VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions
VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions
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DOI：
10.1006/excr.2001.5316
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发表时间：
2001-10-01
影响因子：
3.7
通讯作者：
Langel, U
中科院分区：
文献类型：
--
作者：
Elmquist, A;Lindgren, M;Langel, U
细胞穿透肽，CPPs，已被证明通过受体非依赖的机制转移到活细胞中，并通过质膜携带大分子。本文报道了pVEC内化的研究，pVEC是一种由小鼠细胞黏附分子血管内皮细胞钙粘蛋白615-632氨基酸序列衍生的18个氨基酸组成的多肽。荧光标记的pVEC进入了四种不同的细胞系：人主动脉内皮细胞、脑毛细血管内皮细胞、Bowes黑色素瘤细胞和小鼠脑内皮细胞。为了评估pVEC的易位效率，我们进行了与穿透性CPP的并列比较。小鼠脑内皮细胞对pVEC的摄取最高。所有测试的细胞系中pVEC的浓度都等于或略高于穿透性细胞。PVEC主要聚集在核结构中，但也可见于整个细胞。此外，pVEC作为1.7 kDa的六聚体核酸分子和67 kDa的蛋白链霉亲和素-FITC的转运体，细胞摄取荧光标记的pVEC的温度为4℃，这表明转位是一种非内吞机制。综上所述，我们的结果表明，pVEC被有效地和快速地吸收到细胞中，并作为一种有效的载体多肽发挥作用。(C)2001年学术出版社。
Cell-penetrating peptides, CPPs, have been shown to translocate into living cells by a receptor-independent mechanism and to carry macromolecules over the plasma membrane. This article reports studies of the internalization of pVEC, an 18-amino acid-long peptide derived from the murine sequence of the cell adhesion molecule vascular endothelial cadherin, amino acids 615-632. Fluorophore-labeled pVEC entered four different cell lines tested: human aortic endothelial cells, brain capillary endothelial cells, Bowes melanoma cells, and murine brain endothelial cells. In order to evaluate the translocation efficiency of pVEC, we performed a side-by-side comparison with penetratin, a well-characterized CPP. The cellular uptake of pVEC was highest for murine brain endothelial cells. All cell lines tested contained equal or slightly higher concentrations of pVEC than penetratin. pVEC mainly accumulated in nuclear structures but was also found throughout the cells. Furthermore, pVEC functioned as a transporter of both a hexameric peptide nucleic acid molecule of 1.7 kDa and a 67-kDa protein, streptavidin-FITC, and cellular uptake of fluorophore-labeled pVEC took place at 4 degreesC, suggesting a nonendocytotic mechanism of translocation. In conclusion, our results indicate that pVEC is efficiently and rapidly taken up into cells and functions as a potent carrier peptide. (C) 2001 Academic Press.