ADP-ribosylation of brain neuronal proteins is altered by in vitro and in vivo exposure to inorganic mercury.
ADP-ribosylation is an essential process in the metabolism of brain neuronal proteins, including the regulation of assembly and disassembly of biological polymers. Here, we examine the effect of HgCl2 exposure on the ADP-ribosylation of tubulin and actin, both cytoskeletal proteins also found in neurons, and B-50/43-kDa growth-associated protein (B-50/GAP-43), a neuronal tissue-specific phosphoprotein. In rats we demonstrate, with both in vitro and in vivo experiments, that HgCl2 markedly inhibits the ADP-ribosylation of tubulin and actin. This is direct quantitative evidence that HgCl2, a toxic xenobiotic, alters specific neurochemical reactions involved in maintaining brain neuron structure.
Palkiewicz
P
P
Department of Medical Biochemistry, Faculty of Medicine, University of Calgary, Alberta, Canada.
Zwiers
H
H
Lorscheider
F L
FL
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D001345:Autoradiography; D015180:Electrophoresis, Gel, Two-Dimensional; D005625:Frontal Lobe / Q000187:drug effects / Q000378:metabolism*; D008297:Male; D008627:Mercuric Chloride / Q000494:pharmacology*; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*; D009474:Neurons / Q000187:drug effects / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D051381:Rats; D017207:Rats, Sprague-Dawley
D009419:Nerve Tissue Proteins; D010761:Phosphorus Radioisotopes; D000246:Adenosine Diphosphate Ribose; D008627:Mercuric Chloride