Exp Mol Med.
2006 Aug;38(4):364-374.
Release of heat shock protein 70 (Hsp70) and the effects of extracellular Hsp70 on matric metalloproteinase-9 expression in human monocytic U937 cells
- Affiliations
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- 1Department of Anatomy and Cell Biology, College of Medicine, Kangwon National University, Chuncheon 200-701, Korea. jhahn@kangwon.ac.kr
- 2Department of Biochemistry, College of Natural Science, Kangwon National University, Chuncheon 200-701, Korea.
- 3Vascular System Research Center, Kangwon National University, Chuncheon 200-701, Korea.
- 4Department of Biomedical Science and Institute of Bioscience and Biotechnology, College of Natural Sciences, Hallym University, Chuncheon 200-702, Korea.
- 5Department of Biochemistry, College of Sciences, Yonsei University, Seoul 120-749, Korea.
- 6Laboratory of Radiation Effect, Division of Radiation Biology, Korea Institute of Radiological and Medical Sciences, Seoul 139-706, Korea.
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.
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