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Bovine prion (PrP) and Doppel (Dpl) proteins expression after in vitro leukocyte activation or Dpl/PrP blocking
Author(s) -
Paltrinieri Saverio,
Spagnolo Valentina,
Giordano Alessia,
Gelmetti Daniela,
Comazzi Stefano
Publication year - 2006
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.20682
Subject(s) - incubation , in vitro , biology , antibody , flow cytometry , microbiology and biotechnology , receptor , tumor necrosis factor alpha , cell , cell culture , immunology , biochemistry , genetics
It has been postulated that Doppel (Dpl) and Prion (PrP) proteins have yet undetermined interactions, since Dpl is overexpressed in transgenic PrP‐deficient mice. In this study we investigated the expression levels of Dpl and PrP on lymphocytes, monocytes and neutrophils (PMNs) isolated from bovine blood and incubated (2 and 18 h) with TNFα, IL‐1, IL‐2, IL‐8, C5a, IFNγ, anti‐PrP, and anti‐Dpl antibodies by flow cytometry. The isolation procedures yielded cell populations with high purity, viability and recovery rates. After 2 h incubation, expression of PrP or Dpl was altered only in PMNs. These cells overexpressed PrP when incubated with TNFα and IFNγ, and both PrP and Dpl when incubated with C5a; incubation with TNFα, IL‐8 and IFNγ led to down‐regulation of Dpl. Lymphocytes incubated for 18 h with IL‐2 and with IFNγ overexpressed Dpl. Incubation with the anti‐PrP antibody induced down‐regulation of Dpl in PMNs after 2 h and overexpression of Dpl in lymphocytes after 18 h. The differences recorded after 2 h were likely due to redistribution of pre‐existing PrP or Dpl molecules, while those seen at 18 h were most probably due to increased protein synthesis. The variations seen using the different activators depend on different receptors and/or signaling pathways. These results demonstrate that is possible to alter the expression of Dpl and PrP in blood cells in vitro by incubation with either cytokines or anti‐PrP antibodies. This opens an interesting opportunity to study the biology of these proteins using in vitro systems. J. Cell. Physiol. 208: 446–450, 2006. © 2006 Wiley‐Liss, Inc.