کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
3355950 | 1591580 | 2009 | 7 صفحه PDF | دانلود رایگان |
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.
Journal: Immunology Letters - Volume 126, Issues 1–2, 22 September 2009, Pages 22–28