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

Abstract:

: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.

journal_name

Blood

journal_title

Blood

authors

Bossi F,Rizzi L,Bulla R,Debeus A,Tripodo C,Picotti P,Betto E,Macor P,Pucillo C,Würzner R,Tedesco F

doi

10.1182/blood-2008-03-146472

subject

Has Abstract

pub_date

2009-04-09 00:00:00

pages

3640-8

issue

15

eissn

0006-4971

issn

1528-0020

pii

blood-2008-03-146472

journal_volume

113

pub_type

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