcriptional activation of MEF2. The activity of chloramphenicol acetyltransferase reporter constructs carrying the Myo184 and Myo84 fragments of the myogenin promoter is also induced by AVP. Mutation of the MEF2 site completely abolishes the response to AVP, whereas deletion of the E1 site present in pMyo84 does not impair this response. Together, these results show that AVP induces myogenic differentiation through the transcriptional activation of MEF2, a mechanism that is critical for myogenesis.

This article has been cited by other articles:

				N. Gassanov, M. Jankowski, B. Danalache, D. Wang, R. Grygorczyk, U. C. Hoppe, and J. Gutkowska Arginine Vasopressin-mediated Cardiac Differentiation: INSIGHTS INTO THE ROLE OF ITS RECEPTORS AND NITRIC OXIDE SIGNALING J. Biol. Chem., April 13, 2007; 282(15): 11255 - 11265. [Abstract] [Full Text] [PDF]

				B. M. Scicchitano, L. Spath, A. Musaro, M. Molinaro, N. Rosenthal, C. Nervi, and S. Adamo Vasopressin-dependent Myogenic Cell Differentiation Is Mediated by Both Ca2+/Calmodulin-dependent Kinase and Calcineurin Pathways Mol. Biol. Cell, August 1, 2005; 16(8): 3632 - 3641. [Abstract] [Full Text] [PDF]

				H. Komati, F. Naro, S. Mebarek, V. De Arcangelis, S. Adamo, M. Lagarde, A.-F. Prigent, and G. Nemoz Phospholipase D Is Involved in Myogenic Differentiation through Remodeling of Actin Cytoskeleton Mol. Biol. Cell, March 1, 2005; 16(3): 1232 - 1244. [Abstract] [Full Text] [PDF]