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B-50 Phosphorylation, Protein Kinase C and the Induction of Excessive Grooming Behavior in the Rat

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Molecular Mechanisms of Neuronal Responsiveness

Abstract

Behaviorally active neuropeptides might affect synaptic plasticity by changing the degree of phosphorylation of synaptic proteins. Neuronal electrical activity and neurotransmission are accompanied by covalent modification of synaptic proteins through cyclic phosphorylation and dephosphorylation (c.f. Weller, 1979). Studies using behavioral paradigms similar to those used to measure the behavioral effects of melanocortins (ACTH/MSH) suggested that the acquisition of new information may be accompanied by changes in the degree of phosphorylation of synaptic phosphoproteins (Glassman et al., 1973). The original idea was to study the in vitro modulation of synaptic plasma membrane phosphorylation by ACTH1-24 and its behaviorally active fragments and to compare the structural requirements of ACTH in this assay with those influencing the extinction of active avoidance behavior (Greven and De Wied, 1973). In our first study along this line, we noted that high concentrations of ACTH1-24 indeed inhibited the endogenous phosphorylation of several phosphoproteins in rat brain synaptic membranes (Zwiers et al., 1976). These phosphoproteins were phosphorylated by a cyclic AMP-independent mechanism, at that time the most important phosphorylation system studied (Zwiers et al., 1976). Our next step was to investigate the nature of the affected substrate proteins and their corresponding kinase(s).

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Schrama, L.H., De Graan, P.N.E., Oestreicher, A.B., Gispen, W.H. (1987). B-50 Phosphorylation, Protein Kinase C and the Induction of Excessive Grooming Behavior in the Rat. In: Ehrlich, Y.H., Lenox, R.H., Kornecki, E., Berry, W.O. (eds) Molecular Mechanisms of Neuronal Responsiveness. Advances in Experimental Medicine and Biology, vol 221. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7618-7_29

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