Assessment of goat activin receptor type IIB knockdown by short hairpin RNAs in vitro

References

• Han HQ, Zhou X, Mitch WE, Goldberg AL. Myostatin/activin pathway antagonism: Molecular basis and therapeutic potential. Int J Biochem Cell Biol 2013;45:2333–47
   PubMed Web of Science ®Google Scholar
• Lee SJ, Reed LA, Davies MV, et al. Regulation of muscle growth by multiple ligands signaling through activin type II receptors. Proc Natl Acad Sci USA 2005;102:18117–22
   PubMed Web of Science ®Google Scholar
• Grobet L, Martin LJ, Poncelet D, et al. A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle. Nat Genet 1997;17:71–4
   PubMed Web of Science ®Google Scholar
• McPherron AC, Lee SJ. Double muscling in cattle due to mutations in the myostatin gene. Proc Natl Acad Sci USA 1997;94:12457–61
   PubMed Web of Science ®Google Scholar
• McPherron AC, Lawler AM, Lee SJ. Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature 1997;387:83–90
   PubMed Web of Science ®Google Scholar
• Lee SJ, McPherron AC. Regulation of myostatin activity and muscle growth. Proc Natl Acad Sci USA 2001;98:9306–11
   PubMed Web of Science ®Google Scholar
• Rebbapragada A, Benchabane H, Wrana JL, et al. Myostatin signals through a transforming growth factor beta-like signaling pathway to block adipogenesis. Mol Cell Biol 2003;23:7230–42
   PubMed Web of Science ®Google Scholar
• de Caestecker M. The transforming growth factor-beta superfamily of receptors. Cytokine Growth Factor Rev 2004;15:1–11
   PubMed Web of Science ®Google Scholar
• Cadena SM, Tomkinson KN, Monnell TE, et al. Administration of a soluble activin type IIB receptor promotes skeletal muscle growth independent of fiber type. J Appl Physiol 2010;109:635–42
   PubMed Web of Science ®Google Scholar
• Wells RG, Gilboa L, Sun Y, et al. Transforming growth factor-beta induces formation of a dithiothreitol-resistant type I/Type II receptor complex in live cells. J Biol Chem 1999;274:5716–22
   PubMed Web of Science ®Google Scholar
• Yamashita H, ten Dijke P, Franzen P, et al. Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta. J Biol Chem 1994;269:20172–8
   PubMed Web of Science ®Google Scholar
• Wrana JL, Attisano L, Carcamo J, et al. TGF beta signals through a heteromeric protein kinase receptor complex. Cell 1992;71:1003–14
   PubMed Web of Science ®Google Scholar
• Willis SA, Zimmerman CM, Li LI, Mathews LS. Formation and activation by phosphorylation of activin receptor complexes. Mol Endocrinol 1996;10:367–79
   PubMedGoogle Scholar
• Massague J, Wotton D. Transcriptional control by the TGF-beta/Smad signaling system. EMBO J 2000;19:1745–54
   PubMed Web of Science ®Google Scholar
• Fire A, Xu S, Montgomery MK, et al. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 1998;391:806–11
   PubMed Web of Science ®Google Scholar
• Bernstein E, Caudy AA, Hammond SM, Hannon GJ. Role for a bidentate ribonuclease in the initiation step of RNA interference. Nature 2001;409:363–6
   PubMed Web of Science ®Google Scholar
• Macrae IJ, Zhou K, Li F, et al. Structural basis for double-stranded RNA processing by Dicer. Science 2006;311:195–8
   PubMed Web of Science ®Google Scholar
• Akpan I, Goncalves MD, Dhir R, et al. The effects of a soluble activin type IIB receptor on obesity and insulin sensitivity. Int J Obes (Lond) 2009;33:1265–73
   PubMedGoogle Scholar
• Fakhfakh R, Lee SJ, Tremblay JP. Administration of a soluble activin type IIB receptor promotes the transplantation of human myoblasts in dystrophic mice. Cell Transplant 2012;21:1419–30
   PubMed Web of Science ®Google Scholar
• Fournier B, Murray B, Gutzwiller S, et al. Blockade of the activin receptor IIb activates functional brown adipogenesis and thermogenesis by inducing mitochondrial oxidative metabolism. Mol Cell Biol 2012;32:2871–9
   PubMedGoogle Scholar
• Tripathi AK, Ramani UV, Ahir VB, et al. A modified enrichment protocol for adult caprine skeletal muscle stem cell. Cytotechnology 2010;62:483–8
   Google Scholar
• Baquero-Perez B, Kuchipudi SV, Nelli RK, Chang KC. A simplified but robust method for the isolation of avian and mammalian muscle satellite cells. BMC Cell Biol 2012;13:16
   PubMedGoogle Scholar
• Liu H, Zhang R, Chen D, et al. Functional redundancy of type II BMP receptor and type IIB activin receptor in BMP2-induced osteoblast differentiation. J Cell Physiol 2012;227:952–63
   Google Scholar
• Oh SP, Li E. The signaling pathway mediated by the type IIB activin receptor controls axial patterning and lateral asymmetry in the mouse. Genes Dev 1997;11:1812–26
   PubMed Web of Science ®Google Scholar
• Bentzinger CF, Wang YX, Rudnicki MA. Building muscle: molecular regulation of myogenesis. Cold Spring Harb Perspect Biol 2012;4:1–16
   Web of Science ®Google Scholar
• Berkes CA, Tapscott SJ. MyoD and the transcriptional control of myogenesis. Semin Cell Dev Biol 2005;16:585–95
   PubMed Web of Science ®Google Scholar
• Lu J, Wei C, Zhang X, et al. The effect of myostatin silencing by lentiviral-mediated RNA interference on goat fetal fibroblasts. Mol Biol Rep 2013;40:4101–8
   PubMed Web of Science ®Google Scholar
• Liu C, Li W, Zhang X, et al. Knockdown of endogenous myostatin promotes sheep myoblast proliferation. In Vitro Cell Dev Biol Anim 2013;50:94–102
   Google Scholar
• Langley B, Thomas M, Bishop A, et al. Myostatin inhibits myoblast differentiation by down-regulating MyoD expression. J Biol Chem 2002;277:49831–40
   PubMed Web of Science ®Google Scholar
• Hennebry A, Berry C, Siriett V, et al. Myostatin regulates fiber-type composition of skeletal muscle by regulating MEF2 and MyoD gene expression. Am J Physiol Cell Physiol 2009;296:C525–34
   PubMed Web of Science ®Google Scholar
• Blais A, Tsikitis M, Acosta-Alvear D, et al. An initial blueprint for myogenic differentiation. Genes Dev 2005;19:553–69
   PubMed Web of Science ®Google Scholar
• Dedkov EI, Kostrominova TY, Borisov AB, Carlson BM. MyoD and myogenin protein expression in skeletal muscles of senile rats. Cell Tissue Res 2003;311:401–16
   Google Scholar
• Gantier MP, Williams BR. The response of mammalian cells to double-stranded RNA. Cytokine Growth Factor Rev 2007;18:363–71
   PubMed Web of Science ®Google Scholar
• Stewart CK, Li J, Golovan SP. Adverse effects induced by short hairpin RNA expression in porcine fetal fibroblasts. Biochem Biophys Res Commun 2008;370:113–17
   PubMed Web of Science ®Google Scholar
• Tripathi AK, Aparnathi MK, Patel AK, Joshi CG. In vitro silencing of myostatin gene by shRNAs in chicken embryonic myoblast cells. Biotechnol Prog 2013;29:425–31
   Google Scholar
• Tripathi AK, Ramani UV, Patel AK, et al. Short hairpin RNA-induced myostatin gene silencing in caprine myoblast cells in vitro. Appl Biochem Biotechnol 2013;169:688–94
   PubMed Web of Science ®Google Scholar