Journal
BLOOD
Volume 113, Issue 15, Pages 3640-3648Publisher
AMER SOC HEMATOLOGY
DOI: 10.1182/blood-2008-03-146472
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Funding
- European Network of Excellence (NoE) EMBIC [LSHN-CT-2004-512040]
- Associazione Italiana per la Ricerca sul Cancro (AIRC)
- Ministero dell'Istruzione, Universita e Ricerca (MIUR)
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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)
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