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

Claudio Tripodo, Lucia Rizzi, Paola Picotti, Elena Betto, Francesco Tedesco, Reinhard Wurzner, Paolo Macor, Carlo Pucillo, Fleur Bossi, Roberta Bulla, Alessandra Debeus

Risultato della ricerca: Articlepeer review

29 Citazioni (Scopus)

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 indistinguish-able 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. © 2009 by The American Society of Hematology.
Lingua originaleEnglish
pagine (da-a)3640-3648
Numero di pagine9
RivistaBlood
Volume113
Stato di pubblicazionePublished - 2009

All Science Journal Classification (ASJC) codes

  • Immunology
  • Biochemistry
  • Hematology
  • Cell Biology

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