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  • Ahnström, JosefinLund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups (author)

Activated protein C cofactor function of protein S: a novel role for a gamma-carboxyglutamic acid residue

  • Article/chapterEnglish2011

Publisher, publication year, extent ...

  • American Society of Hematology,2011

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  • LIBRIS-ID:oai:lup.lub.lu.se:f9b75e28-b537-41ed-bbbd-5a3f9623e519
  • https://lup.lub.lu.se/record/2056814URI
  • https://doi.org/10.1182/blood-2010-11-317099DOI

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  • Language:English
  • Summary in:English

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  • Subject category:art swepub-publicationtype
  • Subject category:ref swepub-contenttype

Notes

  • Protein S has an important anticoagulant function by acting as a cofactor for activated protein C (APC). We recently reported that the EGF1 domain residue Asp95 is critical for APC cofactor function. In the present study, we examined whether additional interaction sites within the Gla domain of protein S might contribute to its APC cofactor function. We examined 4 residues, composing the previously reported "Face1" (N33S/P35T/E36A/Y39V) variant, as single point substitutions. Of these protein S variants, protein S E36A was found to be almost completely inactive using calibrated automated thrombography. In factor Va inactivation assays, protein S E36A had 89% reduced cofactor activity compared with wild-type protein S and was almost completely inactive in factor VIIIa inactivation; phospholipid binding was, however, normal. Glu36 lies outside the omega-loop that mediates Ca2+-dependent phospholipid binding. Using mass spectrometry, it was nevertheless confirmed that Glu36 is gamma-carboxylated. Our finding that Gla36 is important for APC cofactor function, but not for phospholipid binding, defines a novel function (other than Ca2+ coordination/phospholipid binding) for a Gla residue in vitamin K-dependent proteins. It also suggests that residues within the Gla and EGF1 domains of protein S act cooperatively for its APC cofactor function. (Blood. 2011;117(24):6685-6693)

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  • Andersson, Helena (author)
  • Canis, Kevin (author)
  • Norström, EvaLund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups(Swepub:lu)klke-eno (author)
  • Yu, Yao (author)
  • Dahlbäck, BjörnLund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups(Swepub:lu)klke-bda (author)
  • Panico, Maria (author)
  • Morris, Howard R. (author)
  • Crawley, James T. B. (author)
  • Lane, David A. (author)
  • Klinisk kemi, MalmöForskargrupper vid Lunds universitet (creator_code:org_t)

Related titles

  • In:Blood: American Society of Hematology117:24, s. 6685-66931528-00200006-4971

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