C7 is expressed on endothelial cells as a trap for the assembling terminal complement complex and may exert anti-inflammatory function

被引：41

作者：

Bossi, Fleur ^{[1
]}

Rizzi, Lucia ^{[1
]}

Bulla, Roberta ^{[1
]}

Debeus, Alessandra ^{[1
]}

Tripodo, Claudio ^{[2
]}

Picotti, Paola ^{[3
,4
]}

Betto, Elena ^{[3
]}

Macor, Paolo ^{[1
]}

Pucillo, Carlo ^{[3
]}

Wuerzner, Reinhard ^{[5
]}

Tedesco, Francesco ^{[1
]}

机构：

[1] Univ Trieste, Dept Life Sci, I-34127 Trieste, Italy

[2] Univ Palermo, Dept Human Pathol, Palermo, Italy

[3] Univ Udine, Dept Biomed Sci & Technol, I-33100 Udine, Italy

[4] ETH, Inst Mol Syst Biol, Zurich, Switzerland

[5] Innsbruck Med Univ, Div Hyg & Med Microbiol, Innsbruck, Austria

来源：

BLOOD | 2009年 / 113卷 / 15期

关键词：

MEMBRANE ATTACK COMPLEX; POLYACRYLAMIDE-GELS; UNSENSITIZED CELLS; MASS-SPECTROMETRY; MEDIATED LYSIS; REACTIVE LYSIS; VIMENTIN; PROTEIN; SURFACE; IDENTIFICATION;

D O I：

10.1182/blood-2008-03-146472

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

We describe a novel localization of C7 as a membrane-bound molecule on endothelial cells (ECs). Data obtained by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Western blot analysis, Northern blot analysis, and mass spectrometry revealed that membrane-associated C7 (mC7) was indistinguishable from soluble C7 and was associated with vimentin on the cell surface. mC7 interacted with the other late complement components to form membrane-bound TCC (mTCC). Unlike the soluble SC5b-9, mTCC failed to stimulate ECs to express adhesion molecules, to secrete IL-8, and to induce albumin leakage through a monolayer of ECs, and more importantly protected ECs from the proinflammatory effect of SC5b-9. Our data disclose the possibility of a novel role of mC7 that acts as a trap for the late complement components to control excessive inflammation induced by SC5b-9. (Blood. 2009; 113: 3640-3648)

引用

页码：3640 / 3648

页数：9

共 40 条

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