Protein kinase C substrate phosphorylation in relation to neural growth and synaptic plasticity: a common molecular mechanism underlying multiple neural functions

Thesis/Dissertation · Thu Jan 01 00:00:00 EST 1987

OSTI ID:7190183

Nelson, R B

In these studies, we addressed the issues of: (1) whether neural protein kinase C (PKC) substrates might be altered in phosphorylation following induction of long-term potentiation (LTP); (2) whether PKC substrate phosphorylation might be specifically related to a model of neural plasticity other than LTP; and (3) whether the PKC substrates implicated in adult synaptic plasticity might be present in axonal growth cones given reports that high concentrations of PKC are found in these structures. Using quantitative analysis of multiple two-dimensional gels, we found that the two major substrates of exogenous purified PKC in adult hippocampal homogenate are both directly correlated to persistence of LTP. In rhesus monkey cerebral cortex, the proteins corresponding to protein F1 and 80k displayed topographical gradients in /sup 32/P-incorporation along the occipitotemporal visual processing pathway. The phosphorylation of both proteins was 11- and 14-fold higher, respectively, in temporal regions of this pathway implicated in the storage of visual representations, than in occipital regions, which do not appear to directly participate in visual memory functions.

• Research Organization: Northwestern Univ., Evanston, IL (USA)
• OSTI ID: 7190183
• Resource Relation: Other Information: Thesis (Ph. D.)
• Country of Publication: United States
• Language: English

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