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
in En
| WPRIM
| ID: wpr-53154
Responsible library:
WPRO
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.
Key words
Full text:
1
Database:
WPRIM
Main subject:
Transfection
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Cell Movement
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Gene Expression Regulation
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NF-kappa B
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Culture Media, Conditioned
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Transcription Factor AP-1
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HSP70 Heat-Shock Proteins
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U937 Cells
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Matrix Metalloproteinase 9
Limits:
Humans
Language:
En
Journal:
Experimental & Molecular Medicine
Year:
2006
Document type:
Article