Purification and characterization of two related but distinct metalloproteinase inhibitors secreted by bovine aortic endothelial cells.

摘要: Abstract Two metalloproteinase inhibitors were purified from serum-free medium conditioned by bovine aortic endothelial cells. One of these inhibitors, with a molecular weight 30,000-34,000 (reduced) is identified as tissue inhibitor metalloproteinases; the second has 27,500 and 20,400 (unreduced), not recognized an antiserum against metalloproteinases, appears unglycosylated, 51% identity metalloproteinases NH2-terminal amino acid sequence analysis. This antiproteinase activities similar to those inhibition classical collagenase, type IV gelatinases but trypsin, plasmin, or bacterial collagenase. Other properties shared include trypsin sensitivity, heat resistance, inactivation reduction-alkylation. The presence in cells suggests that they may play important roles protecting integrity vascular basement membrane.