TY - JOUR
T1 - Hyaluronic acid and its derivative as a multi-functional gene expression enhancer
T2 - Protection from non-specific interactions, adhesion to targeted cells, and transcriptional activation
AU - Ito, Tomoko
AU - Iida-Tanaka, Naoko
AU - Niidome, Takuro
AU - Kawano, Takahito
AU - Kubo, Koji
AU - Yoshikawa, Kenichi
AU - Sato, Toshinori
AU - Yang, Zhihong
AU - Koyama, Yoshiyuki
N1 - Funding Information:
The authors thank Prof. Tatsuo Akitaya (Meijo University) and Dr. Kanta Tsumoto (Mie University) for their helpful suggestions in the transcription study. This work was supported by Japan Society for the Promotion of Science (No. 00162090).
PY - 2006/5/30
Y1 - 2006/5/30
N2 - Hyaluronic acid (HA), a natural anionic mucopolysaccharide, can be deposited onto the cationic surface of DNA/polyethyleneimine (PEI) complexes to recharge the surface potential and reduce nonspecific interactions with proteins. HA can also be used as a ligand to target specific cell receptors. Furthermore, HA-coating enhanced the transcriptional activity of the plasmid/PEI complexes, probably by loosening the tight binding between DNA and PEI, which facilitated the approach of transcription factors. Amphoteric HA derivative having spermine side chains (Spn-HA) with a structure similar to HMG protein showed higher transcription-enhancing activity than HA. Plasmid/PEI/Spn-HA ternary complex exhibited 29-fold higher transgene expression efficiency than naked plasmid/PEI complexes in CHO cells.
AB - Hyaluronic acid (HA), a natural anionic mucopolysaccharide, can be deposited onto the cationic surface of DNA/polyethyleneimine (PEI) complexes to recharge the surface potential and reduce nonspecific interactions with proteins. HA can also be used as a ligand to target specific cell receptors. Furthermore, HA-coating enhanced the transcriptional activity of the plasmid/PEI complexes, probably by loosening the tight binding between DNA and PEI, which facilitated the approach of transcription factors. Amphoteric HA derivative having spermine side chains (Spn-HA) with a structure similar to HMG protein showed higher transcription-enhancing activity than HA. Plasmid/PEI/Spn-HA ternary complex exhibited 29-fold higher transgene expression efficiency than naked plasmid/PEI complexes in CHO cells.
KW - HMG
KW - Hyaluronic acid
KW - Transcription
KW - Transfection
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U2 - 10.1016/j.jconrel.2006.03.013
DO - 10.1016/j.jconrel.2006.03.013
M3 - Article
C2 - 16647780
AN - SCOPUS:33646690293
SN - 0168-3659
VL - 112
SP - 382
EP - 388
JO - Journal of Controlled Release
JF - Journal of Controlled Release
IS - 3
ER -