Abstract
Protein phosphorylation was investigated in primary rat astrocyte cultures treated with and without dibutyryl cyclic AMP. Astrocytes maintained in dibutyryl cyclic AMP for several weeks displayed increased phosphate incorporation in 5 protein bands (55, 52, 45, 43 and 28 kDa) while incorporation in one band (42 kDa) was decreased. Phosphate incorporation in several other protein bands was unchanged. Calcium-dependent phosphate incorporation was also altered by prior exposure of the cells to dibutyryl cyclic AMP: addition of calcium to broken cell preparations resulted in increased incorporation in 75, 53 and 52 kDa while decreased incorporation occurred in 100 kDa. These differences in protein phosphorylation may be related to the previously reported biochemical and morphological changes brought about by dibutyryl cyclic AMP and may provide insights into the mechanisms of reactive gliosis.
| Original language | English |
|---|---|
| Pages (from-to) | 164-168 |
| Number of pages | 5 |
| Journal | Brain Research |
| Volume | 410 |
| Issue number | 1 |
| DOIs | |
| State | Published - Apr 28 1987 |
| Externally published | Yes |
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Keywords
- Astrocyte
- Calcium
- Cyclic adenosine monophosphate
- Protein phosphorylation
ASJC Scopus subject areas
- Developmental Biology
- Molecular Biology
- Clinical Neurology
- Neuroscience(all)
Cite this
Protein phosphorylation in primary astrocyte cultures treated with and without dibutyryl cyclic AMP. / Neary, Joseph T.; Gutierrez, Maria del Pilar; Norenberg, Luz Oliva B; Norenberg, Michael D.
In: Brain Research, Vol. 410, No. 1, 28.04.1987, p. 164-168.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Protein phosphorylation in primary astrocyte cultures treated with and without dibutyryl cyclic AMP
AU - Neary, Joseph T.
AU - Gutierrez, Maria del Pilar
AU - Norenberg, Luz Oliva B
AU - Norenberg, Michael D
PY - 1987/4/28
Y1 - 1987/4/28
N2 - Protein phosphorylation was investigated in primary rat astrocyte cultures treated with and without dibutyryl cyclic AMP. Astrocytes maintained in dibutyryl cyclic AMP for several weeks displayed increased phosphate incorporation in 5 protein bands (55, 52, 45, 43 and 28 kDa) while incorporation in one band (42 kDa) was decreased. Phosphate incorporation in several other protein bands was unchanged. Calcium-dependent phosphate incorporation was also altered by prior exposure of the cells to dibutyryl cyclic AMP: addition of calcium to broken cell preparations resulted in increased incorporation in 75, 53 and 52 kDa while decreased incorporation occurred in 100 kDa. These differences in protein phosphorylation may be related to the previously reported biochemical and morphological changes brought about by dibutyryl cyclic AMP and may provide insights into the mechanisms of reactive gliosis.
AB - Protein phosphorylation was investigated in primary rat astrocyte cultures treated with and without dibutyryl cyclic AMP. Astrocytes maintained in dibutyryl cyclic AMP for several weeks displayed increased phosphate incorporation in 5 protein bands (55, 52, 45, 43 and 28 kDa) while incorporation in one band (42 kDa) was decreased. Phosphate incorporation in several other protein bands was unchanged. Calcium-dependent phosphate incorporation was also altered by prior exposure of the cells to dibutyryl cyclic AMP: addition of calcium to broken cell preparations resulted in increased incorporation in 75, 53 and 52 kDa while decreased incorporation occurred in 100 kDa. These differences in protein phosphorylation may be related to the previously reported biochemical and morphological changes brought about by dibutyryl cyclic AMP and may provide insights into the mechanisms of reactive gliosis.
KW - Astrocyte
KW - Calcium
KW - Cyclic adenosine monophosphate
KW - Protein phosphorylation
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U2 - 10.1016/S0006-8993(87)80040-9
DO - 10.1016/S0006-8993(87)80040-9
M3 - Article
C2 - 3034384
AN - SCOPUS:0023227241
VL - 410
SP - 164
EP - 168
JO - Brain Research
JF - Brain Research
SN - 0006-8993
IS - 1
ER -