The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Pericellular Proteases in Angiogenesis and Vasculogenesis
Abstract
Pericellular proteases play an important role in angiogenesis and vasculogenesis. They comprise (membrane-type) matrix metalloproteinases [(MT-)MMPs], serine proteases, cysteine cathepsins, and membrane-bound aminopeptidases. Specific inhibitors regulate them. Major roles in initiating angiogenesis have been attributed to MT1-matrix metalloproteinase (MMP), MMP-2, and MMP-9. Whereas MT-MMPs are membrane-bound by nature, MMP-2 and MMP-9 can localize to the membrane by binding to αvβ3-integrin and CD44, respectively. Proteases switch on neovascularization by activation, liberation, and modification of angiogenic growth factors and degradation of the endothelial and interstitial matrix. They also modify the properties of angiogenic growth factors and cytokines. Neovascularization requires cell migration, which depends on the assembly of protease–protein complexes at the migrating cell front. MT1-MMP and urokinase (u-PA) form multiprotein complexes in the lamellipodia and focal adhesions of migrating cells, facilitating proteolysis and sufficient support for endothelial cell migration and survival. Excessive proteolysis causes loss of endothelial cell-matrix interaction and impairs angiogenesis. MMP-9 and cathepsin L stimulate the recruitment and action of blood- or bone-marrow-derived accessory cells that enhance angiogenesis. Proteases also generate fragments of extracellular matrix and hemostasis factors that have anti-angiogenic properties. Understanding the complexity of protease activities in angiogenesis contributes to recognizing new targets for stimulation or inhibition of neovascularization in disease.
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Cites
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Endostatin: an endogenous inhibitor of angiogenesis and tumor growth
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Circulating endothelial progenitor cells, vascular function, and cardiovascular risk
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Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis
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Circulating endothelial progenitor cells and cardiovascular outcomes
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Regulation of matrix biology by matrix metalloproteinases
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“Heissig et al144 recently proposed an amplifying mechanism, in which: (1) circulating VEGF induced MMP-9 expression in the bone marrow; (2) MMP-9 released c-kit ligand; (3) c-kit activation recruits hemopoietic, endothelial and mast cell progenitor cells; and (4) mast cells accumulating in the angiogenic area produce…”
Background
Cited by
The matrix corroded: podosomes and invadopodia in extracellular matrix degradation
Linder, S. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.01.002 · Cited by 640
Identification and functional analysis of endothelial tip cell–enriched genes
del Toro, R., Prahst, C., Mathivet, T., Siegfried, G., Kaminker, J. S., Larrivee, B., Breant, C., Duarte, A., Takakura, N., Fukamizu, A., et al. (2010) · Blood · doi:10.1182/blood-2010-02-270819 · Cited by 474
Endothelial sprouting and angiogenesis: matrix metalloproteinases in the lead
van Hinsbergh, V. W. M., & Koolwijk, P. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvm102 · Cited by 420
Self-citationLee, C., Kim, M.-J., Kumar, A., Lee, H.-W., Yang, Y., & Kim, Y. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02249-0 · Cited by 365
In vitro assays of angiogenesis for assessment of angiogenic and anti-angiogenic agents
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Metadata
- Authors
- van Hinsbergh, V. W. M., Engelse, M. A., & Quax, P. H. A.
- Venue
- Arteriosclerosis, Thrombosis, and Vascular Biology
- Published
- 2006-04
- Volume
- 26
- Issue
- 4
- Pages
- 716-728
- ISSN
- 1079-5642 (ISSN-L)
- 1524-4636
- OpenAlex
- W2058239698
- Cited by
- 389
- References
- 13
- FWCI
- 10.87
- Type
- journal article
- Language
- en
- Open access
- closed
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- van Hinsbergh, V. W. M., Engelse, M. A., & Quax, P. H. A. (2006). Pericellular Proteases in Angiogenesis and Vasculogenesis. Arteriosclerosis, Thrombosis, and Vascular Biology. https://doi.org/10.1161/01.atv.0000209518.58252.17
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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