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rdf:type |
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lifeskim:mentions |
umls-concept:C0015350,
umls-concept:C0017262,
umls-concept:C0020564,
umls-concept:C0185117,
umls-concept:C0221464,
umls-concept:C0623362,
umls-concept:C0806140,
umls-concept:C0871261,
umls-concept:C1293134,
umls-concept:C1546857,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2911684,
umls-concept:C2911692
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pubmed:issue |
2
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pubmed:dateCreated |
2002-9-16
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pubmed:abstractText |
This study investigated the effects of high flow and shear stress on the expression of matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinase-2 (TIMP-2) during flow-induced arterial enlargement using a model of arteriovenous fistula (AVF) creation on the carotid artery with the corresponding jugular vein in Japanese white male rabbits. Flow increased 8-fold 7 days after AVF. Endothelial cells (EC) and smooth muscle cells (SMC) proliferated with internal elastic lamina (IEL) degradation in response to high flow and shear stress. Expression of MMP-2 mRNA peaked at 2 days (1700-fold) and maintained high level expression. MMP-9 mRNA gave a 10.8-fold increase within 2 days and decreased later. Their proteins were detected in EC and SMC. Membrane type-1-MMP (MT1-MMP) mRNA increased 121-fold at 3 days and maintained high expression. TGF-beta1 was increased after AVF. Two-peak up-regulation of Egr-1 mRNA was recognized at 1 and 5 days of AVF. These results suggest that high flow and shear stress can mediate EC and SMC to express MMP-2 and MMP-9, which degrade cell basement membranes and IEL to induce arterial enlargement. The disproportional increase in MT1-MMP and TIMP-2 might contribute to MMP-2 activation. Egr-1 and TGF-beta1 might play important roles in this process.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-4800
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
73
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
142-53
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12231217-Animals,
pubmed-meshheading:12231217-Arteries,
pubmed-meshheading:12231217-Arteriovenous Fistula,
pubmed-meshheading:12231217-Blood Flow Velocity,
pubmed-meshheading:12231217-Carotid Arteries,
pubmed-meshheading:12231217-Endothelium, Vascular,
pubmed-meshheading:12231217-Extracellular Matrix,
pubmed-meshheading:12231217-Jugular Veins,
pubmed-meshheading:12231217-Male,
pubmed-meshheading:12231217-Matrix Metalloproteinase 2,
pubmed-meshheading:12231217-Matrix Metalloproteinase 9,
pubmed-meshheading:12231217-Matrix Metalloproteinases,
pubmed-meshheading:12231217-Muscle, Smooth,
pubmed-meshheading:12231217-RNA, Messenger,
pubmed-meshheading:12231217-Rabbits,
pubmed-meshheading:12231217-Regional Blood Flow,
pubmed-meshheading:12231217-Stress, Mechanical,
pubmed-meshheading:12231217-Time Factors,
pubmed-meshheading:12231217-Tissue Inhibitor of Metalloproteinase-2,
pubmed-meshheading:12231217-Transforming Growth Factor beta,
pubmed-meshheading:12231217-Up-Regulation
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pubmed:year |
2002
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pubmed:articleTitle |
Arterial enlargement in response to high flow requires early expression of matrix metalloproteinases to degrade extracellular matrix.
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pubmed:affiliation |
Department of Surgery, Stanford University School of Medicine, Stanford, California 94305-5642, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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