Abstract
Gangliosides inhibit the phosphorylation of both small and large rat myelin basic proteins (SMBP, LMBP) by an endogenous phospholipid‐sensitive Ca2+‐dependent protein kinase (C‐Kinase). Using a rat brain myelin preparation in an in vitro phosphorylation assay system, we determined the inhibition constants (IC50's) of the gangliosides GM1, GD1a, GD1b, and GT1b to be approximately 160 μM, 65 μM, 65 μM, and 40 μM, respectively. Asialoganglioside GA1, ceramide, and Nacetylneuraminic acid (NANA, sialic acid) failed to produce similar inhibition, suggesting that both the lipid and the sialic acid moieties are necessary, but neither alone is sufficient to produce inhibition. The results indicate that gangliosides may regulate protein kinase C activities in the nervous system.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 159-166 |
| Number of pages | 8 |
| Journal | Journal of Neuroscience Research |
| Volume | 15 |
| Issue number | 2 |
| DOIs | |
| State | Published - 1986 |
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Keywords
- ganglioside
- myelin basic protein
- phospholipid‐sensitive Ca‐dependent protein kinase
- protein C‐kinase
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience
Cite this
Gangliosides inhibit phospholipid‐sensitive Ca2+‐dependent kinase phosphorylation of rat myelin basic proteins. / Kim, J. Y.H.; Goldenring, J. R.; DeLorenzo, R. J.; Yu, R. K.
In: Journal of Neuroscience Research, Vol. 15, No. 2, 1986, p. 159-166.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Gangliosides inhibit phospholipid‐sensitive Ca2+‐dependent kinase phosphorylation of rat myelin basic proteins
AU - Kim, J. Y.H.
AU - Goldenring, J. R.
AU - DeLorenzo, R. J.
AU - Yu, R. K.
PY - 1986
Y1 - 1986
N2 - Gangliosides inhibit the phosphorylation of both small and large rat myelin basic proteins (SMBP, LMBP) by an endogenous phospholipid‐sensitive Ca2+‐dependent protein kinase (C‐Kinase). Using a rat brain myelin preparation in an in vitro phosphorylation assay system, we determined the inhibition constants (IC50's) of the gangliosides GM1, GD1a, GD1b, and GT1b to be approximately 160 μM, 65 μM, 65 μM, and 40 μM, respectively. Asialoganglioside GA1, ceramide, and Nacetylneuraminic acid (NANA, sialic acid) failed to produce similar inhibition, suggesting that both the lipid and the sialic acid moieties are necessary, but neither alone is sufficient to produce inhibition. The results indicate that gangliosides may regulate protein kinase C activities in the nervous system.
AB - Gangliosides inhibit the phosphorylation of both small and large rat myelin basic proteins (SMBP, LMBP) by an endogenous phospholipid‐sensitive Ca2+‐dependent protein kinase (C‐Kinase). Using a rat brain myelin preparation in an in vitro phosphorylation assay system, we determined the inhibition constants (IC50's) of the gangliosides GM1, GD1a, GD1b, and GT1b to be approximately 160 μM, 65 μM, 65 μM, and 40 μM, respectively. Asialoganglioside GA1, ceramide, and Nacetylneuraminic acid (NANA, sialic acid) failed to produce similar inhibition, suggesting that both the lipid and the sialic acid moieties are necessary, but neither alone is sufficient to produce inhibition. The results indicate that gangliosides may regulate protein kinase C activities in the nervous system.
KW - ganglioside
KW - myelin basic protein
KW - phospholipid‐sensitive Ca‐dependent protein kinase
KW - protein C‐kinase
UR - http://www.scopus.com/inward/record.url?scp=0022626028&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022626028&partnerID=8YFLogxK
U2 - 10.1002/jnr.490150205
DO - 10.1002/jnr.490150205
M3 - Article
C2 - 2421006
AN - SCOPUS:0022626028
VL - 15
SP - 159
EP - 166
JO - Journal of Neuroscience Research
JF - Journal of Neuroscience Research
SN - 0360-4012
IS - 2
ER -