Exocytotic stimulation promotes association of the ADP-ribosylation factor with PC12 cell membranes

Archives of Biochemistry and Biophysics
T MurayamaY Nomura

Abstract

ADP-ribosylation factors (ARFs) are a family of small molecular, monomeric GTP-binding (G) proteins, initially identified by their ability to enhance cholera toxin (CTX) ADP-ribosyltransferase activity. ARFs have been implicated in protein transport and vesicle and endosome fusion. Although several reports show that synthetic peptides of the N-terminus of ARF inhibited Ca(2+)-dependent exocytosis in permeabilized adrenal chromaffin cells, the role of ARFs in exocytosis has not been established. In this study, we investigated the translocation of ARFs to the membrane fraction from the cytosol fraction in PC12 cells after exocytotic stimulation by measuring the immunoreactivity of ARFs (with anti-ARF anti-serum and with anti-ARF3 antibodies) and enzymatic ARF activity, which enhances the CTX effect. Both the immunoreactivity and the enzymatic activity of ARF in the membrane fraction increased about twofold, significantly, after exocytotic stimulation with ATP and KCl. The translocation of ARF and noradrenaline release was observed in the presence of extracellular CaCl2, but not in the absence of CaCl2. The ARF translocated to the membrane fraction after stimulation in intact cells seemed to be an inactive, perhaps is the GDP form...Continue Reading

References

Oct 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·S C TsaiM Vaughan
Feb 24, 1995·Science·C D'Souza-SchoreyP D Stahl
Mar 10, 1995·Archives of Biochemistry and Biophysics·W BerónP D Stahl
Apr 12, 1994·Proceedings of the National Academy of Sciences of the United States of America·S C TsaiM Vaughan
Mar 22, 1996·The Journal of Biological Chemistry·E WeberK L Kirk
Dec 1, 1996·Journal of Cellular Physiology·T MurayamaY Nomura

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