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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2006.1
- 수록면
- 364 - 374 (11page)
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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 mono-cytic 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 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. Im-munodepletion 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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참고문헌 (28)
참고문헌 신청
/ / Selective release from cultured mammalian cells of heat-shock proteins that resemble glia-axon transfer proteins : 257 ~ 66
/ / v
/ 1998 / Human toll-like receptor 2 confers responsiveness to bacterial lipopoly-saccharide 188 : 2091 ~ 2097
/ 1999 / Anti- heat-shock protein 70 kDa antibodies in vascular patients 18 : 381 ~ 385
/ 2000 / HSP70 stimulates cy-tokine production through a CD14 dependent pathway dem-onstrating its dual roles as a chaperone and cytokine 6 : 435 ~ 442
/ / v
/ 1998 / Human toll-like receptor 2 confers responsiveness to bacterial lipopoly-saccharide 188 : 2091 ~ 2097
/ 1999 / Anti- heat-shock protein 70 kDa antibodies in vascular patients 18 : 381 ~ 385
/ 2000 / HSP70 stimulates cy-tokine production through a CD14 dependent pathway dem-onstrating its dual roles as a chaperone and cytokine 6 : 435 ~ 442
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