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Am J Physiol Lung Cell Mol Physiol 286: L1194-L1201, 2004. First published January 29, 2004; doi:10.1152/ajplung.00427.2003
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Hepatoma-derived growth factor is a pulmonary endothelial cell-expressed angiogenic factor

Allen D. Everett,1,2 Jill V. Narron,1 Tamara Stoops,1 Hideji Nakamura,3 and Amy Tucker2,4

1Department of Pediatrics, Division of Pediatric Cardiology, 4Department of Internal Medicine, Cardiovascular Division, 2Cardiovascular Research Center, University of Virginia Health System, Charlottesville, Virginia 22908; and 3Department of Internal Medicine, Hyogo College of Medicine, Nishinomiya, Hyogo 663-8501, Japan

Submitted 3 December 2003 ; accepted in final form 27 January 2004

Hepatoma-derived growth factor (HDGF) was previously identified as a developmentally regulated cardiovascular and renal gene that is mitogenic for vascular smooth muscle and aortic endothelial cells. As reciprocal interactions of smooth muscle and endothelial cells are necessary for vascular formation, we examined whether HDGF plays a role in angiogenesis. According to immunohistochemistry, HDGF was highly expressed in endothelial cells of nonmuscularized, forming blood vessels of the fetal lung. HDGF was also expressed in endothelial cells of small (20 µm) mature arteries and veins. By Western immunoblotting, HDGF was highly expressed by human pulmonary microvascular endothelial cells in vitro. Adenoviral overexpression of HDGF was mitogenic for human pulmonary microvascular endothelial cells in serum-free medium, stimulating a 1.75-fold increase in bromodeoxyuridine (BrdU) uptake and a twofold increase in cell migration. With the chick chorioallantoic membrane (CAM), a biologic assay for angiogenesis, exogenous recombinant HDGF significantly stimulated blood vessel formation and a dose-dependent reorganization of cells within the CAM into a more compact, linear alignment reminiscent of tube formation. According to double immunostaining for endothelial cells with a transforming growth factor-{beta}II receptor antibody and BrdU as a marker of cell proliferation, exogenous HDGF selectively stimulated endothelial cell BrdU uptake. HDGF also activated specific ERK1/2 signaling and did not overlap with VEGF SAPK/JNK, Akt-mediated pathways. We conclude that HDGF is a highly expressed vascular endothelial cell protein in vivo and is a potent endothelial mitogen and regulator of endothelial cell migration by mechanisms distinct from VEGF.

lung; angiogenesis; growth factors; cell migration


Address for reprint requests and other correspondence: A. D. Everett, Johns Hopkins Hospital, Pediatric Cardiology, Brady 5, 600 N. Wolfe St., Baltimore, MD 21287 (E-mail: aeveret3{at}jhmi.edu).




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