动脉粥样硬化(Atherosclerosis,AS)是心脑血管疾病的病理基础,其发病机制备受关注,但至今尚未阐明。近些年来,研究TLR4(Toll like receptor 4)信号通路在AS中的作用机制成为心血管领域中的热点。本文就TLR4及其抑制剂A20、SOCS1、RP105...动脉粥样硬化(Atherosclerosis,AS)是心脑血管疾病的病理基础,其发病机制备受关注,但至今尚未阐明。近些年来,研究TLR4(Toll like receptor 4)信号通路在AS中的作用机制成为心血管领域中的热点。本文就TLR4及其抑制剂A20、SOCS1、RP105与AS之间关系作一综述。展开更多
We isolated cDNA encoding porcine MyD88 (poMyD88) from Peyer's patches (Pps) of GALT. The complete open reading frame (ORF) of poMyD88 contains 879 bp encoding a deduced 293 aa residues. The amino acid sequence...We isolated cDNA encoding porcine MyD88 (poMyD88) from Peyer's patches (Pps) of GALT. The complete open reading frame (ORF) of poMyD88 contains 879 bp encoding a deduced 293 aa residues. The amino acid sequence of poMyD88 was characterized by N-terminal death, intermediate and C-terminal Toll/IL-1 receptor (TIR) domains. The putative poMyD88 protein shares a higher level of homology with its human (87.2% amino acid identity) than with its mouse (77.4% amino acid identity) counterpart. Overexpression of poMyD88 participated in the further enhanced activation of NF-w.B in human embryonic kidney (HEK) 293 cells expressing porcine TLR2 and porcine TLR4/MD-2, but not porcine RP105/MD-1 after stimulation with the corresponding ligands. The expression levels of MyD88 were highest in the spleen and mesenteric lymph nodes (MLNs), and lower in digestive tissues of newborn swine. In adult swine, the expression levels in the digestive tissues were lower than those in MLNs and the spleen. These results suggest that an MyD88-dependent signaling pathway is present in newborn as well as in adult swine and that it is involved in the innate immune system of these animals.展开更多
文摘动脉粥样硬化(Atherosclerosis,AS)是心脑血管疾病的病理基础,其发病机制备受关注,但至今尚未阐明。近些年来,研究TLR4(Toll like receptor 4)信号通路在AS中的作用机制成为心血管领域中的热点。本文就TLR4及其抑制剂A20、SOCS1、RP105与AS之间关系作一综述。
文摘We isolated cDNA encoding porcine MyD88 (poMyD88) from Peyer's patches (Pps) of GALT. The complete open reading frame (ORF) of poMyD88 contains 879 bp encoding a deduced 293 aa residues. The amino acid sequence of poMyD88 was characterized by N-terminal death, intermediate and C-terminal Toll/IL-1 receptor (TIR) domains. The putative poMyD88 protein shares a higher level of homology with its human (87.2% amino acid identity) than with its mouse (77.4% amino acid identity) counterpart. Overexpression of poMyD88 participated in the further enhanced activation of NF-w.B in human embryonic kidney (HEK) 293 cells expressing porcine TLR2 and porcine TLR4/MD-2, but not porcine RP105/MD-1 after stimulation with the corresponding ligands. The expression levels of MyD88 were highest in the spleen and mesenteric lymph nodes (MLNs), and lower in digestive tissues of newborn swine. In adult swine, the expression levels in the digestive tissues were lower than those in MLNs and the spleen. These results suggest that an MyD88-dependent signaling pathway is present in newborn as well as in adult swine and that it is involved in the innate immune system of these animals.