PMID: 7512616May 1, 1994Paper

Action of brefeldin A on amphibian neurons: passage of newly synthesized proteins through the Golgi complex is not required for continued fast organelle transport in axons

Journal of Neurochemistry
R S SmithJ Bobinski

Abstract

The relation between the availability of newly synthesized protein and lipid and the axonal transport of optically detectable organelles was examined in peripheral nerve preparations of amphibia (Rana catesbeiana and Xenopus laevis) in which intracellular traffic from the endoplasmic reticulum to the Golgi complex was inhibited with brefeldin A (BFA). Accumulation of fast-transported radio-labeled protein or phospholipid proximal to a sciatic nerve ligature was monitored in vitro in preparations of dorsal root ganglia and sciatic nerve. Organelle transport was examined by computer-enhanced video microscopy of single myelinated axons. BFA reduced the amount of radiolabeled protein and lipid entering the fast-transport system of the axon without affecting either the synthesis or the transport rate of these molecules. The time course of the effect of BFA on axonal transport is consistent with an action at an early step in the intrasomal pathway, and with its action being related to the observed rapid (< 1 h) disassembly of the Golgi complex. At a concentration of BFA that reduced fast-transported protein by > 95%, no effect was observed on the flux or velocity of anterograde or retrograde organelle transport in axons for at least ...Continue Reading

References

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