Exposure of Humans to Lead

Hammond, P. Brett

doi:10.1146/annurev.pa.17.040177.001213

Cited by 68 publications

(22 citation statements)

References 85 publications

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“…Histologic changes include eosinophilic intranuclear indusions in proximal tubular cells consisting of lead-protein complexes, and mitochondrial swelling (29)(30)(31)(32)(33). Renal manifestations of acute lead poisoning have been well described both in animal models and in humans; these include glycosuria, aminoaciduria (34,35), and phosphaturia, collectively representing the Fanconi syndrome (36)(37)(38). These functional changes are thought to be related to an effect of lead on mitochondrial respiration and phosphorylation (26).…”

Section: Lead Nephropathymentioning

confidence: 99%

Renal Effects of Environmental and Occupational Lead Exposure

Loghman‐Adham¹

1997

Environmental Health Perspectives

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Section: Lead Nephropathymentioning

confidence: 99%

Renal Effects of Environmental and Occupational Lead Exposure

Loghman‐Adham¹

1997

Environmental Health Perspectives

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“…For Mn, CDTA = DTPA > EDTA > Pen = DFO = no effect [6,7]. For Pb, DTPA > EDTA > CDTA > Pen % BAL > DFO = no effect [8,9]. For Zn, DTPA, CDTA > EDTA > Pen > DFO = no effect [ 10,111.…”

Section: Resultsmentioning

confidence: 99%

Computer simulation of chelation therapy Plasma mobilizing index as a replacement for effective stability constant

1977

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“…Pb2 , Ag+ and Hg2+ strongly inhibited rabbit liver guanine aminohydrolase, a sulfhydryl enzyme, whereas Cd2 , Mn2+, Ca2+ Be2 + Zn2 + Ba2+ Cu2+, Sn2 , Mg2+, Fe2 , and Ni2+ exhibited no inhibition of guanase activity (211). Pb2 + disturbed heme synthesis by inhibiting the cytoplasmic Zndependent, sulfhydryl-rich enzyme, aminolevulinic acid dehydratase, and the mitochondrial sulfihydryl enzyme, ferrochelatase (212). Cu2+, Hg2+, and Ag+ also inhibited aminolevulinic acid dehydratase (212).…”

Section: Divalent Ionsmentioning

confidence: 99%

The role of metals in carcinogenesis: biochemistry and metabolism.

Jennette¹

1981

Environ Health Perspect

154

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The oxyanions of vanadium, chromium, molybdenum, arsenic, and selenium are stable forms of these elements in high oxidation states which cross cell membranes using the normal phosphate and/or sulfate transport systems of the cell. Once inside the cell, these oxyanions may sulfuryl transfer reactions. Often the oxyanions serve as alternate enzyme substrates but form ester products which are hydrolytically unstable compared with the sulfate and phosphate esters and, therefore, decompose readily in aqueous solution. Arsenite and selenite are capable of reacting with sulfhydryl groups in proteins. Some cells are able to metabolize redox active oxyanions to forms of the elements in other stable oxidation states. Specific enzymes may be involved in the metabolic processes. The metabolites of these elements may form complexes with small molecules, proteins and nucleic acids which inhibit their ability to function properly. The divalent ions of beryllium, manganese, cobalt, nickel, cadmium, mercury, and lead are stable forms of these elements which may mimic essential divalent ions such as magnesium, calcium, iron, copper, or zinc. These ions may complex small molecules, enzymes, and nucleic acids in such a way that the normal activity of these species is altered. Free radicals may be produced in the presence of these metal ions which damage critical cellular molecules.

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Exposure of Humans to Lead

Cited by 68 publications

References 85 publications

Renal Effects of Environmental and Occupational Lead Exposure

Renal Effects of Environmental and Occupational Lead Exposure

Computer simulation of chelation therapy Plasma mobilizing index as a replacement for effective stability constant

The role of metals in carcinogenesis: biochemistry and metabolism.

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