.png){kind=icon}
返回
Prohibitin binds to C3 and enhances complement activation
.png){kind=icon}
PRE
AI
DOI：10.1016/j.molimm.2006.09.025.png)
.png){kind=icon}
原文求助.png){kind=icon}
分享.png){kind=icon}
收藏
摘要
En 中文
Prohibitin (PHB 1) is a multifunction protein that is released in lipid droplets from adipocytes and possibly other cells and is detectable in the circulation. We used crosslinking, immunoprecipitation and proteomic analysis to investigate binding partners for circulating PHB 1. Crosslinking of PHB I to serum resulted in two complexes of similar to 150 and 100 kDa, which contained both PHB I and fragments of C3. The binding of PHB I to C3 was confirmed using a solid phase assay where the dissociation constant was similar to 90 fmol/l. PHB 1, but not the closely related PHB2, was able to enhance complement activation and induce lysis of sensitized sheep erythrocytes when added with normal serum but not with C3-deficient serum. The ability of PHB I to bind to, and activate C3 suggests that PHB I may have a previously unrecognized role in innate immunity. (c) 2006 Elsevier Ltd. All rights reserved.
Keyword:
innate immunity
complement
proteomic
prohibitin
期刊
IF:
3
论文数:
9.3K
被引数:
1.3W
机构
暂无机构信息
引用论文
Complement C3 is a risk factor for the development of diabetes -: A population-based cohort study.png)
DIABETES
OAAI
DIABETESIF7.5
OAAI分享收藏Identification of Novel Peptide Binding Proteins in the Endoplasmic Reticulum: ERp72, Calnexin, and grp170Biochemistry
BiochemistryIF0
PREAI
分享收藏
查看更多内容