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

Hyo Young Kim; Seunghoo Kim; Hyewon Youn; June Key Chung; Dong Hae Shin; Kyunglim Lee

doi:10.1016/j.biomaterials.2011.03.074

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

Hyo Young Kim, Seunghoo Kim, Hyewon Youn, June Key Chung, Dong Hae Shin, Kyunglim Lee

Department of Pharmaceutical Sciences

Research output: Contribution to journal › Article › peer-review

56 Scopus citations

Abstract

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 μmol/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.

Original language	English
Pages (from-to)	5262-5268
Number of pages	7
Journal	Biomaterials
Volume	32
Issue number	22
DOIs	https://doi.org/10.1016/j.biomaterials.2011.03.074
State	Published - Aug 2011

Bibliographical note

Funding Information:
This study was supported by a grant of the Seoul R&BD Program ( ST090801 ), NRF of Korea Grant funded by the Korean Government ( 2009-0064401 ), Korea Healthcare technology R&D Project , Ministry for Health, Welfare & Family Affairs ( A090030 ), Mid-career Research Program through NRF grant funded by the MEST ( R01-2007-000-20263-0 ), and the NCRC program of MOST/KOSEF ( R15-2006-020 ).

Keywords

Apoptosis
Cancer
Molecular imaging
Protein transduction domain
TCTP

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.biomaterials.2011.03.074

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

abstract = "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 μmol/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.",

keywords = "Apoptosis, Cancer, Molecular imaging, Protein transduction domain, TCTP",

author = "Kim, {Hyo Young} and Seunghoo Kim and Hyewon Youn and Chung, {June Key} and Shin, {Dong Hae} and Kyunglim Lee",

note = "Funding Information: This study was supported by a grant of the Seoul R&BD Program ( ST090801 ), NRF of Korea Grant funded by the Korean Government ( 2009-0064401 ), Korea Healthcare technology R&D Project , Ministry for Health, Welfare & Family Affairs ( A090030 ), Mid-career Research Program through NRF grant funded by the MEST ( R01-2007-000-20263-0 ), and the NCRC program of MOST/KOSEF ( R15-2006-020 ).",

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doi = "10.1016/j.biomaterials.2011.03.074",

language = "English",

volume = "32",

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T1 - The cell penetrating ability of the proapoptotic peptide, KLAKLAKKLAKLAK fused to the N-terminal protein transduction domain of translationally controlled tumor protein, MIIYRDLISH

AU - Kim, Hyo Young

AU - Kim, Seunghoo

AU - Youn, Hyewon

AU - Chung, June Key

AU - Shin, Dong Hae

AU - Lee, Kyunglim

N1 - Funding Information: This study was supported by a grant of the Seoul R&BD Program ( ST090801 ), NRF of Korea Grant funded by the Korean Government ( 2009-0064401 ), Korea Healthcare technology R&D Project , Ministry for Health, Welfare & Family Affairs ( A090030 ), Mid-career Research Program through NRF grant funded by the MEST ( R01-2007-000-20263-0 ), and the NCRC program of MOST/KOSEF ( R15-2006-020 ).

PY - 2011/8

Y1 - 2011/8

N2 - 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 μmol/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.

AB - 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 μmol/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.

KW - Apoptosis

KW - Cancer

KW - Molecular imaging

KW - Protein transduction domain

KW - TCTP

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

Abstract

Bibliographical note

Keywords

UN SDGs

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