The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
NG2 Proteoglycan Promotes Endothelial Cell Motility and Angiogenesis via Engagement of Galectin-3 and α3β1 Integrin
Open accessAbstract
The NG2 proteoglycan is expressed by microvascular pericytes in newly formed blood vessels. We have used in vitro and in vivo models to investigate the role of NG2 in cross-talk between pericytes and endothelial cells (EC). Binding of soluble NG2 to the EC surface induces cell motility and multicellular network formation in vitro and stimulates corneal angiogenesis in vivo. Biochemical data demonstrate the involvement of both galectin-3 and α3β1 integrin in the EC response to NG2 and show that NG2, galectin-3, and α3β1 form a complex on the cell surface. Transmembrane signaling via α3β1 is responsible for EC motility and morphogenesis in this system. Galectin-3–dependent oligomerization may potentiate NG2-mediated activation of α3β1. In conjunction with recent studies demonstrating the early involvement of pericytes in angiogenesis, these data suggest that pericyte-derived NG2 is an important factor in promoting EC migration and morphogenesis during the early stages of neovascularization.
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Cites
Angiogenesis in cancer, vascular, rheumatoid and other disease
Folkman, J. (1995) · Nature Medicine · doi:10.1038/nm0195-27 · Cited by 7,627
Cited by
Perivascular Gli1+ Progenitors Are Key Contributors to Injury-Induced Organ Fibrosis
Kramann, R., Schneider, R. K., DiRocco, D. P., Machado, F., Fleig, S., Bondzie, P. A., Henderson, J. M., Ebert, B. L., & Humphreys, B. D. (2015) · Cell Stem Cell · doi:10.1016/j.stem.2014.11.004 · Cited by 922
“Given a reported role for NG2 in angiogenesis (Fukushi et al., 2004), we next asked whether Gli1+ cells gain NG2 expression after myocardial infarction because angiogenesis is involved in the repair process of this model.”
Protein Glycosylation in Cancer
Stowell, S. R., Ju, T., & Cummings, R. D. (2015) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012414-040438 · Cited by 873
Advanced glycation endproducts: what is their relevance to diabetic complications?
Ahmed, N., & Thornalley, P. J. (2007) · Diabetes, Obesity and Metabolism · doi:10.1111/j.1463-1326.2006.00595.x · Cited by 371
The CNS microvascular pericyte: pericyte-astrocyte crosstalk in the regulation of tissue survival
Bonkowski, D., Katyshev, V., Balabanov, R. D., Borisov, A., & Dore-Duffy, P. (2011) · Fluids and Barriers of the CNS · doi:10.1186/2045-8118-8-8 · Cited by 207
Virgintino, D., Girolamo, F., Errede, M., Capobianco, C., Robertson, D., Stallcup, W. B., Perris, R., & Roncali, L. (2007) · Angiogenesis · doi:10.1007/s10456-006-9061-x · Cited by 184
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Metadata
- Authors
- Fukushi, J.-I., Makagiansar, I. T., & Stallcup, W. B.
- Venue
- Molecular Biology of the Cell
- Published
- 2004-08
- Volume
- 15
- Issue
- 8
- Pages
- 3580-3590
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2121681121
- Cited by
- 324
- References
- 1
- FWCI
- 5.82
- Type
- journal article
- Language
- en
- Open access
- green
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- Fukushi, J.-I., Makagiansar, I. T., & Stallcup, W. B. (2004). NG2 Proteoglycan Promotes Endothelial Cell Motility and Angiogenesis via Engagement of Galectin-3 and α3β1 Integrin. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.e04-03-0236
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