Calmodulin and cAMP dependent synaptic vesicle protein phosphorylation in rat cortex following lead exposure.
The effect of in vivo and in vitro lead exposure on calmodulin and cAMP dependent synaptic vesicle protein phosphorylation has been investigated. Lead could enhance calmodulin activity following in vitro and in vivo lead exposure. The calmodulin dependent synaptic vesicle protein phosphorylation was enhanced following in vivo and in vitro lead exposure resulting in the depletion of the neurotransmitters norepinephrine and acetylcholine. The cAMP dependent synaptic vesicle protein phosphorylation was inhibited by both in vitro and in vivo lead treatment. The results suggest that lead adversely affects synaptic vesicle protein phosphorylation and this may ultimately effect synaptic functions.
Sandhir
R
R
Department of Biochemistry, Postgraduate Institute of Medical Education and Research, Chandigarh, India.
Gill
K D
KD
D000818:Animals; D002147:Calmodulin / Q000502:physiology*; D002540:Cerebral Cortex / Q000378:metabolism*; D000242:Cyclic AMP / Q000502:physiology*; D007855:Lead Poisoning / Q000378:metabolism*; D008297:Male; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D017208:Rats, Wistar; D013572:Synaptic Vesicles / Q000378:metabolism*
D002147:Calmodulin; D009419:Nerve Tissue Proteins; D000242:Cyclic AMP