Abstract
Abstract: The effects of gangliosides on phosphorylation were studied in rat brain membrane. Gangliosides stimulated phosphorylation only in the presence of Ca2+ with major phosphoproteins of 45,000, 50,000, 60,000, and 80,000 daltons and high‐molecular‐weight species. In addition, gangliosides inhibited the phosphorylation of three proteins with molecular weights of 15,000, 20,000, and 78,000 daltons. The two low‐molecular‐weight proteins comigrated with rat myelin basic proteins. Ganglioside stimulation was dependent on the formation of a Ca2+ ganglioside complex since the calcium salt of gangliosides stimulated phosphorylation maximally. Disialo and trisialo gangliosides were more potent stimulators of kinase activity than the monosialo GM1. GD1a was the most potent activator tested. Asialo‐GM1, cerebroside, sialic acid, neuraminyllactose, sulfatide, and the acidic phospholipids phosphatidylserine and phosphatidylinositol did not stimulate kinase activity. The Ca2+ ‐dependent, ganglioside‐stimulated phosphorylation was qualitatively similar to the pattern for calmodulin‐dependent phosphorylation. However, while calmodulin‐dependent kinase activity was inhibited with an IC50 of 10 μM trifluoperazine, ganglioside‐stimulated kinase was inhibited with an IC50 of 200 μM trifluoperazine. These results indicate that gangliosides have complex effects on membrane‐associated kinase activities and suggest that Ca2+ ‐ganglioside complexes are potent stimulators of membrane kinase activity.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1229-1234 |
| Number of pages | 6 |
| Journal | Journal of Neurochemistry |
| Volume | 44 |
| Issue number | 4 |
| DOIs | |
| State | Published - Apr 1985 |
| Externally published | Yes |
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Keywords
- Calcium
- Ganglioside‐stimulated phosphorylation
- Kinase activity
ASJC Scopus subject areas
- Biochemistry
- Cellular and Molecular Neuroscience
Cite this
Calcium/Ganglioside‐Dependent Protein Kinase Activity in Rat Brain Membrane. / Goldenring, James R.; Otis, Laura C.; Yu, Robert K.; DeLorenzo, Robert J.
In: Journal of Neurochemistry, Vol. 44, No. 4, 04.1985, p. 1229-1234.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Calcium/Ganglioside‐Dependent Protein Kinase Activity in Rat Brain Membrane
AU - Goldenring, James R.
AU - Otis, Laura C.
AU - Yu, Robert K.
AU - DeLorenzo, Robert J.
PY - 1985/4
Y1 - 1985/4
N2 - Abstract: The effects of gangliosides on phosphorylation were studied in rat brain membrane. Gangliosides stimulated phosphorylation only in the presence of Ca2+ with major phosphoproteins of 45,000, 50,000, 60,000, and 80,000 daltons and high‐molecular‐weight species. In addition, gangliosides inhibited the phosphorylation of three proteins with molecular weights of 15,000, 20,000, and 78,000 daltons. The two low‐molecular‐weight proteins comigrated with rat myelin basic proteins. Ganglioside stimulation was dependent on the formation of a Ca2+ ganglioside complex since the calcium salt of gangliosides stimulated phosphorylation maximally. Disialo and trisialo gangliosides were more potent stimulators of kinase activity than the monosialo GM1. GD1a was the most potent activator tested. Asialo‐GM1, cerebroside, sialic acid, neuraminyllactose, sulfatide, and the acidic phospholipids phosphatidylserine and phosphatidylinositol did not stimulate kinase activity. The Ca2+ ‐dependent, ganglioside‐stimulated phosphorylation was qualitatively similar to the pattern for calmodulin‐dependent phosphorylation. However, while calmodulin‐dependent kinase activity was inhibited with an IC50 of 10 μM trifluoperazine, ganglioside‐stimulated kinase was inhibited with an IC50 of 200 μM trifluoperazine. These results indicate that gangliosides have complex effects on membrane‐associated kinase activities and suggest that Ca2+ ‐ganglioside complexes are potent stimulators of membrane kinase activity.
AB - Abstract: The effects of gangliosides on phosphorylation were studied in rat brain membrane. Gangliosides stimulated phosphorylation only in the presence of Ca2+ with major phosphoproteins of 45,000, 50,000, 60,000, and 80,000 daltons and high‐molecular‐weight species. In addition, gangliosides inhibited the phosphorylation of three proteins with molecular weights of 15,000, 20,000, and 78,000 daltons. The two low‐molecular‐weight proteins comigrated with rat myelin basic proteins. Ganglioside stimulation was dependent on the formation of a Ca2+ ganglioside complex since the calcium salt of gangliosides stimulated phosphorylation maximally. Disialo and trisialo gangliosides were more potent stimulators of kinase activity than the monosialo GM1. GD1a was the most potent activator tested. Asialo‐GM1, cerebroside, sialic acid, neuraminyllactose, sulfatide, and the acidic phospholipids phosphatidylserine and phosphatidylinositol did not stimulate kinase activity. The Ca2+ ‐dependent, ganglioside‐stimulated phosphorylation was qualitatively similar to the pattern for calmodulin‐dependent phosphorylation. However, while calmodulin‐dependent kinase activity was inhibited with an IC50 of 10 μM trifluoperazine, ganglioside‐stimulated kinase was inhibited with an IC50 of 200 μM trifluoperazine. These results indicate that gangliosides have complex effects on membrane‐associated kinase activities and suggest that Ca2+ ‐ganglioside complexes are potent stimulators of membrane kinase activity.
KW - Calcium
KW - Ganglioside‐stimulated phosphorylation
KW - Kinase activity
UR - http://www.scopus.com/inward/record.url?scp=0021919509&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021919509&partnerID=8YFLogxK
U2 - 10.1111/j.1471-4159.1985.tb08748.x
DO - 10.1111/j.1471-4159.1985.tb08748.x
M3 - Article
C2 - 2579206
AN - SCOPUS:0021919509
VL - 44
SP - 1229
EP - 1234
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
SN - 0022-3042
IS - 4
ER -