Human HOXA5 homeodomain enhances protein transduction and its application to vascular inflammation

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Title
Human HOXA5 homeodomain enhances protein transduction and its application to vascular inflammation
Author(s)
J Y Lee; Kyoung Sook Park; E J Cho; H K Joo; S K Lee; S D Lee; J B Park; S J Chang; B H Jeon
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 410, no. 2, pp. 312-316
Publication Year
2011
Abstract
Cellular protein delivery is an emerging technique by which exogenous recombinant proteins are delivered into mammalian cells across the membrane. We have developed an Escherichia coli expression vector including human specific gene sequences for protein cellular delivery. The plasmid was generated by ligation the nucleotides 770-817 of the homeobox A5 mRNA sequence which was matched with protein transduction domain (PTD) of homeodomain protein A5 (HOXA5) into pET expression vector. The cellular uptake of HOXA5-PTD-EGFP was detected in 1. min and its transduction reached a maximum at 1. h within cell lysates. The cellular uptake of HOXA5-EGFP at 37. °C was greater than in 4. °C. For study for the functional role of human HOXA5-PTD, we purified HOXA5-APE1/Ref-1 and applied it on monocyte adhesion. Pretreatment with HOXA5-APE1/Ref-1 (100. nM) inhibited TNF-α-induced monocyte adhesion to endothelial cells, compared with HOXA5-EGFP. Taken together, our data suggested that human HOXA5-PTD vector provides a powerful research tools for uncovering cellular functions of proteins or for the generation of human PTD-containing proteins.
Keyword
Cellular transductionHOXA5-APE1/Ref-1HOXA5-EGFPHuman homeodomain protein A5Monocyte adhesion
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2011.05.139
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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