Transcytosis mechanisms of cell-penetrating peptides: Cation-independent CC12 and cationic penetratin
文献类型:期刊论文
作者 | Zhu, Minjiao2; Liu, Haiyang3; Cao, Wenjiao2; Fang, Yuefei4; Chen, Zheng2; Qi, Xinming1![]() |
刊名 | JOURNAL OF PEPTIDE SCIENCE
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出版日期 | 2022-02-15 |
页码 | 9 |
关键词 | cell-penetrating peptides direct translocation pathway drug delivery endocytic pathway penetration transcytosis cell internalization mechanism |
ISSN号 | 1075-2617 |
DOI | 10.1002/psc.3408 |
通讯作者 | Chen, Chong(cicyheart@163.com) |
英文摘要 | Cell-penetrating peptides (CPPs) can aid in intracellular and in vivo drug delivery. However, the mechanisms of CPP-mediated penetration remain unclear, limiting the development and further application of CPPs. Flow cytometry and laser confocal fluorescence microscopy were performed to detect the effects of different endocytosis inhibitors on the internalization of CC12 and penetratin in ARPE-19 cells. The co-localization of CPPs with the lysosome and macropinosome was detected via an endocytosis tracing experiment. The flow cytometry results showed that chlorpromazine, wortmannin, cytochalasin D, and the ATP inhibitor oligomycin had dose-dependent endocytosis-inhibitory effects on CC12. The laser confocal fluorescence results showed that oligomycin had the most significant inhibitory effect on CC12 uptake; CC12 was co-located with the lysosome, but not with the macropinosome. For penetratin, cytochalasin D and oligomycin had obvious inhibitory effects. The laser confocal fluorescence results indicated that oligomycin had the most significant inhibitory effect on penetratin uptake; the co-localization of penetratin with the lysosome was higher than that with the macropinosome. Cation-independent CC12 and cationic penetratin may be internalized into cells primarily through caveolae and clathrin-mediated endocytosis, and they are typically dependent on ATP. The transport of penetratin could be partly achieved through the direct transmembrane pathway, as the positive charge of penetratin interacts with the negative charge of the cell membrane, and partly through the endocytic pathway. |
WOS关键词 | TAT PEPTIDE ; PROTEINS ; ENDOCYTOSIS ; DELIVERY |
资助项目 | Shanghai Sailing Program[18YF1419700] ; National Natural Science Foundation of China[81800835] ; National Natural Science Foundation of China[81970810] ; Shanghai Jiao Tong University[YG2021QN136] ; Shanghai Jiao Tong University[YG2019QNA59] ; Shanghai Rising Stars of Medical Talent Youth Development Program ; Shanghai Talent Development Fund |
WOS研究方向 | Biochemistry & Molecular Biology ; Chemistry |
语种 | 英语 |
WOS记录号 | WOS:000755360000001 |
出版者 | WILEY |
源URL | [http://119.78.100.183/handle/2S10ELR8/300418] ![]() |
专题 | 新药研究国家重点实验室 |
通讯作者 | Chen, Chong |
作者单位 | 1.Chinese Acad Sci, Ctr Drug Safety Evaluat & Res, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai, Peoples R China 2.Shanghai Jiao Tong Univ, Shanghai Key Lab Embryo Original Dis, Shanghai Municipal Key Clin Specialty, Sch Med,Dept Obstet & Gynecol,Int Peace Matern &, Shanghai, Peoples R China 3.Peoples Hosp Dongtai, Dept Resp Med, Dongtai, Jiangsu, Peoples R China 4.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai, Peoples R China 5.Shanghai Jiao Tong Univ, Shanghai Gen Hosp,Shanghai Engn Ctr Visual Sci &, Sch Med,Shanghai Key Lab Ocular Fundus Dis, Dept Ophthalmol,Natl Clin Res Ctr Eye Dis,Shangha, 100 Haining Rd, Shanghai 200080, Peoples R China |
推荐引用方式 GB/T 7714 | Zhu, Minjiao,Liu, Haiyang,Cao, Wenjiao,et al. Transcytosis mechanisms of cell-penetrating peptides: Cation-independent CC12 and cationic penetratin[J]. JOURNAL OF PEPTIDE SCIENCE,2022:9. |
APA | Zhu, Minjiao.,Liu, Haiyang.,Cao, Wenjiao.,Fang, Yuefei.,Chen, Zheng.,...&Chen, Chong.(2022).Transcytosis mechanisms of cell-penetrating peptides: Cation-independent CC12 and cationic penetratin.JOURNAL OF PEPTIDE SCIENCE,9. |
MLA | Zhu, Minjiao,et al."Transcytosis mechanisms of cell-penetrating peptides: Cation-independent CC12 and cationic penetratin".JOURNAL OF PEPTIDE SCIENCE (2022):9. |
入库方式: OAI收割
来源:上海药物研究所
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