Asymmetric Dimethylarginine, an Endogenous NOS Inhibitor, Is Actively Metabolized in Rat Erythrocytes

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  • YOKORO Miyuki
    Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University
  • SUZUKI Makiko
    Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University
  • MUROTA Kaeko
    Department of Life Science, School of Science and Engineering, Kinki University Department of Life Science, School of Science and Engineering, Kinki University
  • OTSUKA Chie
    Department of Biochemistry, Shujitsu University School of Pharmacy Department of Biochemistry, Shujitsu University School of Pharmacy
  • YAMASHITA Hiromi
    Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University
  • TAKAHASHI Yoshitaka
    Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University
  • TSUJI Hideaki
    Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University
  • KIMOTO Masumi
    Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University Department of Nutritional Science, Faculty of Health and Welfare Science, Okayama Prefectural University

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NG,NG-Dimethyl-L-arginine (asymmetric dimethylarginine: ADMA) is an endogenous competitive inhibitor of nitric oxide synthase (NOS). Plasma ADMA concentrations have been reported to increase in connection with diseases associated with an impaired endothelial L-arginine/NO pathway. In this study, we investigated the metabolism of ADMA in circulating blood cell populations to elucidate the regulatory mechanism of elevation of plasma ADMA, a novel risk factor for cardiovascular disease. We found by RT-PCR and Western blot analyses that protein arginine methyltransferase (PRMT)1 and dimethylarginine dimethylaminohydrolase (DDAH)-1, responsible for the biosynthesis and degradation of ADMA respectively, are expressed in erythrocytes (ECs), leukocytes, and platelets. We also identified a major ADMA-containing protein in ECs as catalase, confirmed by GST-pull down assay to bind to PRMT1 in vitro. This is the first report that the ADMA-metabolizing system, including the arginine methylation of proteins and the breakdown of free ADMA, occurs in circulating blood cell-populations, and that catalase in ECs might be a potential protein targeted by PRMT1.

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