Over-expression of integrin β3 can partially overcome the defect of integrin β3 signaling in transglutaminase 2 null macrophages

Beáta Tóth, Zsolt Sarang, György Vereb, Ailiang Zhang, Sakae Tanaka, Gerry Melino, László Fésüs, Zsuzsa Szondy

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)22-28
Number of pages7
JournalImmunology Letters
Volume126
Issue number1-2
DOIs
Publication statusPublished - Sep 22 2009

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Keywords

  • Apoptotic cells
  • Integrin signaling
  • Macrophages
  • Transglutaminase 2

ASJC Scopus subject areas

  • Immunology
  • Immunology and Allergy

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