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Endogenous IgG-based affinity-controlled release of TRAIL exerts superior antitumor effects

The inefficiency of recombinant tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-based clinical regimens has been dominantly attributed to the short half-life of TRAIL. Affinity-controlled release using endogenous long-acting proteins, such as IgG and albumin, as carriers is extremely...

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Autores principales: Yang, Hao, Feng, Yanru, Cai, Huawei, Jia, Dianlong, Li, Heng, Tao, Ze, Zhong, Yi, Li, Zhao, Shi, Qiuxiao, Wan, Lin, Li, Lin, Lu, Xiaofeng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Ivyspring International Publisher 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5928902/
https://www.ncbi.nlm.nih.gov/pubmed/29721092
http://dx.doi.org/10.7150/thno.23880
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author Yang, Hao
Feng, Yanru
Cai, Huawei
Jia, Dianlong
Li, Heng
Tao, Ze
Zhong, Yi
Li, Zhao
Shi, Qiuxiao
Wan, Lin
Li, Lin
Lu, Xiaofeng
author_facet Yang, Hao
Feng, Yanru
Cai, Huawei
Jia, Dianlong
Li, Heng
Tao, Ze
Zhong, Yi
Li, Zhao
Shi, Qiuxiao
Wan, Lin
Li, Lin
Lu, Xiaofeng
author_sort Yang, Hao
collection PubMed
description The inefficiency of recombinant tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-based clinical regimens has been dominantly attributed to the short half-life of TRAIL. Affinity-controlled release using endogenous long-acting proteins, such as IgG and albumin, as carriers is extremely attractive for improving the pharmacokinetics of TRAIL. Up to now, it is unclear whether IgG-binding is efficient for affinity-controlled release of TRAIL. Methods: An IgG-binding affibody, IgBD, was genetically fused to the N-terminus of TRAIL to produce IgBD-TRAIL.The IgG-binding ability, cytotoxicity, serum half-life, and in vivo antitumor effect of IgBD-TRAIL were compared with that of TRAIL. In addition, an albumin-binding affibody, ABD, was fused to TRAIL to produce ABD-TRAIL. The cytototoxicity, serum half-life, and antitumor effect of IgBD-TRAIL and ABD-TRAIL were compared. Results: IgBD fusion endowed TRAIL with high affinity (nM) for IgG without interference with its cytotoxicity. The serum half-life of IgBD-TRAIL is 50-60 times longer than that of TRAIL and the tumor uptake of IgBD-TRAIL at 8-24 h post-injection was 4-7-fold that of TRAIL. In vivo antitumor effect of IgBD-TRAIL was at least 10 times greater than that of TRAIL. Owing to the high affinity (nM) for albumin, the serum half-life of ABD-TRAIL was 80-90 times greater than that of TRAIL. However, after binding to albumin, the cytotoxicity of ABD-TRAIL was reduced more than 10 times. In contrast, binding to IgG had little impact on the cytotoxicity of IgBD-TRAIL. Consequently, intravenously injected IgBD-TRAIL showed antitumor effects superior to those of ABD-TRAIL. Conclusions: Endogenous long-acting proteins, particularly IgG-based affinity-controlled release, prolonged the serum half-life as well as significantly enhanced the antitumor effect of TRAIL. IgBD-mediated endogenous IgG binding might be a novel approach for the affinity-controlled release of other protein drugs.
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spelling pubmed-59289022018-05-02 Endogenous IgG-based affinity-controlled release of TRAIL exerts superior antitumor effects Yang, Hao Feng, Yanru Cai, Huawei Jia, Dianlong Li, Heng Tao, Ze Zhong, Yi Li, Zhao Shi, Qiuxiao Wan, Lin Li, Lin Lu, Xiaofeng Theranostics Research Paper The inefficiency of recombinant tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-based clinical regimens has been dominantly attributed to the short half-life of TRAIL. Affinity-controlled release using endogenous long-acting proteins, such as IgG and albumin, as carriers is extremely attractive for improving the pharmacokinetics of TRAIL. Up to now, it is unclear whether IgG-binding is efficient for affinity-controlled release of TRAIL. Methods: An IgG-binding affibody, IgBD, was genetically fused to the N-terminus of TRAIL to produce IgBD-TRAIL.The IgG-binding ability, cytotoxicity, serum half-life, and in vivo antitumor effect of IgBD-TRAIL were compared with that of TRAIL. In addition, an albumin-binding affibody, ABD, was fused to TRAIL to produce ABD-TRAIL. The cytototoxicity, serum half-life, and antitumor effect of IgBD-TRAIL and ABD-TRAIL were compared. Results: IgBD fusion endowed TRAIL with high affinity (nM) for IgG without interference with its cytotoxicity. The serum half-life of IgBD-TRAIL is 50-60 times longer than that of TRAIL and the tumor uptake of IgBD-TRAIL at 8-24 h post-injection was 4-7-fold that of TRAIL. In vivo antitumor effect of IgBD-TRAIL was at least 10 times greater than that of TRAIL. Owing to the high affinity (nM) for albumin, the serum half-life of ABD-TRAIL was 80-90 times greater than that of TRAIL. However, after binding to albumin, the cytotoxicity of ABD-TRAIL was reduced more than 10 times. In contrast, binding to IgG had little impact on the cytotoxicity of IgBD-TRAIL. Consequently, intravenously injected IgBD-TRAIL showed antitumor effects superior to those of ABD-TRAIL. Conclusions: Endogenous long-acting proteins, particularly IgG-based affinity-controlled release, prolonged the serum half-life as well as significantly enhanced the antitumor effect of TRAIL. IgBD-mediated endogenous IgG binding might be a novel approach for the affinity-controlled release of other protein drugs. Ivyspring International Publisher 2018-03-28 /pmc/articles/PMC5928902/ /pubmed/29721092 http://dx.doi.org/10.7150/thno.23880 Text en © Ivyspring International Publisher This is an open access article distributed under the terms of the Creative Commons Attribution (CC BY-NC) license (https://creativecommons.org/licenses/by-nc/4.0/). See http://ivyspring.com/terms for full terms and conditions.
spellingShingle Research Paper
Yang, Hao
Feng, Yanru
Cai, Huawei
Jia, Dianlong
Li, Heng
Tao, Ze
Zhong, Yi
Li, Zhao
Shi, Qiuxiao
Wan, Lin
Li, Lin
Lu, Xiaofeng
Endogenous IgG-based affinity-controlled release of TRAIL exerts superior antitumor effects
title Endogenous IgG-based affinity-controlled release of TRAIL exerts superior antitumor effects
title_full Endogenous IgG-based affinity-controlled release of TRAIL exerts superior antitumor effects
title_fullStr Endogenous IgG-based affinity-controlled release of TRAIL exerts superior antitumor effects
title_full_unstemmed Endogenous IgG-based affinity-controlled release of TRAIL exerts superior antitumor effects
title_short Endogenous IgG-based affinity-controlled release of TRAIL exerts superior antitumor effects
title_sort endogenous igg-based affinity-controlled release of trail exerts superior antitumor effects
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5928902/
https://www.ncbi.nlm.nih.gov/pubmed/29721092
http://dx.doi.org/10.7150/thno.23880
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