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Titolo:
LEAD-PROTEIN INTERACTIONS AS A BASIS FOR LEAD TOXICITY
Autore:
GOERING PL;
Indirizzi:
US FDA,CTR DEVICES & RADIOL HLTH OFF SCI & TECHNOL,DIV LIFE SCI,HFZ 112 ROCKVILLE MD 20857
Titolo Testata:
Neurotoxicology
fascicolo: 2-3, volume: 14, anno: 1993,
pagine: 45 - 60
SICI:
0161-813X(1993)14:2-3<45:LIAABF>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
DELTA-AMINOLEVULINIC-ACID; LOW-MOLECULAR WEIGHT; BOVINE CARBONIC-ANHYDRASE; TRANSCRIPTION FACTOR-IIIA; ZINC-BINDING DOMAINS; KINASE-C; RAT-LIVER; DEHYDRATASE INHIBITION; ACTIVE-SITE; METAL-IONS;
Keywords:
LEAD-PROTEIN INTERACTIONS; LEAD-BINDING PROTEINS; METALLOTHIONEIN; CARBONIC ANHYDRASE; PROTEIN KINASE-C; CALMODULIN; NUCLEIC ACID BINDING PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
79
Recensione:
Indirizzi per estratti:
Citazione:
P.L. Goering, "LEAD-PROTEIN INTERACTIONS AS A BASIS FOR LEAD TOXICITY", Neurotoxicology, 14(2-3), 1993, pp. 45-60

Abstract

The interaction of lead (Pb) with proteins may represent a fundamental mechanism by which Pb exerts toxicity. In this overview, various factors which influence the interaction of Pb with proteins will be discussed. Pb interacts with enzyme functional groups, and high-affinity metal-binding proteins, such as Pb-binding proteins and metallothioneins, can mediate this Pb-enzyme interaction. Many other factors influencePb-protein interactions including ligand competition and binding affinities; protein folding and the nature of the metal-binding site; rates of protein synthesis and degradation; and intracellular localizationof the ligand and metal. The remainder of this overview will focus onspecific examples of important proteins known to be influenced by Pb or which hypothetically may be influenced by Pb. Gaps in knowledge andimportant research needs are emphasized. Many of the factors discussed play a role in the relative sensitivity of various enzymes in heme biosynthesis to Pb. Disruption of this critical pathway by Pb may result in neuropathologies and accumulation of neurotoxic heme precursors. High-affinity metal-binding proteins have been shown to play a role inmediating Pb inhibition of the octameric Zn-containing enzyme, ALA dehydratase. Knowledge of regional localization in brain and the postnatal ontogeny of the high-affinity metal-binding proteins may be pivotalin understanding Pb neurotoxicity. Other specific examples related toor potentially related to Pb toxicity which are discussed include nucleic acid binding proteins, calmodulin, protein kinase C, and carbonicanhydrase. These proteins will serve as models to understand some basic principles and differences in Pb-protein interactions.. (C) 1993 Intox Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 13:06:26