Abstract
Transglutaminase 2 (TG2) is a protein crosslinking enzyme with many additional biological functions. We have previously shown that in TG2-/- mice the in vivo clearance of apoptotic cells is defective leading to autoimmunity. TG2 contributes to the formation of phagocytic portals by binding to both integrin β3, a known phagocytic receptor, and its bridging molecule, MFG-E8. In TG2 null macrophages integrin β3 cannot accumulate around the apoptotic cells and its signaling is impaired. In the present study we describe a subline of TG2 null mice, in which a compensatory increase in integrin β3 expression, which resulted alone in a high receptor concentration around the apoptotic cells without the requirement for accumulation, partially corrected the defect in integrin β3 signaling. Our data provide a proof for the concept that the function of TG2 is to stabilize accumulated integrin β3 concentration in the phagocytic cup.
Original language | English |
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Pages (from-to) | 22-28 |
Number of pages | 7 |
Journal | Immunology Letters |
Volume | 126 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - Sep 22 2009 |
Keywords
- Apoptotic cells
- Integrin signaling
- Macrophages
- Transglutaminase 2
ASJC Scopus subject areas
- Immunology
- Immunology and Allergy