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Activated protein C...
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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 ...
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American Society of Hematology,2011
Numbers
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LIBRIS-ID:oai:lup.lub.lu.se:f9b75e28-b537-41ed-bbbd-5a3f9623e519
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https://lup.lub.lu.se/record/2056814URI
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https://doi.org/10.1182/blood-2010-11-317099DOI
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Language:English
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Summary in:English
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Subject category:art swepub-publicationtype
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Subject category:ref swepub-contenttype
Notes
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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)
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Canis, Kevin
(author)
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Norström, EvaLund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups(Swepub:lu)klke-eno
(author)
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Yu, Yao
(author)
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Dahlbäck, BjörnLund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups(Swepub:lu)klke-bda
(author)
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Panico, Maria
(author)
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Morris, Howard R.
(author)
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Crawley, James T. B.
(author)
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Lane, David A.
(author)
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Klinisk kemi, MalmöForskargrupper vid Lunds universitet
(creator_code:org_t)
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In:Blood: American Society of Hematology117:24, s. 6685-66931528-00200006-4971
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Ahnström, Josefi ...
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Andersson, Helen ...
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Canis, Kevin
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Norström, Eva
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Yu, Yao
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Dahlbäck, Björn
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Panico, Maria
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Morris, Howard R ...
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Crawley, James T ...
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Lane, David A.
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