Release of heat shock protein 70 (Hsp70) and the effects of extracellular Hsp70 on matric metalloproteinase-9 expression in human monocytic U937 cells
Experimental & Molecular Medicine
;
: 364-374, 2006.
Article
Dans Anglais
| WPRIM
| ID: wpr-53154
ABSTRACT
Heat shock protein 70 (Hsp70) release and its effects on pro-inflammatory cytokine production have been controversial. In this study, we investigated whether Hsp70 could be released from monocytes and activates matrix metalloproteinase-9 (MMP-9) gene expression. Hsp70 overexpression in human monocytic cell line U937 was found to increase PMA- induced MMP-9 expression and enhance cell motility. Hsp70 cDNA transfectants released Hsp70 protein into culture supernatants, and a part of released Hsp70 subsequently was bound to the surface of U937 cells. Addition of culture medium containing the extracelluar Hsp70 led to an increase not only in proMMP-9 secretion, but also the invasiveness of U937 cells through Matrigel or human umbilical vascular endothelial cells (HUVEC) in vitro. Immunodepletion of Hsp70 abolished its effect on MMP-9 expression. The released Hsp70 activated nuclear factor kappa B (NF-kappa B) and activating protein-1 (AP-1), which led to the activation of MMP-9 transcription. Taken together, these results suggest that extracellular Hsp70 induces the expression of MMP-9 gene through activation of NF-kappa B and AP-1.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Transfection
/
Mouvement cellulaire
/
Régulation de l'expression des gènes
/
Facteur de transcription NF-kappa B
/
Milieux de culture conditionnés
/
Facteur de transcription AP-1
/
Protéines du choc thermique HSP70
/
Cellules U937
/
Matrix metalloproteinase 9
Limites du sujet:
Humains
langue:
Anglais
Texte intégral:
Experimental & Molecular Medicine
Année:
2006
Type:
Article
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