2011
DOI: 10.1182/blood-2010-11-317099
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Activated protein C cofactor function of protein S: a novel role for a γ-carboxyglutamic acid residue

Abstract: 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, prot… Show more

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Cited by 38 publications
(74 citation statements)
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“…26,27 Only protein S Gla variants previously shown to bind normally to phospholipid membranes were evaluated for their TFPI cofactor function. 27,28 In addition, the cDNA for 3 previously described protein S/Gas6 chimeras were available.…”
Section: Generation and Expression Of Protein S Variantsmentioning
confidence: 99%
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“…26,27 Only protein S Gla variants previously shown to bind normally to phospholipid membranes were evaluated for their TFPI cofactor function. 27,28 In addition, the cDNA for 3 previously described protein S/Gas6 chimeras were available.…”
Section: Generation and Expression Of Protein S Variantsmentioning
confidence: 99%
“…26,27 Protein S purification and quantification WT protein S and protein S variants were either concentrated in conditioned medium or purified using barium citrate precipitation 29 followed by anionexchange chromatography as previously described. 27 Protein S concentrations of WT protein S and protein S single or composite variants (spanning Gla-TSR-EGF1-EGF2-EGF3-EGF4) were determined by a previously described in-house enzyme-linked immunosorbent assay (ELISA).…”
Section: Generation and Expression Of Protein S Variantsmentioning
confidence: 99%
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