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@ARTICLE{Mhlis:642769,
      author       = {Möhlis, Kevin and Useini, Abibe and Betat, Heike and
                      Bonin, Sonja and Broghammer, Helen and Nuwayhid, Rima and
                      Langer, Stefan and Mörl, Mario and Sträter, Norbert and
                      Heiker, John T.},
      title        = {{V}aspin identified as a {DNA} ‐binding serpin with
                      functional consequences for protease inhibition},
      journal      = {The FEBS journal},
      volume       = {NN},
      issn         = {0014-2956},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {PUBDB-2025-05618},
      pages        = {NN},
      year         = {2025},
      note         = {OnlineFirst VDB},
      abstract     = {Vaspin is highly expressed not only in the skin but also in
                      the liver and adipose tissue. It counteracts inflammation
                      and oxidative stress in inflammatory skin diseases, obesity,
                      and associated metabolic disorders, in part by inhibiting
                      the kallikrein proteases KLK7 and KLK14. Vaspin binds the
                      cell-surface low-density lipoprotein receptor-related
                      protein 1 (LRP1) with nanomolar affinity, and is rapidly
                      internalized into adipocytes and other cells. We found
                      intracellular vaspin partially localized in the nucleus.
                      Since vaspin binds heparin and inorganic polyphosphates, we
                      investigated the DNA binding of vaspin. Using DNA-affinity
                      chromatography and differential radial capillary action of
                      ligand assays, we found high-affinity binding to random
                      sequences of single- and double-stranded DNA for both vaspin
                      and KLK7. Furthermore, KLK7 inhibition was accelerated
                      fivefold in the presence of DNA molecules at least 40 bases
                      in length. We previously identified the heparin-binding site
                      at a basic patch on the central beta-sheet A of vaspin. In
                      the current work, we determined the crystal structure of
                      polyphosphate P45-bound vaspin, which confirmed previously
                      identified residues mutated to generate a nonheparin-binding
                      (NHB) vaspin variant. While NHB vaspin failed to bind
                      heparin and polyP45, it still bound DNA with high affinity
                      and accelerated protease inhibition. Mutation of closely
                      spaced basic residues in helix A and helix G did not
                      significantly alter DNA binding. In conclusion, we have
                      identified vaspin as the second human DNA-binding serpin.
                      While the exact mode of the nonspecific interaction remains
                      unclear, it accelerates protease inhibition and likely
                      contributes to the nuclear localization observed for
                      internalized vaspin and may allow for intracellular
                      effects.},
      cin          = {EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / SFB 1052 C07 -
                      Molekulare Mechanismen der Vaspin-KLK7 Achse bei Adipositas
                      und Diabetes (C07) (250084214) / SFB 1052 Z06 -
                      Identifizierung und molekulare Charakterisierung von
                      potentiellen Adipositas-Pharmakotherapien (Z06*)
                      (465387892)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)250084214 /
                      G:(GEPRIS)465387892},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1111/febs.70270},
      url          = {https://bib-pubdb1.desy.de/record/642769},
}