Regenerating neurons |
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Authors: | L Austin J G Watterson M T W Hearn |
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Institution: | (1) Department of Biochemistry, Monash University, 3168 Clayton, Victoria, Australia |
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Abstract: | We have been studying the phosphorylation of proteins of both normal and regenerating superior cervical ganglia of the rat.
Here we report the incorporation of radioactive phosphate into proteins of ganglia homogenates incubated with32P-labeled ATP under various conditions at day 3 after postganglionic axotomy. The proteins were analyzed by two-dimensional
electrophoresis followed by autoradiography. Incubation in the presence of Ca2+ or Ca2+ plus cyclic AMP produced only about 20 spots corresponding to distinctly labeled proteins. This number was reduced to about
five under EGTA plus cyclic AMP conditions, whereas the presence of EGTA alone suppressed the phosphorylation reaction almost
totally. All these proteins fell within the narrow pI range of 4–6, whereby no qualitative differences between regenerating and control cases were observed. However, the growth-associated
protein, variously designated GAP-43, B-50, F-1, and pp-46, had enhanced levels of phosphate incorporation in regenerating
ganglia compared to controls. Injury also caused consistently higher levels of phosphorylation of proteins running in the
position of α- and β-tubulin. Since these three proteins are major constitutents of regenerating axons, these results suggest
that the changes in their phosphorylation induced by injury may be involved in the regulation of their transport. |
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Keywords: | Superior cervical ganglion axotomy nerve regeneration protein phosphorylation axonal transport GAP-43 tubulins |
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