Aberrant Glycosylation of Lumican in Aortic Valve Stenosis Revealed by Proteomic Analysis

  • Suzuki Hirotoshi
    Department of Cardiovascular Surgery, St. Marianna University Graduate School of Medicine Department of Clinical Proteomics & Molecular Medicine, St. Marianna University Graduate School of Medicine
  • Chikada Masahide
    Department of Cardiovascular Surgery, St. Marianna University Graduate School of Medicine
  • Yokoyama Michiyo K.
    Department of Clinical Proteomics & Molecular Medicine, St. Marianna University Graduate School of Medicine
  • Kurokawa Manae S.
    Department of Disease Biomarker Analysis & Molecular Regulation, St. Marianna University Graduate School of Medicine
  • Ando Takashi
    Department of Cardiovascular Surgery, St. Marianna University Graduate School of Medicine
  • Furukawa Hiroshi
    Department of Cardiovascular Surgery, St. Marianna University Graduate School of Medicine
  • Arito Mitsumi
    Department of Clinical Proteomics & Molecular Medicine, St. Marianna University Graduate School of Medicine
  • Miyairi Takeshi
    Department of Cardiovascular Surgery, St. Marianna University Graduate School of Medicine
  • Kato Tomohiro
    Department of Clinical Proteomics & Molecular Medicine, St. Marianna University Graduate School of Medicine

この論文をさがす

説明

To identify proteins related to the pathophysiology of aortic valve stenosis (AS), we investigated the protein profiles of AS aortic valves. Specifically, proteins were extracted from a thickened and calcified area (AS-C) and an apparently non-thickened and non-calcified area (AS-N) in an identical aortic valve leaflet in each of 6 AS patients. The proteins were then separated by 2-dimensional gel electrophoresis (2DE). Protein spots detected by 2DE were compared between the AS-C and AS-N samples. Protein spots of interest were subjected to protein identification by mass spectrometry.<br>In total, 670 protein spots were detected by 2DE, 28 of which showed more than 1.5-fold different intensity (P < 0.05) between the AS-C and AS-N samples. Proteins were identified in 17 out of the 28 spots. Fibrinogen and lumican were identified in 9 and 3 spots, respectively. Intensity of these 12 spots was lower in the AS-C samples than in the AS-N samples. In the 1D-Western blot analysis, 4 lumican bands (80 kDa, 75 kDa, 65 kDa, and 53 kDa) were detected, of which 2 bands with 80 kDa and 75 kDa showed lower intensity in the AS-C samples than in the AS-N samples. When de-glycosylated protein samples were used in the 1D-Western blot, only a single lumican band with ~40 kDa was detected, indicating that lumican was variously glycosylated and that highly glycosylated lumican molecules were decreased in AS-C.<br>Collectively, insufficient glycosylation of lumican in the thickened and calcified areas of AS aortic valves may be involved in the pathophysiology of AS.

収録刊行物

  • International Heart Journal

    International Heart Journal 57 (1), 104-111, 2016

    一般社団法人 インターナショナル・ハート・ジャーナル刊行会

被引用文献 (3)*注記

もっと見る

参考文献 (27)*注記

もっと見る

関連プロジェクト

もっと見る

詳細情報 詳細情報について

問題の指摘

ページトップへ