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Title: Stimulation of a Ca sup 2+ -dependent protein kinase by G sub M1 ganglioside in nerve growth factor-treated PC12 cells

Abstract

The authors have investigated the ability of exogenous gangliosides to modulate nerve growth factor (NGF) signal transduction in PC12 cells. The effects of exogenous ganglioside G{sub M1} on multiple protein kinase activities were assayed by analyzing site-specific serine phosphorylation of tyrosine hydroxylase (TyrOHase) by two-dimensional phosphopeptide mapping. In the presence of NGF, exogenous G{sub M1} increased {sup 32}P incorporation into TyrOHase phosphopeptide T2, a Ca{sup 2+}/calmodulin-dependent protein kinase substrate whose phosphorylation is not normally affected by NGF treatment. In the absence of NGF, G{sub M1} treatment had no significant effects on TyrOHase phosphorylation. The removal of extracellular Ca{sup 2+} or blockade of dihydropyridine-sensitive Ca{sup 2+} channels prevented the G{sub M1}-induced increases in {sup 32}P incorporation into phosphopeptide T2. Exogenous G{sub M1} also potentiated K{sup +} depolarization-induced increases in the phosphorylation of TyrOHase. These results suggest that the stimulatory effects of exogenous G{sub M1} ganglioside on NGF actions may be due to its ability to potentiate a Ca{sup 2+}-dependent signaling pathway.

Authors:
;  [1]
  1. State Univ. of New York, Stony Brook (United States)
Publication Date:
OSTI Identifier:
5933583
Resource Type:
Journal Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America; (United States)
Additional Journal Information:
Journal Volume: 88:13; Journal ID: ISSN 0027-8424
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; GANGLIOSIDES; BIOLOGICAL EFFECTS; PHOSPHOTRANSFERASES; BIOLOGICAL PATHWAYS; TOXINS; RADIORECEPTOR ASSAY; CALCIUM COMPOUNDS; GROWTH FACTORS; HYDROXYLASES; IODINE 125; PHOSPHORUS 32; TWO-DIMENSIONAL ELECTROPHORESIS; ALKALINE EARTH METAL COMPOUNDS; ANTIGENS; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; CARBOHYDRATES; DAYS LIVING RADIOISOTOPES; ELECTRON CAPTURE RADIOISOTOPES; ELECTROPHORESIS; ENZYMES; GLYCOLIPIDS; INTERMEDIATE MASS NUCLEI; INTERNAL CONVERSION RADIOISOTOPES; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; LIGHT NUCLEI; LIPIDS; MATERIALS; MITOGENS; NUCLEI; ODD-EVEN NUCLEI; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; OXIDOREDUCTASES; PHOSPHORUS ISOTOPES; PHOSPHORUS-GROUP TRANSFERASES; PROTEINS; RADIOISOTOPES; SACCHARIDES; TOXIC MATERIALS; TRACER TECHNIQUES; TRANSFERASES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Hilbush, B S, and Levine, J M. Stimulation of a Ca sup 2+ -dependent protein kinase by G sub M1 ganglioside in nerve growth factor-treated PC12 cells. United States: N. p., 1991. Web. doi:10.1073/pnas.88.13.5616.
Hilbush, B S, & Levine, J M. Stimulation of a Ca sup 2+ -dependent protein kinase by G sub M1 ganglioside in nerve growth factor-treated PC12 cells. United States. https://doi.org/10.1073/pnas.88.13.5616
Hilbush, B S, and Levine, J M. 1991. "Stimulation of a Ca sup 2+ -dependent protein kinase by G sub M1 ganglioside in nerve growth factor-treated PC12 cells". United States. https://doi.org/10.1073/pnas.88.13.5616.
@article{osti_5933583,
title = {Stimulation of a Ca sup 2+ -dependent protein kinase by G sub M1 ganglioside in nerve growth factor-treated PC12 cells},
author = {Hilbush, B S and Levine, J M},
abstractNote = {The authors have investigated the ability of exogenous gangliosides to modulate nerve growth factor (NGF) signal transduction in PC12 cells. The effects of exogenous ganglioside G{sub M1} on multiple protein kinase activities were assayed by analyzing site-specific serine phosphorylation of tyrosine hydroxylase (TyrOHase) by two-dimensional phosphopeptide mapping. In the presence of NGF, exogenous G{sub M1} increased {sup 32}P incorporation into TyrOHase phosphopeptide T2, a Ca{sup 2+}/calmodulin-dependent protein kinase substrate whose phosphorylation is not normally affected by NGF treatment. In the absence of NGF, G{sub M1} treatment had no significant effects on TyrOHase phosphorylation. The removal of extracellular Ca{sup 2+} or blockade of dihydropyridine-sensitive Ca{sup 2+} channels prevented the G{sub M1}-induced increases in {sup 32}P incorporation into phosphopeptide T2. Exogenous G{sub M1} also potentiated K{sup +} depolarization-induced increases in the phosphorylation of TyrOHase. These results suggest that the stimulatory effects of exogenous G{sub M1} ganglioside on NGF actions may be due to its ability to potentiate a Ca{sup 2+}-dependent signaling pathway.},
doi = {10.1073/pnas.88.13.5616},
url = {https://www.osti.gov/biblio/5933583}, journal = {Proceedings of the National Academy of Sciences of the United States of America; (United States)},
issn = {0027-8424},
number = ,
volume = 88:13,
place = {United States},
year = {Mon Jul 01 00:00:00 EDT 1991},
month = {Mon Jul 01 00:00:00 EDT 1991}
}