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Am J Physiol Heart Circ Physiol 284: H1388-H1397, 2003. First published December 27, 2002; doi:10.1152/ajpheart.00414.2002
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Vol. 284, Issue 4, H1388-H1397, April 2003

Physiological concentration of atrial natriuretic peptide induces endothelial regeneration in vitro

Hyun Kook1, Hiroshi Itoh2, Bong Seok Choi1, Naoki Sawada2, Kentaro Doi2, Tae Ju Hwang1, Kyung Keun Kim1, Hiroshi Arai2, Yung Hong Baik1, and Kazuwa Nakao2

1 Research Institute of Medical Sciences, Chonnam National University Medical School, Gwangju 501-746, Republic of Korea; and 2 Department of Medicine and Clinical Science, Kyoto University Graduate School of Medicine, Kyoto 606-8507, Japan

Both nitric oxide (NO) and natriuretic peptides produce apoptosis of vascular smooth muscle cells. However, there is evidence that NO induces endothelial cell proliferation, which suggests that there is a difference in the response of endothelial cells to natriuretic peptides. The purpose of this study was to investigate the effect of atrial natriuretic peptide (ANP) on human endothelial cell survival. ANP within the physiological concentration (10-11 mol/l) induced a 52% increase in the number of human coronary arterial endothelial cells and a 63% increase in human umbilical vein endothelial cells at a low concentration of serum. The increase in cell numbers was blocked by pretreatment with RP8-CPT-cGMP (RP8), a cGMP-dependent protein kinase inhibitor, with wortmannin, an Akt/PKB inhibitor, and with PD-98059, an ERK1/2 inhibitor. In a Transwell migration test, ANP also increased the cell migration, and RP8, wortmannin, and PD-98059 blocked this increase. A wound healing assay was performed to examine the effects of ANP on regeneration in vitro. ANP increased both cell numbers and migration, but the effects were blocked by the above three kinase inhibitors. ANP increased the expression of phospho-Akt and of phospho-ERK1/2 within 1.5 h. These results suggest that ANP can potentiate endothelial regeneration by cGMP-dependent protein kinase stimulation and subsequent Akt and ERK1/2 activations.

cGMP-dependent protein kinase; Akt/protein kinase B; extracellular signal-regulated kinase 1/2


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