[Frontiers in Bioscience S3, 655-661, January 1, 2011]

Regulation of protein expression by L-arginine in endothelial cells

Xiaoqing Lei1, Cuiping Feng2, Chuang Liu1, Guoyao Wu1,3,4, Cynthia J. Meininger4, Fenglai Wang1, Defa Li1, Junjun Wang1,3

1State Key Laboratory of Animal Nutrition, China Agricultural University, Beijing, China 100193, 2Department of Obstetrics and Gynecology, China-Japan Friendship Hospital, Beijing, China 100029, 3Department of Animal Science and Faculty of Nutrition, Texas A&M University, College Station, TX, 77843, 4Cardiovascular Research Institute, Texas A and M Health Science Center, Temple, TX, 76504

TABLE OF CONTENTS

1. Abstract
2. Introduction
3. Comparative proteome analysis of endothelial cells exposed to arginine
4. Conclusion and perspectives
5. Acknowledgements
6. References

1. ABSTRACT

L-Arginine is a conditionally essential amino acid for humans and plays an important role in the regulation of cardiovascular function and antioxidative defense. Previous studies have focused on the important role of L-arginine as a physiological precursor in the generation of nitric oxide and polyamines in endothelial cells (cells that line the interior surface of blood vessels). Because of the rapid development of high-throughput proteomics technology, there is now growing interest in studying roles for L-arginine in modulating endothelial-cell protein expression. Of particular interest, recent proteomics analysis has shown that treatment of coronary venular endothelial cells with a physiological level of L-arginine (e.g., 0.1 mM) increases expression of structural proteins (vimentin and tropomyosin) and cytochrome bc1 complex iii-chain A, while decreasing expression of stress-related proteins (PDZ domain containing-3), in these cells. These findings aid in elucidating the mechanisms responsible for the beneficial effect of physiological levels of L-arginine on the circulatory system.