The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Heterodimers of Placenta Growth Factor/Vascular Endothelial Growth Factor
Open accessAbstract
Here we show that the Escherichia coli expressed monomers of placenta growth factor (PLGF)129 and vascular endothelial growth factor (VEGF)165 can be re-folded in vitro to form PLGF/VEGF heterodimers. The purified recombinant PLGF/VEGF heterodimers and VEGF homodimers have potent mitogenic and chemotactic effects on endothelial cells. However, PLGF/VEGF heterodimers display 20-50-fold less mitogenic activity than VEGF165 homodimers. In contrast, PLGF129 homodimers have little or no effect in these in vitro assays. We also demonstrate the presence of natural PLGF/VEGF heterodimers in the conditioned media of various human tumor cell lines. While PLGF/VEGF heterodimers bind with high affinity to a soluble Flk-1/KDR receptor, PLGF129 homodimers fail to bind to this receptor. Cross-linking of 125I-ligands to human umbilical vein endothelial cells reveals that PLGF/VEGF heterodimers and VEGF165 homodimers, but not PLGF129 homodimers, form complexes with membrane receptors. VEGF165 homodimers and PLGF/VEGF heterodimers stimulate tyrosine phosphorylation of a 220-kDa protein, the expected size for the KDR receptor in human umbilical vein endothelial cells, whereas PLGF129 homodimers are unable to induce tyrosine phosphorylation of this protein. These data indicate that PLGF may modulate VEGF-induced angiogenesis by the formation of PLGF/VEGF heterodimers in cells producing both factors.
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Cites
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Cited by
The splice variants of vascular endothelial growth factor (VEGF) and their receptors
Robinson, C. J., & Stringer, S. E. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.853 · Cited by 944
Mechanisms of normal and tumor-derived angiogenesis
Papetti, M., & Herman, I. M. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00389.2001 · Cited by 809
Proteolytic processing regulates receptor specificity and activity of VEGF-C
Joukov, V., Sorsa, T., Kumar, V., Jeltsch, M., Claesson-Welsh, L., Cao, Y., Saksela, O., Kalkkinen, N., & Alitalo, K. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.3898 · Cited by 773
Self-citationRegulation of angiogenesis: Wound healing as a model
EMING, S., BRACHVOGEL, B., ODORISIO, T., & KOCH, M. (2007) · Progress in Histochemistry and Cytochemistry · doi:10.1016/j.proghi.2007.06.001 · Cited by 392
Cao, R., Eriksson, A., Kubo, H., Alitalo, K., Cao, Y., & Thyberg, J. (2004) · Circulation Research · doi:10.1161/01.res.0000118600.91698.bb · Cited by 324
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Metadata
- Authors
- Cao, Y., Chen, H., Zhou, L., Chiang, M.-K., Anand-Apte, B., Weatherbee, J. A., Wang, Y., Fang, F., Flanagan, J. G., & Tsang, M. L.-S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-02
- Volume
- 271
- Issue
- 6
- Pages
- 3154-3162
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2013141629
- Cited by
- 295
- References
- 46
- FWCI
- 8.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Cao, Y., Chen, H., Zhou, L., Chiang, M.-K., Anand-Apte, B., Weatherbee, J. A., Wang, Y., Fang, F., Flanagan, J. G., & Tsang, M. L.-S. (1996). Heterodimers of Placenta Growth Factor/Vascular Endothelial Growth Factor. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.271.6.3154
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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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