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Binding of Amadori glucose-modified albumin by the monocytic cell line MonoMac 6 activates protein kinase Cε protein tyrosine kinases and the transcription factors AP-1 and NF-κB

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Abstract

An affinity purification procedure is employed for the isolation of FL-specific binding proteins from MM6 cell membranes using magnetobeads coated with glycated polylysine and elution with FL and glycated 6-aminocaproic acid. Two main binding proteins were identified as membrane-bound nucleolin and cellular myosin heavy chain, which are glycosylated. This study shows that in these cells binding of short-term glycated albumin leads to activation of PKC, especially its isoform ε and this is linked to translocation of AP-1 and NF-κB into the nucleus. Consequently, an increased formation of IL-1ß mRNA is observed. The PKC inhibitor GÖ6976 prevents all these effects. Glycated albumin also stimulates activation of PTK. The PTK inhibitor genistein prevents activation of AP-1 indicating that PTK is also involved in this process, whereas NF-κB translocation is only dependent on PKC activation.

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Authors and Affiliations

  1. Institute of Medical Biochemistry and Molecular Biology, Ernst Moritz Arndt University, Greifswald, Germany

    Ramona Salazar & Rowena Brandt

  2. Institute of Medical Biochemistry and Molecular Biology, Ernst Moritz Arndt University, Greifswald, Germany

    Sven Krantz

Authors
  1. Ramona Salazar
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  2. Rowena Brandt
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  3. Sven Krantz
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Salazar, R., Brandt, R. & Krantz, S. Binding of Amadori glucose-modified albumin by the monocytic cell line MonoMac 6 activates protein kinase Cε protein tyrosine kinases and the transcription factors AP-1 and NF-κB. Glycoconj J 18, 769–777 (2001). https://doi.org/10.1023/A:1021151417556

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  • DOI: https://doi.org/10.1023/A:1021151417556

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