Publication | Open Access
Rapid transport of phosphatidylcholine occurring simultaneously with protein transport in the frog sciatic nerve
102
Citations
30
References
1973
Year
Proteinlipid InteractionNeurotransmissionPeripheral NerveLipid MovementPeripheral NervesCellular PhysiologyMembrane TransportPeripheral TransportNeurochemistryFrog Sciatic NerveBiophysicsRapid TransportMolecular PhysiologyBiochemistrySciatic NerveProtein TransportNervous SystemSimultaneous TransportNeurophysiologyNatural SciencesPhysiologyCellular BiochemistryMedicine
1. Either l-[4,5-(3)H]leucine or [Me-(3)H]choline, or both l-[U-(14)C]leucine and [Me-(3)H]-choline, were injected into the ninth dorsal root ganglion of the frog, and peripheral transport of labelled proteins and/or phospholipids, mostly phosphatidylcholine, was studied by analysis of consecutive segments of the sciatic nerve. 2. At 25 degrees C, approx. 5% of the (3)H-labelled protein was transported at the rate of 152mm/day. The rate was temperature-dependent with the Q(10) value of 2.6. The flow was completely blocked by the local application of colchicine, but was unaffected by cytochalasin D. 3. [Me-(3)H]-Choline was incorporated into phosphatidylcholine at a comparatively slow rate, but was transported in the nerve at a rate equivalent to that for (3)H-labelled proteins. 4. The simultaneous transport of phosphatidylcholine and the protein was further supported in the double-labelling experiments by an identical transport rate of (3)H-labelled phosphatidylcholine and (14)C-labelled proteins, by their identical temperature dependence, by simultaneous blockade with colchicine, and also by the parallel distribution of the two labels in subcellular fractions. Specific radioactivities on a protein basis of both (3)H and (14)C labels were highest in microsomal subfractions enriched with Na(+)-plus-K(+)-stimulated adenosine triphosphatase and acetylcholinesterase. It is suggested that (3)H-labelled phosphatidylcholine and (14)C-labelled proteins transported in the nerve reside in the same structural entity, most probably a membrane component.
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