In ovo electroporation of avian somites

Scaal, Martin; Gros, Jérôme; Lesbros, Cynthia; Marcelle, Christophe

doi:10.1002/dvdy.10433

Cited by 92 publications

(73 citation statements)

References 43 publications

(38 reference statements)

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“…To start with, we tested three cationic lipids, DOTAP (Bollérot et al, 2006), DOTMA, and DODAC. (Inoue et al, 2001;Scaal et al, 2004;Baeriswyl et al, 2008;Sauka-Spengler and Barembaum, 2008). A variety of plasmids and nucleic acids can be delivered.…”

Section: Resultsmentioning

confidence: 99%

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Development of high-concentration lipoplexes for in vivo gene function studies in vertebrate embryos

et al. 2011

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Here we report that highly concentrated cationic lipid/helper lipid‐nucleic acid complexes (lipoplexes) can facilitate reproducible delivery of a variety of oligonucleotides and plasmids to chicken embryos or to mouse embryonic mesenchyme. Specifically, liposomes composed of N,N‐dioleyl‐N,N‐dimethylammonium chloride (DODAC)/1,2 dioleoyl glycero‐3‐phosphorylethanolamine (DOPE) prepared at 18‐mM concentrations produced high levels of transfection of exogenous genes in vivo and in vitro. Furthermore, we report sufficient uptake of plasmids expressing interference RNA to decrease expression of both exogenous and endogenous genes. The simplicity of preparation, implementation, and relatively low toxicity of this transfection reagent make it an attractive alternative for developmental studies in post‐gastrulation vertebrate embryos. Developmental Dynamics 240:2108–2119, 2011. © 2011 Wiley‐Liss, Inc.

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Section: Resultsmentioning

confidence: 99%

“…S2A-C, data not shown). In the case of the neural crest (Betancur et al, 2010;Rinon et al, 2011) and dermomyotome (Scaal et al, 2004;Gros et al, 2009;Wang et al, 2011), electroporation appears to result in a greater number of cells being transfected compared to our liposomes (Supp. Fig.…”

Section: Adenovirusmentioning

confidence: 96%

Development of high-concentration lipoplexes for in vivo gene function studies in vertebrate embryos

et al. 2011

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“…To test the function of BAI3 in myoblast fusion in vivo, we used in ovo electroporation to express BAI3 proteins in developing myoblasts, as previously described (39). GFP-encoding expression plasmid or human Flag-BAI3-mVenus protein or human Flag-BAI3 RKR/EEE mutant-encoding expression plasmids were microinjected into the somitocoele of developing interlimb somites of HH stage 12-17 embryos, and a current was applied (Fig.…”

Section: Lack Of Myoblast Fusion Functional Redundancy Of Bai Proteinsmentioning

confidence: 99%

G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates

Hamoud

Tran

Croteau

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

100

113

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Muscle fibers form as a result of myoblast fusion, yet the cell surface receptors regulating this process are unknown in vertebrates. In Drosophila, myoblast fusion involves the activation of the Rac pathway by the guanine nucleotide exchange factor Myoblast City and its scaffolding protein ELMO, downstream of cellsurface cell-adhesion receptors. We previously showed that the mammalian ortholog of Myoblast City, DOCK1, functions in an evolutionarily conserved manner to promote myoblast fusion in mice. In search for regulators of myoblast fusion, we identified the G-protein coupled receptor brain-specific angiogenesis inhibitor (BAI3) as a cell surface protein that interacts with ELMO. In cultured cells, BAI3 or ELMO1/2 loss of function severely impaired myoblast fusion without affecting differentiation and cannot be rescued by reexpression of BAI3 mutants deficient in ELMO binding. The related BAI protein family member, BAI1, is functionally distinct from BAI3, because it cannot rescue the myoblast fusion defects caused by the loss of BAI3 function. Finally, embryonic muscle precursor expression of a BAI3 mutant unable to bind ELMO was sufficient to block myoblast fusion in vivo. Collectively, our findings provide a role for BAI3 in the relay of extracellular fusion signals to their intracellular effectors, identifying it as an essential transmembrane protein for embryonic vertebrate myoblast fusion. myotube formation | myogenesis | model system | ced-12 | RhoGTP

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“…Recently, a gene transfer system by electroporation into aortic endothelial cell has been reported (Rossello and Torres, 2010). However, only a few studies have reported specific limb somite electroporation allowing gene expression in chick limb muscles (Krull, 2004;Scaal et al, 2004;Bonafede et al, 2006;Bonnet et al, 2010). All these studies (neural tube, aortic endothelium, and somite electroporation) used similar vectors (pCAGGS, pCAb) containing a strong and ubiquitous promoter (combination of a CMV enhancer and the chick bactin promoter), which allows efficient but transient expression of transgenes.…”

Section: Introductionmentioning

confidence: 99%

Stable, conditional, and muscle‐fiber‐specific expression of electroporated transgenes in chick limb muscle cells

Wang

Bonnet

Delfini

et al. 2010

Developmental Dynamics

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Limb muscle formation is spread out over time and, consequently, muscle cells are not easy to target at any particular stages. We aimed to design a technique to study gene function in the different steps of limb muscle formation. We have associated transposon-mediated gene transfer and a tetracycline-dependent activation method with forelimb somite electroporation. In addition, we have established a new vector combining a differentiated-muscle-cell-specific promoter and the transposon system, which allows stable gene expression in limb differentiated muscle cells and not in muscle progenitors. Using these methods, we observed that conditional Fgf4 expression in muscle cells at the onset of fetal muscle differentiation and specific Fgf4 expression in differentiated muscle cells alter muscle fiber formation in chick limbs. Limb somite electroporation with these set of vectors allowing stable, conditional, and differentiated-muscle-specific expression of transgenes opens new perspectives for investigating gene function at various steps of limb muscle formation.

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In ovo electroporation of avian somites

Cited by 92 publications

References 43 publications

Development of high-concentration lipoplexes for in vivo gene function studies in vertebrate embryos

Development of high-concentration lipoplexes for in vivo gene function studies in vertebrate embryos

G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates

Stable, conditional, and muscle‐fiber‐specific expression of electroporated transgenes in chick limb muscle cells

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