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Cardiovascular Research 2002 55(2):225-228; doi:10.1016/S0008-6363(02)00465-0
© 2002 by European Society of Cardiology
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Copyright © 2002, European Society of Cardiology

Response to: endomyocardial nitric oxide synthase and the hemodynamic phenotypes of human dilated cardiomyopathy and of athlete's heart

Jamie T Stark, David J Schaeffer and David R Gross*

Department of Veterinary Biosciences, College of Veterinary Medicine, University of Illinois, Urbana–Champaign, 3516 VMBS Bldg., 2001 S. Lincoln Ave., Urbana, IL 61802, USA

* Corresponding author. Tel.: +1-217-333-2506; fax: +1-217-244-1652 dgross@cvm.uiuc.edu

Received 7 May 2002; accepted 7 May 2002

The first 150 words of the full text of this article appear below.

See article by Bronzwaer et al. [15] (pages 270–278) in this issue.

The nitric oxide synthase (NOS) family of enzymes consists of three protein products from three distinct genes that catalyze the conversion of L-citrulline to L-arginine in the presence of NADPH and O2 yielding the diffusible free radical gas NO. The current viewpoint is that two of these genes NOS1 (nNOS) and NOS3 (eNOS) are constitutively expressed while NOS2 (iNOS) is readily inducible. In addition, the neuronal (nNOS) and endothelial (eNOS) proteins contain flexible calmodulin binding domains making these low-output enzymes sensitive to Ca2+ activation. Conversely, the inducible (iNOS) protein binds calmodulin tightly, making this enzyme Ca2+ insensitive. However, this protein is readily induced by numerous cytokines (IL-1β, TNF{alpha}, IFN{gamma}, IL-6) as well as lipopolysaccharide (LPS) [1]. NOS1 and NOS3, by nature of their calcium sensitive, transient activity, mediate cell signaling events associated with . . . [Full Text of this Article]


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