Activated alpha2 macroglobulin induces matrix metalloproteinase 9 expression by low density lipoprotein receptor-related protein 1 through MAPK-ERK1/2 and NF-kappaB activation in macrophage derived cell lines.

CACERES L; BONACCI G; SANCHEZ MC; CHIABRANDO GA

JOURNAL OF CELLULAR BIOCHEMISTRY

WILEY-LISS, DIV JOHN WILEY & SONS INC

Año: 2010 vol. 111 p. 607 - 607

0730-2312

acrophages under certain stimuli induce matrix metalloproteinase 9 (MMP-9) expression and protein secretion through the activation of MAPK-ERK and NF-kappaB signaling pathways. Previously, we demonstrated that activated alpha(2)-macroglulin (alpha(2)M*) through the interaction with its receptor low density lipoprotein receptor-related protein 1 (LRP1) induces macrophage proliferation mediated by the activation of MAPK-ERK1/2. In the present work, we examined whether 2M*/LRP1interaction could induce the MMP-9 production in J774 and Raw264.7 macrophage-derived cell lines. It was shown that alpha(2)M* promoted MMP-9 expression and protein secretion by LRP1 in both macrophage-derived cell lines, which was mediated by the activation of MAPK-ERK1/2 and NF-kappaB. Both intracellular signaling pathways activated by alpha(2)M* were effectively blocked by calphostin-C, suggesting involvement of PKC. In addition, we demonstrate that alpha(2)M* produced extracellular calcium influx via LRP1. Howe