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

DOI Web Site Web Site PubMed 被引用文献2件 参考文献100件
  • 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

この論文をさがす

説明

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.

収録刊行物

被引用文献 (2)*注記

もっと見る

参考文献 (100)*注記

もっと見る

関連プロジェクト

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ