The α7β0 isoform of the complement regulator C4b-binding protein induces a semimature, anti-inflammatory state in dendritic cells.

@article{Olivar2013TheI,
  title={The α7β0 isoform of the complement regulator C4b-binding protein induces a semimature, anti-inflammatory state in dendritic cells.},
  author={Rut Olivar and Ana Luque and Mar Naranjo-G{\'o}mez and Josep Quer and Pablo Garc{\'i}a de Frutos and Francesc Enric Borr{\`a}s and Santiago Rodr{\'i}guez de C{\'o}rdoba and Anna M. Blom and Josep M Aran},
  journal={Journal of immunology},
  year={2013},
  volume={190 6},
  pages={2857-72}
}
The classical pathway complement regulator C4b-binding protein (C4BP) is composed of two polypeptides (α- and β-chains), which form three plasma oligomers with different subunit compositions (α7β1, α7β0, and α6β1). We show in this article that the C4BP α7β0 isoform (hereafter called C4BP[β(-)] [C4BP lacking the β-chain]), overexpressed under acute-phase conditions, induces a semimature, tolerogenic state on human monocyte-derived dendritic cells (DCs) activated by a proinflammatory stimulus… CONTINUE READING

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