Reference : Effect of ADAMTS-2, a metalloproteinase containing a disintegrin domain and thrombospond...
Scientific congresses and symposiums : Paper published in a journal
Life sciences : Anatomy (cytology, histology, embryology...) & physiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/8123
Effect of ADAMTS-2, a metalloproteinase containing a disintegrin domain and thrombospondin type I repeats, during angiogenesis in vitro and in vivo
English
Dubail, Johanne [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Protéines et glycoprot. de matr.extracell. et membran.basal. >]
Kesteloot, Frédéric mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Protéines et glycoprot. de matr.extracell. et membran.basal. > >]
Motte, Patrick mailto [Université de Liège - ULg > Département des sciences de la vie > Génomique fonctionnelle et imagerie moléculaire végétale >]
Lambert, Vincent mailto [Centre Hospitalier Universitaire de Liège - CHU > > Ophtalmologie > >]
Rakic, Jean-Marie mailto [Université de Liège - ULg > Département des sciences cliniques > Ophtalmologie >]
Lapière, Charles M [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Protéines et glycoprot. de matr.extracell. et membran.basal. > >]
Nusgens, Betty mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Département des sciences biomédicales et précliniques >]
Colige, Alain mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Protéines et glycoprot. de matr.extracell. et membran.basal. >]
2004
Angiogenesis
Kluwer Academic Publishers
7
2
172
Yes (verified by ORBi)
No
0969-6970
Dordrecht
The Netherlands
15th Endothelial Cell Research Symposium
23/11/2004
University Maastricht
Maastricht
The Netherlands
[en] Formation of new blood vessels (angiogenesis) is a key step during the development of various pathologies, including cancer. Enzymes of the ADAMTS family are closely related to MMPs and ADAMs. They further contain specific domains, such as the ‘‘Thrombospondin type I’’ (TSP1) repeats, that are able to strongly repress angiogenesis, as described for thrombospondin-1 and -2, and for ADAMTS-1 and -8. The primary function of ADAMTS-2 is to process collagen type I, II and III precursors into mature molecules by excising the aminopropeptide. We further hypothesized that it could modulate angiogenesis through its TSP1 repeats. This hypothesis was investigated using different in vitro experimental models of angiogenesis. Recombinant ADAMTS-2 induced morphological changes in human umbilical vein endothelial cells (HUVEC) and human microvessel endothelial cells (HMEC), and significantly reduced their proliferation, attachment and spreading. Similar effects were observed when using inactive ADAMTS-2 mutated at the Zn2+-binding catalytic site. ADAMTS-2 did not alter the initial steps of formation of capillary-like structures by HUVEC in vitro. However, these structures appeared much less stable and were more rapidly disrupted in presence of ADAMTS-2 than in control conditions. ADAMTS-2 was also tested in an ex vivo angiogenesis model using aortic rings from rats and mice, wild type or KO for ADAMTS-2. Outgrowth of capillaries was slightly increased from aortas of ADAMTS-2 KO mice (TS2-/-) as compared to aortas from control animals (TS2+/+), while addition of full size recombinant ADAMTS-2 reduced the formation of capillary structures from rat aortas, suggesting its anti-angiogenic activity. Choroidal neovascularization induced in TS2+/+ or TS2-/- mice by LASER burns was used as in vivo model to confirm the in vitro and ex vivo results. Several genes involved in the healing and angiogenesis processes (fibrillar collagens, VEGF, TGF-beta and CTGF) were not differently regulated in TS2+/+ and TS2-/- mice at 5 days.
Researchers
http://hdl.handle.net/2268/8123

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