The Compact and Biologically Relevant Structure of Inter-α-inhibitor Is Maintained by the Chondroitin Sulfate Chain and Divalent Cations.

@article{Scavenius2016TheCA,
  title={The Compact and Biologically Relevant Structure of Inter-α-inhibitor Is Maintained by the Chondroitin Sulfate Chain and Divalent Cations.},
  author={Carsten Scavenius and Camilla Lund Nikolajsen and Marcel R Stenvang and Ida Bukh Th\ogersen and Łukasz Wyrożemski and H G Wisniewski and Daniel E Otzen and Kristian Wejse Sanggaard and Jan J Enghild},
  journal={The Journal of biological chemistry},
  year={2016},
  volume={291 9},
  pages={4658-70}
}
Inter-α-inhibitor is a proteoglycan of unique structure. The protein consists of three subunits, heavy chain 1, heavy chain 2, and bikunin covalently joined by a chondroitin sulfate chain originating at Ser-10 of bikunin. Inter-α-inhibitor interacts with an inflammation-associated protein, tumor necrosis factor-inducible gene 6 protein, in the extracellular matrix. This interaction leads to transfer of the heavy chains from the chondroitin sulfate of inter-α-inhibitor to hyaluronan and… CONTINUE READING