Production and activation of matrix metalloprotease-9 (MMP-9) by HL-60 promyelocytic leukemia cells
作者： Laetitia Devy , Agnès Noël , Eugénia Baramova , Khalid Bajou , Chantal Trentesaux
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摘要: Human promyelocytic HL-60 cells have been used as a model of acute leukemia to investigate the expression and regulation matrix metalloproteases (MMPs), known contribute degradation extracellular components. As shown by gelatin zymography, constitutively released significant amounts proMMP-9 (92 kDa) moderate proMMP-2 (72 kDa). Furthermore, casein zymography confirmed presence serine proteases in form pro-urokinase. Activation was dependent on plasminogen activator/plasmin (PA/plasmin) system inhibited aprotinin. MMP-9 only detected cellular extracts or conditioned media incubated with cells, indicating that are essential activation process. Addition increased 3-fold basal invasive rate these across matrigel layer (2.1% versus 0.7% control after 4 h incubation). Taken together, results indicate exhibit an autocrine mechanism via PA/plasmin increases their potential.
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