|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0026473,
umls-concept:C0030685,
umls-concept:C0086418,
umls-concept:C0185117,
umls-concept:C0243043,
umls-concept:C0391871,
umls-concept:C0521119,
umls-concept:C0600531,
umls-concept:C0680255,
umls-concept:C1280500,
umls-concept:C1283071,
umls-concept:C1963578,
umls-concept:C2911684
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
2006-9-5
|
|
pubmed:abstractText |
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-kappaB) 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-KappaB and AP-1.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
1226-3613
|
|
pubmed:author |
pubmed-author:HahnJang-HeeJH,
pubmed-author:HanKyuhyungK,
pubmed-author:JeoungDooilD,
pubmed-author:KimDae JoongDJ,
pubmed-author:KimDae YoungDY,
pubmed-author:KimYoo MihYM,
pubmed-author:LeeKyoung-JinKJ,
pubmed-author:LeeSeung-TaekST,
pubmed-author:LeeYun-SilYS,
pubmed-author:ParkJeong HyunJH,
pubmed-author:ParkKyeong HanKH
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
31
|
|
pubmed:volume |
38
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
364-74
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:16953115-Cell Movement,
pubmed-meshheading:16953115-Culture Media, Conditioned,
pubmed-meshheading:16953115-Gene Expression Regulation,
pubmed-meshheading:16953115-HSP70 Heat-Shock Proteins,
pubmed-meshheading:16953115-Humans,
pubmed-meshheading:16953115-Matrix Metalloproteinase 9,
pubmed-meshheading:16953115-NF-kappa B,
pubmed-meshheading:16953115-Transcription Factor AP-1,
pubmed-meshheading:16953115-Transfection,
pubmed-meshheading:16953115-U937 Cells
|
|
pubmed:year |
2006
|
|
pubmed:articleTitle |
Release of heat shock protein 70 (Hsp70) and the effects of extracellular Hsp70 on matric metalloproteinase-9 expression in human monocytic U937 cells.
|
|
pubmed:affiliation |
Department of Anatomy and Cell Biology, College of Medicine, Kangwon National University, Chuncheon 200-701, Korea.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
