Molecular cloning and characterization of a novel angiopoietin family protein, angiopoietin‐3

Kim, Injune; Kwak, Hee Jin; Ahn, Ji-Eun; So, June-No; Liu, Mingzhu; Koh, Keum Nim; Koh, Gou Young

doi:10.1016/s0014-5793(99)00008-3

Cited by 75 publications

(59 citation statements)

References 15 publications

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“…The expression vectors encoded gD epitope-tagged versions of ANGPTL3 and Ang2, which served as a positive control for Tie2 binding. As negative control, we included conditioned media containing ARP1 (28), an angiopoietin-like ligand encoding a signal peptide, an N-terminal coiled-coil, and a Cterminal FBN-like domain. As shown in Fig.…”

Section: Angptl3 Binds To Endothelial Cells Via Receptorsmentioning

confidence: 99%

ANGPTL3 Stimulates Endothelial Cell Adhesion and Migration via Integrin αvβ3 and Induces Blood Vessel Formation in Vivo

Camenisch¹,

Pisabarro²,

Sherman³

et al. 2002

Journal of Biological Chemistry

225

209

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The angiopoietin family of secreted factors is functionally defined by the C-terminal fibrinogen (FBN)-like domain, which mediates binding to the Tie2 receptor and thereby facilitates a cascade of events ultimately regulating blood vessel formation. By screening expressed sequence tag data bases for homologies to a consensus FBN-like motive, we have identified ANGPTL3, a liver-specific, secreted factor consisting of an N-terminal coiled-coil domain and the C-terminal FBN-like domain. Co-immunoprecipitation experiments, however, failed to detect binding of ANGPTL3 to the Tie2 receptor. A molecular model of the FBN-like domain of ANGPTL3 was generated and predicted potential binding to integrins. This hypothesis was experimentally confirmed by the finding that recombinant ANGPTL3 bound to ␣ v ␤ 3 and induced integrin ␣ v ␤ 3 -dependent haptotactic endothelial cell adhesion and migration and stimulated signal transduction pathways characteristic for integrin activation, including phosphorylation of Akt, mitogen-activated protein kinase, and focal adhesion kinase. When tested in the rat corneal assay, ANGPTL3 strongly induced angiogenesis with comparable magnitude as observed for vascular endothelial growth factor-A. Moreover, the C-terminal FBN-like domain alone was sufficient to induce endothelial cell adhesion and in vivo angiogenesis. Taken together, our data demonstrate that ANGPTL3 is the first member of the angiopoietin-like family of secreted factors binding to integrin ␣ v ␤ 3 and suggest a possible role in the regulation of angiogenesis.

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Section: Angptl3 Binds To Endothelial Cells Via Receptorsmentioning

confidence: 99%

ANGPTL3 Stimulates Endothelial Cell Adhesion and Migration via Integrin αvβ3 and Induces Blood Vessel Formation in Vivo

Camenisch¹,

Pisabarro²,

Sherman³

et al. 2002

Journal of Biological Chemistry

225

209

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“…To date there are four known angiopoietins, which all bind to the Tie-2 receptor, mediating vessel stabilization signals, whereas the Tie-1 receptor has so far no known ligand (Figure 2) Maisonpierre et al, 1997;Kim et al, 1999;Valenzuela et al, 1999). The phenotypes of Tie-2 and Ang-1 de®cient mice suggest a role for this ligand ± receptor system in maintaining communication between endothelial cells and the surrounding mesenchyme, in order to establish stable cellular and biochemical interactions between endothelial cells and pericytes/ smooth muscle cells (Dumont et al, 1994;Puri et al, 1995;Suri et al, 1997).…”

Section: Angiopoietinsmentioning

confidence: 99%

Mechanisms of angiogenesis and their use in the inhibition of tumor growth and metastasis

2000

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“…Recently, we (8)(9)(10) and others (11)(12)(13)(14)(15) identified several genes encoding proteins containing both the coiled-coil domain and the fibrinogen-like domain. Although these factors were initially predicted to function as ligands for Tie receptors, they bound neither Tie1 nor Tie2.…”

mentioning

confidence: 99%

“…Therefore, they are currently orphan ligands and designated angiopoietin-like proteins (Angptls) or angiopoietin-related proteins (ARPs). Several studies show that Angptl͞ARP family proteins possess potent activities in the vascular system (8)(9)(10)(11)(12)(13)(14)(15)(16). Angptl1 and Angptl2 have been reported to possess weak endothelial cell-sprouting activities (11,12); however, there is little information as to their physiological functions.…”

mentioning

confidence: 99%

Cooperative interaction of Angiopoietin-like proteins 1 and 2 in zebrafish vascular development

Kubota

Oike

Satoh

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Angiopoietin-like protein (Angptl) 1 and Angptl2, which are considered orphan ligands, are highly homologous, particularly in the fibrinogen-like domain containing the putative receptor binding site. This similarity suggests potentially cooperative functions between the two proteins. In this report, the function of Angptl1 and Angptl2 is analyzed by using morpholino antisense technology in zebrafish. Knockdown of both Angptl1 and Angptl2 produced severe vascular defects due to increased apoptosis of endothelial cells at the sprouting stage. In vitro studies showed that Angptl1 and Angptl2 have antiapoptotic activities through the phosphatidylinositol 3-kinase͞Akt pathway, and coinjection of constitutively active Akt͞protein kinase B mRNA rescued impaired vascular development seen in double knockdown embryos. These results provide a physiological demonstration of the cooperative interaction of Angptl1 and Angptl2 in endothelial cells through phosphatidylinositol 3-kinase͞Akt mediated antiapoptotic activities.angiogenesis ͉ morpholino ͉ phosphatidylinositol 3-kinase ͉ Akt ͉ apoptosis

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Molecular cloning and characterization of a novel angiopoietin family protein, angiopoietin‐3

Cited by 75 publications

References 15 publications

ANGPTL3 Stimulates Endothelial Cell Adhesion and Migration via Integrin αvβ3 and Induces Blood Vessel Formation in Vivo

ANGPTL3 Stimulates Endothelial Cell Adhesion and Migration via Integrin αvβ3 and Induces Blood Vessel Formation in Vivo

Mechanisms of angiogenesis and their use in the inhibition of tumor growth and metastasis

Cooperative interaction of Angiopoietin-like proteins 1 and 2 in zebrafish vascular development

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