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Published online before print November 11, 2004

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(Journal of Leukocyte Biology. 2005;77:238-246.)
© 2005 by Society for Leukocyte Biology

The cellular prion protein modulates phagocytosis and inflammatory response

Cecília J. G. de Almeida^*,1, Luciana B. Chiarini^*, Juliane Pereira da Silva, Patrícia M. R. e Silva, Marco Aurélio Martins and Rafael Linden^*,2

^* Instituto de Biofísica da UFRJ, and
Instituto Oswaldo Cruz, Rio de Janeiro, RJ, Brasil

² Correspondence: Instituto de Biofísica da UFRJ, CCS, Bloco G, Cidade Universitária, 21949-900, Rio de Janeiro, RJ, Brasil. E-mail: rlinden{at}biof.ufrj.br

The cellular prion protein (PrP^c) is a glycoprotein anchored by glycosylphosphatidylinositol (GPI) to the cell surface and is abundantly expressed in the central nervous system. It is also expressed in a variety of cell types of the immune system. We investigated the role of PrP^c in the phagocytosis of apoptotic cells and other particles. Macrophages from mice with deletion of the Prnp gene showed higher rates of phagocytosis than wild-type macrophages in in vitro assays. The elimination of GPI-anchored proteins from the cell surface of macrophages from wild-type mice rendered these cells as efficient as macrophages derived from knockout mice. In situ detection of phagocytosis of apoptotic bodies within the retina indicated augmented phagocytotic activity in knockout mice. In an in vivo assay of acute peritonitis, knockout mice showed more efficient phagocytosis of zymosan particles than wild-type mice. In addition, leukocyte recruitment was altered in knockout mice, as compared with wild type. The data show that PrP^c modulates phagocytosis in vitro and in vivo. This activity is described for the first time and may be important for normal macrophage functions as well as for the pathogenesis of prion diseases.

Key Words: macrophage • apoptosis • zymosan • PrP^c

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