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肠道上皮细胞中Toll样受体4对脂多糖的细胞内识别

Intracellular recognition of lipopolysaccharide by toll-like receptor 4 in intestinal epithelial cells.

作者信息

Hornef Mathias W, Normark Birgitta Henriques, Vandewalle Alain, Normark Staffan

机构信息

Swedish Institute for Infectious Disease Control SMI, 17182 Solna, Sweden.

出版信息

J Exp Med. 2003 Oct 20;198(8):1225-35. doi: 10.1084/jem.20022194.

DOI:10.1084/jem.20022194
PMID:14568981
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2194240/
Abstract

Toll-like receptor (TLR)4 has recently been shown to reside in the Golgi apparatus of intestinal crypt epithelial m-ICcl2 cells, colocalizing with internalized lipopolysaccharide (LPS). Here we demonstrate that disruption of the integrity of the Golgi apparatus significantly reduced LPS-mediated nuclear factor kappaB activation. Also, the TLR4 adaptor protein MyD88 and the serine/threonine kinase IRAK-1 were rapidly recruited to the Golgi apparatus upon stimulation. LPS-mediated activation required lipid raft formation and intact clathrin-dependent internalization. In contrast to macrophages, prevention of ligand internalization by use of LPS-coated beads significantly impaired recognition by epithelial cells. The localization of TLR4 to the Golgi apparatus was abrogated by expression of a genetically modified form of the TLR4 binding chaperone gp96. Thus, our data provide evidence that in contrast to the situation in macrophages, LPS recognition in intestinal epithelial cells may occur in the Golgi apparatus and require LPS internalization.

摘要

Toll样受体（TLR）4最近被证明存在于肠道隐窝上皮m-ICcl2细胞的高尔基体中，与内化的脂多糖（LPS）共定位。在此，我们证明高尔基体完整性的破坏显著降低了LPS介导的核因子κB激活。此外，刺激后TLR4衔接蛋白MyD88和丝氨酸/苏氨酸激酶IRAK-1迅速募集到高尔基体。LPS介导的激活需要脂筏形成和完整的网格蛋白依赖性内化。与巨噬细胞不同，使用LPS包被的珠子阻止配体内化会显著损害上皮细胞的识别。通过表达经基因修饰的TLR4结合伴侣gp96，TLR4在高尔基体的定位被消除。因此，我们的数据提供了证据，表明与巨噬细胞的情况不同，肠道上皮细胞中LPS的识别可能发生在高尔基体中，并且需要LPS内化。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/642839ea7cf5/20022194f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/45a78b7485c6/20022194f1ad.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/e9d6c3ac37f4/20022194f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/b8d0e92385b2/20022194f3ab.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/d07a5b1488f5/20022194f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/9dc664160c35/20022194f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/d6529c94f60b/20022194f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/642839ea7cf5/20022194f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/45a78b7485c6/20022194f1ad.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/e9d6c3ac37f4/20022194f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/b8d0e92385b2/20022194f3ab.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/d07a5b1488f5/20022194f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/9dc664160c35/20022194f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/d6529c94f60b/20022194f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8afd/2194240/642839ea7cf5/20022194f7.jpg

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