Visualization of differential neurofilament phosphorylation in the pre- and postsynaptic axoplasm of the squid giant synapse: an electron spectroscopic study.
When inelastically scattered electrons with an energy loss specific for interaction with phosphorus atoms were used for visualization of sections of squid axons, bead-like domains of elongated proteins, presumably neurofilaments, exhibited distinct phosphorus signals. A marked asymmetry of these phosphorus signals was detectable between the pre- and the postsynaptic cytoskeleton of the giant synapse. Signals were very numerous and intense in the presynaptic terminal, while rare and weak in the postsynaptic axoplasm. The giant axon revealed a delayed appearance of phosphorus signals in its course from the cell bodies in the giant fibre lobe to its exit from the stellate ganglion. Numerous and intense phosphorylation signals were evident only in the peripheral giant axon. Asymmetry in the distribution of phosphorus signals between pre- and postsynaptic axoplasm paralleled differences in Ca(2+)-buffering mechanisms, as shown in a previous study. In the presynaptic terminal patterns of phosphorus signals correlated with precipitates which had formed after intra-axonal injection of calcium. Our observations suggest a role of phosphorylated neurofilaments in binding of calcium in the squid synapse.
Martin
R
R
Sekt. Elektronenmikroskopie, Universität Ulm, F.R.G.
Schilling
K
K
Fritz
W
W
Giuditta
A
A
D000818:Animals; D001369:Axons / Q000378:metabolism* / Q000648:ultrastructure; D049832:Decapodiformes; D007382:Intermediate Filaments / Q000378:metabolism* / Q000648:ultrastructure; D008854:Microscopy, Electron; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D012270:Ribosomes / Q000378:metabolism / Q000648:ultrastructure; D013233:Stellate Ganglion / Q000166:cytology / Q000502:physiology; D013569:Synapses / Q000378:metabolism* / Q000648:ultrastructure
D010750:Phosphoproteins