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J Biol Chem, Vol. 274, Issue 36, 25297-25300, September 3, 1999
From the Department of Cell Biology and Physiology, Washington
University School of Medicine, St. Louis, Missouri 63110
ADP-ribosylation factor 6 (ARF6) appears to play
an essential role in the endocytic/recycling pathway in several cell
types. To determine whether ARF6 is involved in insulin-regulated
exocytosis, 3T3-L1 adipocytes were infected with recombinant adenovirus
expressing wild-type ARF6 or an ARF6 dominant negative mutant (D125N)
that encodes a protein with nucleotide specificity modified from
guanine to xanthine. Overexpression of these ARF6 proteins affected
neither basal nor insulin-regulated glucose uptake in 3T3-L1
adipocytes, nor did it affect the subcellular distribution of Glut1 or
Glut4. In contrast, the secretion of adipsin, a serine protease
specifically expressed in adipocytes, was increased by the expression
of wild-type ARF6 and was inhibited by the expression of D125N. These
results indicate a requirement for ARF6 in basal and insulin-regulated adipsin secretion but not in glucose transport. Our results suggest the
existence of at least two distinct pathways that undergo
insulin-stimulated exocytosis in 3T3-L1 adipocytes, one for adipsin
release and one for glucose transporter translocation.
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