Adenovirus-mediated expression of tissue factor pathway inhibitor-2 inhibits endothelial cell migration and angiogenesis
Arteriosclerosis, Thrombosis, and Vascular Biology, ISSN: 1079-5642, Vol: 27, Issue: 2, Page: 310-316
2007
- 61Citations
- 18Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations61
- Citation Indexes61
- 61
- CrossRef42
- Captures18
- Readers18
- 18
Article Description
OBJECTIVE - Extracellular matrix (ECM) remodeling during angiogenesis is accomplished through plasmin-dependent pericellular proteolysis and through the action of matrix metalloproteinases (MMPs). Because tissue factor pathway inhibitor-2 (TFPI-2), a Kunitz-type protease inhibitor with prominent ECM localization, inhibits plasmin and MMPs activity, we investigated the role of TFPI-2 in endothelial cell (EC) migration and angiogenesis. METHODS AND RESULTS - Real-time polymerase chain reaction and immunostaining showed that the expression of TFPI-2 mRNA and protein was upregulated in migrating ECs. The effect of TFPI-2 on angiogenesis was studied in mouse models of Matrigel and polyvinylalcohol sponge implants by overexpressing TFPI-2 through infection with a replication-deficient adenovirus (AdTFPI-2). Using (immuno)fluorescence and confocal microscopy we observed that TFPI-2 reduced neovascularization and promoted ECM deposition. Lateral cell migration and capillary tube formation in vitro also were impaired by TFPI-2, a process reversed by anti-TFPI-2 antibodies. Increased apoptosis occurred both in AdTFPI-2-treated ECs and in the mouse implants. Zymography and assays in the absence of plasminogen confirmed plasmin inhibition as a main mechanism through which TFPI-2 inhibits EC migration. CONCLUSIONS - Our data suggest that TFPI-2 may be an important regulator of aberrant angiogenesis associated with tumor growth/metastasis, cardiovascular diseases, chronic inflammation, or diabetes. © 2007 American Heart Association, Inc.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33846403724&origin=inward; http://dx.doi.org/10.1161/01.atv.0000254147.89321.cf; http://www.ncbi.nlm.nih.gov/pubmed/17138934; https://www.ahajournals.org/doi/10.1161/01.ATV.0000254147.89321.cf; http://atvb.ahajournals.org/cgi/doi/10.1161/01.ATV.0000254147.89321.cf; https://www.ahajournals.org/doi/full/10.1161/01.ATV.0000254147.89321.cf
Ovid Technologies (Wolters Kluwer Health)
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