Actions of Anti-insulin Serum on the Interactions of Insulin with Human Liver Membranes

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  • Sasaki Takashi
    The Second Department of Medicine, Hokkaido University School of Medicine
  • Komori Katsutoshi
    The Second Department of Medicine, Hokkaido University School of Medicine
  • Nakayama Hidetaka
    The Second Department of Medicine, Hokkaido University School of Medicine
  • Nakagawa Shoichi
    The Second Department of Medicine, Hokkaido University School of Medicine

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Other Title
  • ヒト肝細胞膜のインスリン結合に及ぼすインスリン抗体の作用
  • ヒト カン サイボウ マク ノ インスリン ケツゴウ ニ オヨボス インスリン

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Abstract

The actions of porcine insulin antiserum on the interactions of insulin with human liver membranes were investigated. When 125I-insulin was preincubated with anti-insulin serum, the insulin binding was decreased in relation to the concentration of antiserum. The 125I-insulin binding to liver membranes in the presence of serum from insulin-treated patients, had an inverse relationship with the 125I-insulin binding to patient serum (r=0.93, p<0.05).<BR>Scatchard plot analysis of the 125I-insulin binding data revealed no change in affinity in the binding data in the presence of antiinsulin serum, but there was a decrease in total binding capacity (high affinity plus low affinity). Anti-insulin serum accelerated the dissociation of insulin from liver membranes as compared to the control (p<0.05), and 98.5% of the dissociated insulin was found to rebind to anti-insulin serum. Similarly, 125I-insulin dissociated from anti-insulin serum rebound to liver membranes.<BR>The above results suggest that in vivo insulin bound to insulin antibodies does not bind to insulin receptor, and that insulin antibodies accelerate the dissociation of insulin from the receptor.

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