Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The neurohypophyseal nonapeptide arginine8-vasopressin (AVP) induces phosphoinositide turnover and calcium and pH changes in skeletal myogenic cells in culture. In order to investigate the effect of AVP on skeletal myogenesis, we examined the effect of this hormone on proliferating mononucleated L6 myoblast cultures. Addition of AVP to the medium resulted in the formation of much larger myotubes than those formed in its absence and in a significant increase (2.2-fold) of the percentage of fusion within 3-4 days of treatment. The effect of AVP was dose dependent, in the 10 nM to 1 microM range, and was observed also in primary cultures of mouse satellite cells. The rate of growth of L6 cells was not affected by AVP treatment. The induction of morphological differentiation by AVP correlated with an increased expression of muscle-specific gene products, such as myosin, and an increased number of acetylcholine receptor sites. The accumulation of mRNA transcripts of the acetylcholine receptor subunits was also enhanced by AVP. The mechanism involved in the myogenic action of AVP was investigated. Using AVP-related peptides and antagonists, we found that a specific chemical structure is required and that V1 receptors probably mediate the effect on myogenesis. Expression of muscle-specific transcription factor genes Myf-5 and myogenin and their products are strongly upregulated by AVP. Our findings support the hypothesis that AVP may represent a novel physiological modulator of skeletal muscle differentiation through its action on muscle regulatory genes.
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PMID:Arginine-vasopressin induces differentiation of skeletal myogenic cells and up-regulation of myogenin and Myf-5. 771 87

Terminal differentiation of myogenic cells has long been known to be positively regulated by insulin-like growth factors (IGFs). Arg8-vasopressin (AVP) has been recently reported to potently induce myogenic differentiation. In the present study, the effects and the mechanisms of action of AVP and IGFs on myogenic cells have been investigated under conditions allowing growth and differentiation of myogenic cells in a simple serum-free medium. Under these conditions, L6 and L5 myogenic cells slowly proliferate and do not undergo differentiation (less than 1% fusion up to 7 days). AVP rapidly (2-3 days) and dose-dependently induces the formation of multinucleated myotubes. Creatine kinase activity and myosin accumulation are strongly up-regulated by AVP. Insulin or IGF-I or IGF-II, at concentrations that cause extensive differentiation in serum-containing medium, induces a modest degree of differentiation in serum-free medium. The simultaneous presence of AVP and of one of the IGFs in the synthetic medium induces maximal differentiation of L6, L5, and satellite cells. The expression of both myogenin and Myf-5 is dramatically stimulated by AVP. Our results indicate that AVP induces a significant level of myogenic differentiation in the absence of other factors. Furthermore, they suggest that to express their full myogenic potential, IGFs require the presence of other factors normally present in serum and fully mimicked by AVP. These studies support the conclusion that terminal myogenic differentiation may depend on the presence of differentiation factors rather than the absence of growth factors.
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PMID:Vasopressin and insulin-like growth factors synergistically induce myogenesis in serum-free medium. 948 52

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.
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PMID:AVP induces myogenesis through the transcriptional activation of the myocyte enhancer factor 2. 1204 25