Genome organization and transcriptional regulation of Adenosine Deaminase Acting on RNA gene 1 (ADAR1) in grass carp (Ctenopharyngodon idella)

Sun, Zhicheng; Wang, Binhua; Liu, Yong; Liu, Xiancheng; Mi, Yichuan; Gu, Meihui; Wang, Fang; Wu, Chuxin; Hu, Chengyu

doi:10.1016/j.dci.2015.02.006

Cited by 8 publications

(1 citation statement)

References 43 publications

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“…The RNAi technology has been widely used to regulate gene expression and shows potential for the treatment of many human disorders. To determine whether siRNA can be delivered by hPP10, hPP10‐E3 (E3, c‐terminal double‐stranded RNA binding domain from Vaccinia virus [Ostertag, Hoblitzell‐Ostertag, & Perrault, ]), and TAT‐HA‐hADR1 (hADR1, double‐stranded RNA binding domain from human adenosine deaminase [Sun et al, ; Washburn et al, ]) fusion protein encoding plasmids were constructed (Supporting Information Figure S3), and the fusion protein was prepared (Figure a and b). After G418 screening, the GFP‐expressing stable Caski cell line was established for further hPP10‐mediated siRNA transfection analysis (Supporting Information Figure S4).…”

Section: Resultsmentioning

confidence: 99%

Intracellular delivery of nucleic acid by cell‐permeable hPP10 peptide

Ding

Zhao

Geng

et al. 2018

Journal Cellular Physiology

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Although gene therapy offers hope against incurable diseases, nonreplicating transduction vectors remain lacking. We have previously characterized a cell‐penetrating peptide hPP10 for the delivery of various cargoes; however, whether hPP10 can mediate nucleic acid delivery is still unknown. Here, examining via different ways, we demonstrate that hPP10 stably complexes with plasmid DNA (pDNA) and safely mediates nucleic acid transfection. hPP10 can mediate GFP‐, dsRed‐, and luciferase‐expressing plasmids into cells with nearly the same efficiency as commercial transfection reagents Turbofectin or Lipofect. Furthermore, hPP10 can mediate Cre fusion protein delivery and pDNA transfection simultaneously in the Cre/loxp system in vitro. In addition, hPP10 fused with an RNA‐binding domain can mediate delivery of small interfering RNA into cells to silence the reporter gene expression. Collectively, our results suggest that hPP10 is an option for nucleic acid delivery with efficiencies similar to that of commercial reagents.

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Section: Resultsmentioning

confidence: 99%