Binding Specificity of Anti-Human Pancreatic Elastase 1 Autoantibodies and Conjugation Forms of Elastase 1 in Serum.

DOI
  • ASADA Hidehisa
    Research and Development, Diagnostic Science Department, Shionogi & Co., Ltd.
  • KONO Masao
    Research and Development, Diagnostic Science Department, Shionogi & Co., Ltd.
  • UCHIDA Kiyohisa
    Research and Development, Diagnostic Science Department, Shionogi & Co., Ltd.
  • FUNAKOSHI Akihiro
    National Kyushu Cancer Center

抄録

Anti-human pancreatic elastase 1 autoantibodies occurring in sera of patients with pancreatic diseases specifically bound elastase 1 but showed little binding with proelastase 1. Binding of proelastase 1 to the autoantibodies was effectively elevated by tryptic digestion of the proelastase 1 for activation, suggesting that the autoantibodies recognized some conformational change from proelastase 1 to elastase 1. Gel filtration analysis of the 125I-labeled elastase 1 and proelastase 1 added to sera revealed that both elastase 1 and proelastase 1 existed as conjugates with α1-antitrypsin or α2-macroglobulin in autoantibody-negative sera; but in autoantibody-positive sera, more than 80% of elastase 1 was assumed to form an immune complex with the autoantibodies, while proelastase 1 did not seem to form an immune complex, but existed as conjugates with the serum protease inhibitors as was the case of autoantibody-negative serum. Therefore, conversion of proelastase 1 into the active form does not seem to occur in serum. These results indicate that anti-elastase 1 autoantibodies are produced as a consequence of the leakage of unusually large amounts of elastase 1 into the circulation after an attack of pancreatitis.

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詳細情報 詳細情報について

  • CRID
    1390001204671068288
  • NII論文ID
    130003670290
  • DOI
    10.3164/jcbn.16.67
  • ISSN
    18805086
    09120009
  • 本文言語コード
    en
  • データソース種別
    • JaLC
    • Crossref
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

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