Human beta-defensin DEFB126 is capable of inhibiting LPS-mediated inflammation

	Human beta-defensin DEFB126 is capable of inhibiting LPS-mediated inflammation
	Liu, HY; Yu, HG; Gu, YH; Xin, AJ; Zhang, YL; Diao, H; Lin, DH
刊名	APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
	2013
卷号	97 期号:8 页码:3395-3408
关键词	Defensin 126 LPS Anti-inflammatory Cytokines RAW264.7
通讯作者	Diao, H (reprint author), Shanghai Inst Planned Parenthood Res, NPFPC Key Lab Contracept & Devices, Shanghai 200032, Peoples R China.,diaohua@gmail.com ; dhlin@xmu.edu.cn
英文摘要	beta-Defensins are cationic, antimicrobial peptides that participate in antimicrobial defense as well as the regulation of innate and adaptive immunity. Human beta-defensin 126 (DEFB126) is a multifunctional glycoprotein consisting of a conserved beta-defensin core and a unique long glycosylated peptide tail. The long glycosylated peptide tail has been proven to be critical for efficient transport of sperm in the female reproductive tract, preventing their immune recognition, and efficient delivery of capacitated sperm to the site of fertilization. However, the functions of the conserved beta-defensin core remain to be fully elucidated. In the present work, the conserved beta-defensin core of the DEFB126 was expressed to explore its potential antimicrobial and anti-inflammatory activities. The DEFB126 core peptide exhibited both high potency for binding and neutralizing lipopolysaccharide (LPS) in vitro, and potent anti-inflammatory ability by down-regulating the mRNA expression of pro-inflammatory cytokines including IL-alpha, IL-1 beta, IL-6 and TNF-alpha in a murine macrophage cell line RAW264.7. The treatment with the DEFB126 core peptide also led to correspondingly decreased secretion of IL-6 and TNF-alpha. The blockade of LPS-induced p42/44 and p38 MAPK signal pathway might contribute to the anti-inflammation effects of the DEFB126 core peptide. Furthermore, fluorescence-labeled DEFB126 could enter RAW 264.7 cells and reduce the production of LPS-stimulated inflammatory factors, implying that DEFB126 might also participate in intracellular regulation beyond its direct LPS neutralization. In summary, our results demonstrate that the DEFB 126 core peptide has critical functions in parallel to its C-terminal tail by showing LPS-binding activity, anti-inflammatory effects and intracellular regulatory function.
学科主题	Biotechnology & Applied Microbiology
类目[WOS]	Biotechnology & Applied Microbiology
关键词[WOS]	LIPOPOLYSACCHARIDE-BINDING-PROTEIN ; ANTIMICROBIAL PEPTIDES ; ADAPTIVE IMMUNITY ; GENE CLUSTERS ; COPY NUMBER ; IN-VITRO ; EXPRESSION ; DISEASE ; SURFACE ; INNATE
收录类别	SCI
语种	英语
WOS记录号	WOS:000317136700014
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/421]
专题	上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式 GB/T 7714	Liu, HY,Yu, HG,Gu, YH,et al. Human beta-defensin DEFB126 is capable of inhibiting LPS-mediated inflammation[J]. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,2013,97(8):3395-3408.
APA	Liu, HY.,Yu, HG.,Gu, YH.,Xin, AJ.,Zhang, YL.,...&Lin, DH.(2013).Human beta-defensin DEFB126 is capable of inhibiting LPS-mediated inflammation.APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,97(8),3395-3408.
MLA	Liu, HY,et al."Human beta-defensin DEFB126 is capable of inhibiting LPS-mediated inflammation".APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 97.8(2013):3395-3408.