Matrix metalloproteinases (MMPs) are enzymes involved in the degradation of the extracellular matrix. MMP-2 and MMP-9 have been implicated in a variety of pathological conditions including cardiovascular and neoplastic diseases, and recent studies have shown that circulating concentrations of MMP-9 may be a marker helping in the diagnosis and prognosis of cardiovascular and neoplastic diseases. We investigated whether there is an association between plasma MMP-2 and MMP-9 activities and the concentrations of lead in whole blood (blood Pb) or plasma (plasma Pb) from 40 lead-exposed persons (22 men and 18 women). Plasma Pb was determined by inductively coupled plasma mass spectrometry (ICP-MS) and blood Pb by graphite furnace atomic absorption spectrometry (GF-AAS). Plasma MMP-2 and MMP-9 activities were measured by gelatin zymography. We found a significant correlation between pro-MMP-9 activity in plasma and blood Pb (r=0.454; P=0.003), and between pro-MMP-9 activity in plasma and plasma Pb (r=0.312; P=0.049). No significant correlations were found between blood Pb or plasma Pb and plasma MMP-2. The association between pro-MMP-9 activity in plasma and both blood Pb and plasma Pb concentrations suggests a mechanism through which low lead exposure may increase the susceptibility to cardiovascular and neoplastic diseases. A causal relationship, however, remains to be proved.
pubmed-meshheading:16700817-Adolescent, pubmed-meshheading:16700817-Adult, pubmed-meshheading:16700817-Demography, pubmed-meshheading:16700817-Enzyme Precursors, pubmed-meshheading:16700817-Female, pubmed-meshheading:16700817-Humans, pubmed-meshheading:16700817-Lead, pubmed-meshheading:16700817-Lead Poisoning, pubmed-meshheading:16700817-Male, pubmed-meshheading:16700817-Matrix Metalloproteinase 2, pubmed-meshheading:16700817-Matrix Metalloproteinase 9, pubmed-meshheading:16700817-Middle Aged
Matrix metalloproteinase-9 activity in plasma correlates with plasma and whole blood lead concentrations.
Department of Clinical, Toxicological and Food Science Analysis, Faculty of Pharmaceutical Sciences of Ribeirao Preto, University of Sao Paulo, Av. do Cafe s/n, S.P. 14040-903, Ribeirao Preto, SP, Brazil.
Journal Article, Research Support, Non-U.S. Gov't