ARF-GEP100, a guanine nucleotide-exchange protein for ADP-ribosylation factor 6, involved in the apoptotic cell death of phagocytes
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ADP-ribosylation factors(ARFs) are 20-kDa GTP-binding proteins involved in the vesicular trafficking, the activation of phospholipase D and phosphatidylinositol 4-phosphate 5-kinase, and the modulation of phagocyte functions. Like other GTP-binding proteins, ARFs cycle between GTP-bound, active and GDP-bound, inactive status. Guanine nucleotide-exchange proteins(GEPs), which catalyze the change of bound GDP for GTP, are necessary for the activation of ARFs. Previously, we found a novel GEP with 100kDa, named ARF-GEP<SUB>100</SUB>. In this study, we elucidated the role in ARF-GEP<SUB>100</SUB> on phagocyte functions by transfection of ARF-GEP<SUB>100</SUB>.<BR>Overexpression of ARF-GEP<SUB>100</SUB> induced apoptosis of mouse macrophage RAW264.7 cells and phorbol 12- myristate 13-acetate treated human monocyte U937 cells, which could be detected by morphological changes (nuclear condensation and formation of apoptotic bodies), annexin V-staining and TUNEL assay. ARF-GEP<SUB>100</SUB>- induced apoptosis was not inhibited by a caspase inhibitor zVAD-FMK. Furthermore, mutant analysis of ARFGEP<SUB>100</SUB> revealed that two regions (N- and C- termini) of ARF-GEP<SUB>100</SUB> were essential for the induction of apoptosis, but the mutant defective in GDP-GTP exchange domain induced apoptosis. These results suggest that ARFGEP<SUB>100</SUB> induces apoptosis of monocytic phagocytes independent of both the caspase activation and GDP-GTP exchange activity.
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