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Title: Ganglioside inhibition of glutamate-mediated protein kinase C translocation in primary cultures of cerebellar neurons

Abstract

In primary cultures of cerebellar granule cells, protein kinase C (PKC) translocation and activation can be triggered by the stimulation of excitatory amino acid neurotransmitter receptors. Glutamate evokes a dose-related translocation of 4-..beta..-(/sup 3/H)phorbol 12,13-dibutyrate /(/sup 3/H)-P(BtO)/sub 2// binding sites from the cytosol to the neuronal membrane and stimulates the incorporation of /sup 32/P into a number of membrane proteins, particularly protein bands in the range of 80, 50, and 40 kDa. The glutamate-evoked PKC translocation is Mg/sup 2 +/ sensitive, is prevented by 2-amino-5-phosphonovalerate and phencyclidine, is not inhibited by nitrendipine (a voltage-dependent Ca/sup 2 +/-channel-blocker) but is abolished by the removal of Ca/sup 2 +/ from the incubation medium, suggesting that glutamate-mediated Ca/sup 2 +/ influx is operative in the redistribution of PKC. Exposure of granule cells to the gangliosides trisialosylgangliotetraglycosylceramide (GT1b) of monosialosylgangliotetraglycosylceramide (GM1) inhibits the translocation and activation of PKC evoked by glutamate. These glycosphingolipids fail to interfere with glutamate binding to its high-affinity recognition site of with the (/sup 3/H)P(BtO)/sub 2/ binding, nor do they affect the Ca/sup 2 +/ influx. These gangliosides may prevent PKC translocation by interfering with the PKC binding to the neuronal membrane phosphatidylserine.

Authors:
; ;
Publication Date:
Research Org.:
Georgetown Univ. Medical School, Washington, DC (USA)
OSTI Identifier:
6408832
Resource Type:
Journal Article
Journal Name:
Proc. Natl. Acad. Sci. U.S.A.; (United States)
Additional Journal Information:
Journal Volume: 84:23
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; GANGLIOSIDES; BIOCHEMISTRY; PHORBOL ESTERS; CROSS-LINKING; PHOSPHOTRANSFERASES; SUBCELLULAR DISTRIBUTION; RECEPTORS; CELL CULTURES; CELL MEMBRANES; CEREBRUM; CYTOPLASM; DOSE-RESPONSE RELATIONSHIPS; GLUTAMIC ACID; INHIBITION; NERVE CELLS; PHOSPHORUS 32; TRITIUM COMPOUNDS; AMINO ACIDS; ANIMAL CELLS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; BODY; BRAIN; CARBOHYDRATES; CARBOXYLIC ACIDS; CARCINOGENS; CELL CONSTITUENTS; CENTRAL NERVOUS SYSTEM; CHEMICAL REACTIONS; CHEMISTRY; DAYS LIVING RADIOISOTOPES; DISTRIBUTION; ENZYMES; ESTERS; GLYCOLIPIDS; ISOTOPES; LABELLED COMPOUNDS; LIGHT NUCLEI; LIPIDS; MEMBRANE PROTEINS; MEMBRANES; NERVOUS SYSTEM; NUCLEI; ODD-ODD NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANS; PHOSPHORUS ISOTOPES; PHOSPHORUS-GROUP TRANSFERASES; POLYMERIZATION; PROTEINS; RADIOISOTOPES; SACCHARIDES; SOMATIC CELLS; TRANSFERASES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Vaccarino, F, Guidotti, A, and Costa, E. Ganglioside inhibition of glutamate-mediated protein kinase C translocation in primary cultures of cerebellar neurons. United States: N. p., 1987. Web. doi:10.1073/pnas.84.23.8707.
Vaccarino, F, Guidotti, A, & Costa, E. Ganglioside inhibition of glutamate-mediated protein kinase C translocation in primary cultures of cerebellar neurons. United States. https://doi.org/10.1073/pnas.84.23.8707
Vaccarino, F, Guidotti, A, and Costa, E. 1987. "Ganglioside inhibition of glutamate-mediated protein kinase C translocation in primary cultures of cerebellar neurons". United States. https://doi.org/10.1073/pnas.84.23.8707.
@article{osti_6408832,
title = {Ganglioside inhibition of glutamate-mediated protein kinase C translocation in primary cultures of cerebellar neurons},
author = {Vaccarino, F and Guidotti, A and Costa, E},
abstractNote = {In primary cultures of cerebellar granule cells, protein kinase C (PKC) translocation and activation can be triggered by the stimulation of excitatory amino acid neurotransmitter receptors. Glutamate evokes a dose-related translocation of 4-..beta..-(/sup 3/H)phorbol 12,13-dibutyrate /(/sup 3/H)-P(BtO)/sub 2// binding sites from the cytosol to the neuronal membrane and stimulates the incorporation of /sup 32/P into a number of membrane proteins, particularly protein bands in the range of 80, 50, and 40 kDa. The glutamate-evoked PKC translocation is Mg/sup 2 +/ sensitive, is prevented by 2-amino-5-phosphonovalerate and phencyclidine, is not inhibited by nitrendipine (a voltage-dependent Ca/sup 2 +/-channel-blocker) but is abolished by the removal of Ca/sup 2 +/ from the incubation medium, suggesting that glutamate-mediated Ca/sup 2 +/ influx is operative in the redistribution of PKC. Exposure of granule cells to the gangliosides trisialosylgangliotetraglycosylceramide (GT1b) of monosialosylgangliotetraglycosylceramide (GM1) inhibits the translocation and activation of PKC evoked by glutamate. These glycosphingolipids fail to interfere with glutamate binding to its high-affinity recognition site of with the (/sup 3/H)P(BtO)/sub 2/ binding, nor do they affect the Ca/sup 2 +/ influx. These gangliosides may prevent PKC translocation by interfering with the PKC binding to the neuronal membrane phosphatidylserine.},
doi = {10.1073/pnas.84.23.8707},
url = {https://www.osti.gov/biblio/6408832}, journal = {Proc. Natl. Acad. Sci. U.S.A.; (United States)},
number = ,
volume = 84:23,
place = {United States},
year = {Tue Dec 01 00:00:00 EST 1987},
month = {Tue Dec 01 00:00:00 EST 1987}
}