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Am J Physiol Lung Cell Mol Physiol 277: L794-L801, 1999;
1040-0605/99 $5.00
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Vol. 277, Issue 4, L794-L801, October 1999

Increased expression of calreticulin is linked to ANG IV-mediated activation of lung endothelial NOS

Jawaharlal M. Patel1,2, Yong D. Li2, Jianliang Zhang2, Craig H. Gelband3, Mohan K. Raizada3, and Edward R. Block1,2

1 Research Service, Malcom Randall Department of Veterans Affairs Medical Center, and Departments of 2 Medicine and 3 Physiology, University of Florida College of Medicine, Gainesville, Florida 32608

This study demonstrates that ANG IV-induced activation of lung endothelial cell nitric oxide synthase (ecNOS) is mediated through mobilization of Ca2+ concentration and by increased expression and release of the Ca2+ binding protein calreticulin in pulmonary artery endothelial cells (PAEC). In Ca2+-free medium and in the presence of the ANG II AT1 and AT2 receptor antagonists losartan and PD-123319 (1 µM each), respectively, ANG IV (5, 50, and 500 nM) significantly increased intracellular Ca2+ release in PAEC (P < 0.05 for all concentrations). In contrast, ANG IV-mediated activation of ecNOS was abolished by the intracellular Ca2+ chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid-AM. ANG IV stimulation resulted in significantly increased expression of calreticulin in cells as well as release of calreticulin into the medium of cells as early as 2 h after ANG IV stimulation (P < 0.05). Catalytic activity of purified ecNOS in the absence of calmodulin was increased in a concentration-dependent fashion by calreticulin. Immunocoprecipitation studies revealed that ecNOS and calreticulin were coprecipitated in ANG IV-stimulated PAEC. These results demonstrate that ANG IV-mediated activation of ecNOS is regulated by intracellular Ca2+ mobilization and by increased expression of calreticulin, which appears to involve interaction of ecNOS and calreticulin proteins in PAEC.

endothelial cell nitric oxide synthase; calcium; angiotensin IV; protein interaction; protein synthesis; protein-protein interaction


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