The cell penetrating ability of the proapoptotic peptide, KLAKLAKKLAKLAK fused to the N-terminal protein transduction domain of translationally controlled tumor protein, MIIYRDLISH

被引：58
|
作者：
Kim, Hyo Young [1 ]
Kim, Seunghoo [2 ,3 ]
Youn, Hyewon [2 ,4 ]
Chung, June-Key [2 ,3 ,4 ]
Shin, Dong Hae [1 ]
Lee, Kyunglim [1 ]
机构：
[1] Ewha Womans Univ, Coll Pharm, Ctr Cell Signaling & Drug Discovery Res, Seoul, South Korea
[2] Seoul Natl Univ, Dept Nucl Med, Coll Med, Seoul, South Korea
[3] Seoul Natl Univ, Canc Res Inst, Lab Mol Imaging & Therapy, Seoul, South Korea
[4] Seoul Natl Univ, Med Res Ctr, Inst Radiat Med, Seoul, South Korea
来源：
BIOMATERIALS | 2011年 / 32卷 / 22期
关键词：
Apoptosis; Cancer; Molecular imaging; Protein transduction domain; TCTP; TAT PROTEIN; APOPTOSIS; MOLECULES; MECHANISM; DELIVERY;
D O I：
10.1016/j.biomaterials.2011.03.074
中图分类号：
R318 [生物医学工程];
学科分类号：
0831 ;
摘要：
We show here, that the proapoptotic peptide, KLAKLAKKLAKLAK (KLA), which by itself does not penetrate cell membranes, can do so when fused to a protein transduction domain derived from NH2-terminus of translationally controlled tumor protein (TCTP-PTD, MIIYRDLISH). Once inside the cell, the conjugated KLA exerts its proapoptotic activity to inhibit tumor growth. We evaluated the cellular uptake of KLA fused to TCTP-PTD (hereafter called TCTP-KLA) and its effect on cancer cell viability. The IC50 of TCTP-KLA was between 7 and 10 mu mol/L. We also evaluated its anti-tumor activity in vivo by injecting it into xenografts of lung carcinoma in Balb/c nude mice. Tumor growth inhibition resulting from treatment with TCTP-KLA was better than that of TAT-KLA. These results suggest that TCTP-KLA can be applied to design cancer therapeutics. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码：5262 / 5268
页数：7
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