Galectin-1 is essential in tumor angiogenesis and is a target for antiangiogenesis therapy.

Archive ouverte

Thijssen, Victor, L. J. L. | Postel, Ruben | Brandwijk, Ricardo, J. M. G. E. | Dings, Ruud, P. M. | Nesmelova, Irina | Satijn, Sietske | Verhofstad, Nicole | Nakabeppu, Yusaku | Baum, Linda, G. | Bakkers, Jeroen | Mayo, Kevin, H. | Poirier, Françoise | Griffioen, Arjan, W.

Edité par CCSD ; National Academy of Sciences -

International audience. We describe that galectin-1 (gal-1) is a receptor for the angiogenesis inhibitor anginex, and that the protein is crucial for tumor angiogenesis. gal-1 is overexpressed in endothelial cells of different human tumors. Expression knockdown in cultured endothelial cells inhibits cell proliferation and migration. The importance of gal-1 in angiogenesis is illustrated in the zebrafish model, where expression knockdown results in impaired vascular guidance and growth of dysfunctional vessels. The role of gal-1 in tumor angiogenesis is demonstrated in gal-1-null mice, in which tumor growth is markedly impaired because of insufficient tumor angiogenesis. Furthermore, tumor growth in gal-1-null mice no longer responds to antiangiogenesis treatment by anginex. Thus, gal-1 regulates tumor angiogenesis and is a target for angiostatic cancer therapy.

Suggestions

Du même auteur

Galectins in the tumor endothelium: opportunities for combined cancer therapy.

Archive ouverte | Thijssen, Victor L J L | CCSD

International audience. Galectins are emerging as a family of proteins that play an important role in several steps of tumorigenesis. Evidence is accumulating that galectins are expressed by the tumor endothelium, w...

GDNF promotes neurite outgrowth and upregulates galectin-1 through the RET/PI3K signaling in cultured adult rat dorsal root ganglion neurons.

Archive ouverte | Takaku, Shizuka | CCSD

International audience. Galectin-1 (GAL-1), a member of a family of β-galactoside binding animal lectins, is predominantly expressed in isolectin B4 (IB4)-binding small non-peptidergic (glial cell line-derived neuro...

Substrate recognition by the human MTH1 protein.

Archive ouverte | Kamiya, Hiroyuki | CCSD

A nucleotide pool sanitizing enzyme, the human MTH1 protein, hydrolyzes 2-hydroxy-dATP, 8-hydroxy-dATP, and 8-hydroxyd-GTP. To examine the substrate recognition mechanism of the MTH1 protein, ten nucleotide analogs (8-bromo-dATP, ...

Chargement des enrichissements...