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Ethanol-induced growth inhibition in embryonic chick brain is associated with changes in cytoplasmic cyclic
1Department of Biochemistry, ECU School of Medicine, Greenville, NC 27834.
Insights
Ethanol exposure in utero may impair infant growth by disrupting the adenylate cyclase/protein kinase pathway. Studies show chronic ethanol reduces cyclic AMP binding and protein phosphorylation in developing brains.
Area of Science:
- Neuroscience
- Developmental Biology
- Pharmacology
Background:
- Ethanol exposure during pregnancy is linked to fetal growth retardation.
- The adenylate cyclase/protein kinase cascade is implicated in ethanol's developmental effects.
Purpose of the Study:
- To investigate the impact of chronic ethanol exposure on the adenylate cyclase/protein kinase pathway in a developing brain model.
- To determine if ethanol affects cyclic AMP (cAMP) binding and protein phosphorylation.
Main Methods:
- Utilized an embryonic chick model for chronic ethanol exposure.
- Assessed cyclic AMP binding to protein kinase regulatory subunit II (RII).
- Measured the phosphorylation levels of RII and other brain cytosolic proteins.
Main Results:
- Chronic ethanol treatment significantly decreased cAMP binding to RII.
- Ethanol reduced the phosphorylation of RII by endogenous protein kinase.
- Alterations in the phosphorylation of a 62-65 kD brain cytosolic protein were observed.
Conclusions:
- Ethanol exposure disrupts key components of the adenylate cyclase/protein kinase cascade.
- These disruptions may underlie the growth retardation associated with prenatal ethanol exposure.
Abstract:
Several lines of research have suggested that ethanol-induced changes in the adenylate cyclase/protein kinase cascade may contribute to the growth retardation observed in infants exposed to ethanol in utero. Based on studies with an embryonic chick model, the data presented here suggest that chronic ethanol treatment significantly lowered the binding of cyclic AMP by protein kinase regulatory subunit (RII) and reduced the level of phosphorylation of RII by the endogenous cytoplasmic protein kinase catalytic subunit. Furthermore, ethanol treatment altered the phosphorylation of at least one other brain cytosolic protein (molecular weight = 62-65 kD).