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ADP‐Ribosylation of Brain Neuronal Proteins Is Altered by In Vitro and In Vivo Exposure to Inorganic Mercury
Author(s) -
Palkiewicz Pawel,
Zwiers Henk,
Lorscheider Fritz L.
Publication year - 1994
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1994.62052049.x
Subject(s) - tubulin , in vivo , cytoskeleton , in vitro , microbiology and biotechnology , biochemistry , chemistry , microtubule , biology , phosphoprotein , adp ribosylation , phosphorylation , enzyme , nad+ kinase , cell
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 HgCl 2 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 HgCl 2 markedly inhibits the ADP‐ribosylation of tubulin and actin. This is direct quantitative evidence that HgCl 2 , a toxic xenobiotic, alters specific neurochemical reactions involved in maintaining brain neuron structure.