A novel peptide binding to the cytoplasmic domain of class A scavenger receptor reduces lipid uptake in THP-1 macrophages

被引：10

作者：

Wang, Xiaohua ^{[1
,2
,3
]}

Zheng, Yuan ^{[1
,2
]}

Xu, Yiming ^{[2
]}

Ben, Jingjing ^{[2
]}

Gao, Song ^{[2
]}

Zhu, Xudong ^{[2
]}

Zhuang, Yan ^{[2
]}

Yue, Shen ^{[2
]}

Bai, Hui ^{[2
]}

Chen, Yaoyu ^{[2
]}

Jiang, Li ^{[2
]}

Ji, Yong ^{[2
]}

Xu, Yong ^{[2
]}

Fan, Leming ^{[2
]}

Sha, Jiahao ^{[1
]}

He, Zhigang ^{[4
]}

Chen, Qi ^{[1
,2
]}

机构：

[1] Nanjing Med Univ, Inst Reprod Med, Key Lab Human Funct Genom, Nanjing 210029, Peoples R China

[2] Nanjing Med Univ, Atherosclerosis Res Ctr, Key Lab Human Funct Genom, Nanjing 210029, Peoples R China

[3] Nanjing Med Univ, Affiliated Hosp 1, Dept Pediat, Nanjing 210006, Peoples R China

[4] Harvard Univ, Sch Med, Div Neurosci, Childrens Hosp, Boston, MA 02115 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2009年 / 1791卷 / 01期

基金：

中国国家自然科学基金;

关键词：

Class A scavenger receptor (SR-A); Cytoplasmic domain; Foam cell; Phage peptide library; Acetylated low density lipoprotein (AcLDL); Atherosclerosis; LIGAND-BINDING; PROTEIN-KINASE; TAT PEPTIDE; FOAM CELL; ATHEROSCLEROSIS; INTERNALIZATION; ACCUMULATION; LIPOPROTEINS; INFLAMMATION; PATHWAYS;

D O I：

10.1016/j.bbalip.2008.10.011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Class A scavenger receptor (SR-A) contributes primarily to lipid accumulation in cells. The cytoplasmic domain of SR-A (CSR-A) is responsible for internalization of the receptor-ligand complex into cells. In the present study we tried to reduce cellular uptake of acetylated low density lipoprotein (AcLDL) by inducing the interaction between the CSR-A and a novel peptide H11, which was screened from a phage-displayed peptide library. When H11 was fused with a cross membrane peptide TAT, the fusion peptide could enter cell efficiently. The peptide H11 inhibited the binding and uptake of Dil-AcLDL and attenuated lipid accumulation in the differentiated human acute monocytic leukemia cell line (THP-1) macrophages. Furthermore, the interaction of peptide H11 with the CSR-A inhibited the expression of SR-A protein as well as the phosphorylation of c-jun N-terminal kinase 2 (JNK2) in cells, which mediates cellular lipid accumulation-related signaling pathways. These results suggest that the CSR-A can be a potential target to prevent lipid accumulation in cells. The peptide H11 may be useful in regulating SR-A functions in macrophages. (C) 2008 Elsevier B.V. All rights reserved.

引用

页码：76 / 83

页数：8

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