Bone morphogenetic protein-9 is a circulating vascular quiescence factor. Laurent David, Christine Mallet, Michelle Keramidas, No¨ el Lamand´ e, Jean-Marie Gasc, Sophie Dupuis-Girod, Henri Plauchu, Jean-Jacques Feige, Sabine Bailly To cite this version: Laurent David, Christine Mallet, Michelle Keramidas, No¨ el Lamand´ e, Jean-Marie Gasc, et al.. Bone morphogenetic protein-9 is a circulating vascular quiescence factor.: BMP9 is present in serum and inhibits angiogenesis. Circulation Research, American Heart Association, 2008, 102 (8), pp.914-22. <10.1161/CIRCRESAHA.107.165530>. <inserm-00277236> HAL Id: inserm-00277236 http://www.hal.inserm.fr/inserm-00277236 Submitted on 29 Aug 2008 HAL is a multi-disciplinary open access archive for the deposit and dissemination of sci- entific research documents, whether they are pub- lished or not. The documents may come from teaching and research institutions in France or abroad, or from public or private research centers. L’archive ouverte pluridisciplinaire HAL, est destin´ ee au d´ epˆ ot et ` a la diffusion de documents scientifiques de niveau recherche, publi´ es ou non, ´ emanant des ´ etablissements d’enseignement et de recherche fran¸cais ou ´ etrangers, des laboratoires publics ou priv´ es.
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Bone morphogenetic protein-9 is a circulating vascular
Jean-Marie Gasc, Sophie Dupuis-Girod, Henri Plauchu, Jean-Jacques Feige,
Sabine Bailly
To cite this version:
Laurent David, Christine Mallet, Michelle Keramidas, Noel Lamande, Jean-Marie Gasc, et al..Bone morphogenetic protein-9 is a circulating vascular quiescence factor.: BMP9 is present inserum and inhibits angiogenesis. Circulation Research, American Heart Association, 2008, 102(8), pp.914-22. <10.1161/CIRCRESAHA.107.165530>. <inserm-00277236>
HAL Id: inserm-00277236
http://www.hal.inserm.fr/inserm-00277236
Submitted on 29 Aug 2008
HAL is a multi-disciplinary open accessarchive for the deposit and dissemination of sci-entific research documents, whether they are pub-lished or not. The documents may come fromteaching and research institutions in France orabroad, or from public or private research centers.
L’archive ouverte pluridisciplinaire HAL, estdestinee au depot et a la diffusion de documentsscientifiques de niveau recherche, publies ou non,emanant des etablissements d’enseignement et derecherche francais ou etrangers, des laboratoirespublics ou prives.
This is an un-copyedited author manuscript that was accepted for publication in Coirculation Research, copyright The American Heart Association. This may not be duplicated or reproduced, other than for personal use or within the “Fair Use of Copyrighted Materials” (section 107, title 17, U.S. Code) without prior permission of the copyright owner, The American Heart Association. The final copyedited article, which is the version of record, can be found at http://circres.ahajournals.org. The American Heart Association disclaims any responsibility or liability for errors or omissions in this version of the manuscript or in any version derived from it
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BMP9 IS A CIRCULATING VASCULAR QUIESCENCE FACTOR
Running title: BMP9 is present in serum and inhibits angiogenesis
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12. Brown MA, Zhao Q, Baker KA, Naik C, Chen C, Pukac L, Singh M, Tsareva T, Parice Y, Mahoney A, Roschke V, Sanyal I, Choe S. Crystal structure of BMP-9 and functional interactions with pro-region and receptors. J Biol Chem. 2005;280:25111-25118.
13. David L, Mallet C, Mazerbourg S, Feige JJ, Bailly S. Identification of BMP9 and BMP10 as functional activators of the orphan activin receptor-like kinase 1 (ALK1) in endothelial cells. Blood. 2007;109:1953-1961.
14. Scharpfenecker M, van Dinther M, Liu Z, van Bezooijen RL, Zhao Q, Pukac L, Lowik CW, ten Dijke P. BMP-9 signals via ALK1 and inhibits bFGF-induced endothelial cell proliferation and VEGF-stimulated angiogenesis. J Cell Sci. 2007;120:964-972.
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23. Trembath RC, Thomson JR, Machado RD, Morgan NV, Atkinson C, Winship I, Simonneau G, Galie N, Loyd JE, Humbert M, Nichols WC, Morrell NW, Berg J, Manes A, McGaughran J, Pauciulo M, Wheeler L. Clinical and molecular genetic features of pulmonary hypertension in patients with hereditary hemorrhagic telangiectasia. N Engl J Med. 2001;345:325-334.
24. Valdimarsdottir G, Goumans MJ, Rosendahl A, Brugman M, Itoh S, Lebrin F, Sideras P, ten Dijke P. Stimulation of Id1 expression by bone morphogenetic protein is sufficient and necessary for bone morphogenetic protein-induced activation of endothelial cells. Circulation. 2002;106:2263-2270.
25. Yamashita H, Shimizu A, Kato M, Nishitoh H, Ichijo H, Hanyu A, Morita I, Kimura M, Makishima F, Miyazono K. Growth/differentiation factor-5 induces angiogenesis in vivo. Exp Cell Res. 1997;235:218-226.
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Figure Legends 1
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Figure 1. Presence of an ALK1 ligand in human serum that differs from TGFβ
NIH-3T3 cells were transiently transfected with pALK1 and pRL-TK-luc and either
pGL3(BRE)-luc (A) or pGL3(CAGA)12-luc (B). Transfected cells were then treated either
with human serum (2%), TGFß1 (0.5 ng/ml) or heat-activated human serum (2%) with or
without pan-specific neutralizing TGFß antibody (1 µg/ml). C: NIH-3T3 cells were
transiently transfected with pGL3(BRE)-luc, pALK1 and pRL-TK-luc. Transfected cells were
then treated with human serum (2%) in presence or absence of either ALK1ecd, ALK2ecd,
ALK3ecd, ALK6ecd or soluble endoglin (200 ng/ml). The luciferase activities were then
measured as described in Materials and Methods. Data shown in A, B and C are expressed as
mean values ± SD from a representative experiment out of three.
Figure 2. Purification and estimation of the molecular weight of the ALK1 ligand from
the human serum
A: Scheme of purification of ALK1 ligand from 250 ml of a pool of human sera. The proteins
present in the active fractions (23 and 24) of the Pro-RPC column and the two surrounding
fractions (22 and 25), as determined with the BRE reporter gene assay (see Material and
Methods), were then separated by 12% SDS-PAGE. After the migration, the gel (fractions 23
and 24) was sliced into 6 parts as indicated by the dotted lines and the proteins were electro-
eluted. B: NIH-3T3 cells were transiently transfected with pGL3(BRE)-luc, pALK1 and pRL-
TK-luc. Transfected cells were then treated with 100 µl of either the active fractions (fraction
23 and 24) or 100 µl of the proteins eluted from each gel slice. The luciferase activities were
then measured as described in Materials and Methods. Data are expressed as mean values ±
SD from a representative experiment out of three.
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Figure 3. The ALK1 activity of the human serum is due to BMP9 1
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A, B, C and D: NIH-3T3 cells were transiently transfected with pGL3(BRE)-luc, pRL-TK-luc
and pALK1. A: Transfected cells were then treated with BMP9 (0.1 ng/ml), or BMP10 (20
ng/ml), or BMP2 (100 ng/ml) in the presence or the absence of a neutralizing BMP9 antibody
(1 µg/ml) or an isotype-matched control antibody (1µg/ml) . B: Transfected cells were then
treated with human serum (1%) or 100 µl of active fraction (fractions 23 and 24 of Fig. 2A).
C: Transfected cells were treated with 2% human serum in the presence or the absence of