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 Blood, 9 April 2009, Vol. 113, No. 15, pp. 3640-3648.
Prepublished online as a Blood First Edition Paper on January 29, 2009; DOI 10.1182/blood-2008-03-146472.

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VASCULAR BIOLOGY

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

Fleur Bossi1, Lucia Rizzi1, Roberta Bulla1, Alessandra Debeus1, Claudio Tripodo2, Paola Picotti3,4, Elena Betto3, Paolo Macor1, Carlo Pucillo3, Reinhard Würzner5, and Francesco Tedesco1

1 Department of Life Sciences, University of Trieste, Trieste, Italy; 2 Department of Human Pathology, University of Palermo, Palermo, Italy; 3 Department of Science and Biomedical Technology, University of Udine, Udine, Italy; 4 Institute of Molecular Systems Biology, Eidgenössische Technische Hochschule (ETH) Zürich, Zürich, Switzerland; and 5 Division of Hygiene and Medical Microbiology, Innsbruck Medical University, Innsbruck, Austria

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.


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