Release of heat shock protein 70 (Hsp70) and the effects of extracellular Hsp70 on matric metalloproteinase-9 expression in human monocytic U937 cells

Kyoung Jin Lee, Yoo Mih Kim, Dae Young Kim, Dooil Jeoung, Kyuhyung Han, Seung Taek Lee, Yun Sil Lee, Kyeong Han Park, Jeong Hyun Park, Dae Joong Kim, Jang Hee Hahn

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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-κB) 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-κB and AP-1.

Original languageEnglish
Pages (from-to)364-374
Number of pages11
JournalJournal of the Chinese Medical Association
Volume38
Issue number4
Publication statusPublished - 2006 Aug 31

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U937 Cells
HSP70 Heat-Shock Proteins
Metalloproteases
Matrix Metalloproteinase 9
NF-kappa B
Umbilicus
Proteins
Transcriptional Activation
Cell Movement
Culture Media
Monocytes
Endothelial Cells
Complementary DNA
Cytokines
Gene Expression
Cell Line

All Science Journal Classification (ASJC) codes

  • Medicine(all)

Cite this

Lee, Kyoung Jin ; Kim, Yoo Mih ; Kim, Dae Young ; Jeoung, Dooil ; Han, Kyuhyung ; Lee, Seung Taek ; Lee, Yun Sil ; Park, Kyeong Han ; Park, Jeong Hyun ; Kim, Dae Joong ; Hahn, Jang Hee. / Release of heat shock protein 70 (Hsp70) and the effects of extracellular Hsp70 on matric metalloproteinase-9 expression in human monocytic U937 cells. In: Journal of the Chinese Medical Association. 2006 ; Vol. 38, No. 4. pp. 364-374.
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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-κB) 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-κB and AP-1.",
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Lee, KJ, Kim, YM, Kim, DY, Jeoung, D, Han, K, Lee, ST, Lee, YS, Park, KH, Park, JH, Kim, DJ & Hahn, JH 2006, 'Release of heat shock protein 70 (Hsp70) and the effects of extracellular Hsp70 on matric metalloproteinase-9 expression in human monocytic U937 cells', Journal of the Chinese Medical Association, vol. 38, no. 4, pp. 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. / Lee, Kyoung Jin; Kim, Yoo Mih; Kim, Dae Young; Jeoung, Dooil; Han, Kyuhyung; Lee, Seung Taek; Lee, Yun Sil; Park, Kyeong Han; Park, Jeong Hyun; Kim, Dae Joong; Hahn, Jang Hee.

In: Journal of the Chinese Medical Association, Vol. 38, No. 4, 31.08.2006, p. 364-374.

Research output: Contribution to journalArticle

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AU - Lee, Kyoung Jin

AU - Kim, Yoo Mih

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AU - Jeoung, Dooil

AU - Han, Kyuhyung

AU - Lee, Seung Taek

AU - Lee, Yun Sil

AU - Park, Kyeong Han

AU - Park, Jeong Hyun

AU - Kim, Dae Joong

AU - Hahn, Jang Hee

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N2 - 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-κB) 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-κB and AP-1.

AB - 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-κB) 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-κB and AP-1.

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