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ARF1(2-17) Does Not Specifically Interact With ARF1-dependent Pathways. Inhibition by Peptide of Phospholipases C Beta, D and Exocytosis in HL60 Cells

ARF1(2-17) Does Not Specifically Interact With ARF1-dependent Pathways. Inhibition by Peptide of Phospholipases C Beta, D and Exocytosis in HL60 Cells

A Fensome, E Cunningham, O Troung, S Cockcroft

FEBS Lett. 1994 Jul 25;349(1):34-8.

PMID: 8045298

Abstract:

The small GTP-binding protein ARF has been shown recently to regulate phospholipase D (PLD). In order to investigate the role of ARF proteins in regulated exocytosis, we have used the N-terminal peptide ARF1(2-17) of the ARF1 protein. ARF1 reconstituted PLD activity in cytosol-depleted HL60 cells was inhibited by ARF1(2-17). In the presence of endogenous cytosol, ARF1(2-17) also inhibited GTP-gamma-S-stimulated PLD activity and exocytosis. Mastoparan Politses jadwagae and mastoparan Vespula lewisii which exhibit similar structural properties to ARF1(2-17) also inhibited GTP-gamma-S-stimulated PLD and exocytosis. GTP-gamma-S-stimulated phospholipase C-beta (PLC-beta) was also inhibited by ARF(2-17) and mastoparan. In cytosol-depleted HL60 cells, the ARF(2-17) inhibited the reconstitution of GTP-gamma-S-stimulated PLC-beta activity with exogenously-added PLC-beta 1 and phosphatidylinositol transfer protein. We conclude that the widely-used ARF1(2-17) peptide inhibits both ARF-independent (i.e. PLC-beta) and ARF-dependent pathways (i.e. PLD) and therefore cannot be regarded as a specific inhibitor of ARF function.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP72093211	Mastoparan, Vespula lewisii		72093-21-1	Price

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