Source:http://linkedlifedata.com/resource/pubmed/id/12499112
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
2002-12-24
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pubmed:abstractText |
Compounds derived from Dimercaprol, such as meso-2,3-dimercaptosuccinic acid (DMSA) and 2,3-dimercaptopropane-1-sulfonic acid (DMPS), are becoming common agents for treating humans exposed to heavy metals. Heavy metals such as Pb(2+), Hg(2+) and Cd(2+) can inhibit delta-aminolevulinate dehydratase (delta-ALA-D) activity. Delta-ALA-D catalyzes the condensation of two delta-aminolevulinic acid (delta-ALA) molecules with the formation of porphobilinogen, a heme precursor. The effects of DMSA and DMPS alone or in combination with Cd(2+), Hg(2+), or Pb(2+) on hepatic delta-ALA-D were examined. DMPS and DMSA caused a dose-dependent inhibition of hepatic delta-ALA-D. In the presence of Hg(2+) or Cd(2+) the inhibitory potency of DMPS increased. Similarly, the inhibitory effects of Hg(2+) and Cd(2+) were markedly increased in the presence of DMSA. In contrast, the inhibitory effect of DMPS was not changed by inclusion of Pb(2+). As observed with DMSA, Zn(2+) did not modified the inhibitory effect of DMPS. Data of the present report support the idea that the complexes formed (metals-DMSA or DMPS) were more inhibitory than the metal (Hg(2+) and Cd(2+)) or the chelating agent alone to the hepatic delta-ALA-D activity, in vitro. The mechanism of hepatic delta-ALA-D inhibition by Hg(2+)-DMPS/DMSA and Cd(2+)-DMPS/DMSA complexes involve the essential thiol groups of the enzyme.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cadmium,
http://linkedlifedata.com/resource/pubmed/chemical/Chelating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Lead,
http://linkedlifedata.com/resource/pubmed/chemical/Mercury,
http://linkedlifedata.com/resource/pubmed/chemical/Porphobilinogen Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Succimer,
http://linkedlifedata.com/resource/pubmed/chemical/Unithiol,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0300-483X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
184
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
85-95
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12499112-Animals,
pubmed-meshheading:12499112-Cadmium,
pubmed-meshheading:12499112-Chelating Agents,
pubmed-meshheading:12499112-Drug Synergism,
pubmed-meshheading:12499112-Enzyme Inhibitors,
pubmed-meshheading:12499112-Lead,
pubmed-meshheading:12499112-Male,
pubmed-meshheading:12499112-Mercury,
pubmed-meshheading:12499112-Mice,
pubmed-meshheading:12499112-Polarography,
pubmed-meshheading:12499112-Porphobilinogen Synthase,
pubmed-meshheading:12499112-Succimer,
pubmed-meshheading:12499112-Unithiol,
pubmed-meshheading:12499112-Zinc
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pubmed:year |
2003
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pubmed:articleTitle |
2,3-Dimercaptopropane-1-sulfonic acid and meso-2,3-dimercaptosuccinic acid increase mercury- and cadmium-induced inhibition of delta-aminolevulinate dehydratase.
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pubmed:affiliation |
Departamento de Quimica, Centro de Ciencias Naturais e Exatas, Universidade Federal de Santa Maria, Santa Maria, RS, Brazil.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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