PubMed · 8415799
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G J Miller. 1993. Hyperlipidaemia and hypercoagulability.. https://doi.org/10.1016/0163-7827(93)90005-h
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PURPOSE: To determine the influence of body weight on the international normalized ratio (INR) response to a fixed dose of vitamin K in overanticoagulated patients. METHODS: Retrospective review of records of patients who received 1 mg of vitamin K subcutaneously to correct excessive INR. Dose of vitamin K in milligrams per kilograms plotted against change in INR in 24 hours. RESULTS: Fifteen patients were identified who met all inclusion criteria. Linear regression analysis plotted INR response at 24 hours versus dose of vitamin K adjusted for body weight. Pearson's product moment correlation (R = 0.85) indicated a significant relationship between INR response at 24 hours to an adjusted body weight dose of subcutaneous vitamin K (P = 0.0000523). A strong correlation (r = 0.69) also existed between INR response at 24 hours and the actual body weight dose of subcutaneous vitamin K (P = 0.004). CONCLUSIONS: In overanticoagulated patients, variability in response to vitamin K may be explained by variability in body weight. Dosing vitamin K according to body weight may result in a more predictable INR response.
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Human coagulation factor XI (FXI) is a plasma serine protease composed of 2 identical 80-kd polypeptides connected by a disulfide bond. This dimeric structure is unique among blood coagulation enzymes. The hypothesis was tested that dimeric conformation is required for normal FXI function by generating a monomeric version of FXI (FXI/PKA4) and comparing it to wild-type FXI in assays requiring factor IX activation by activated FXI (FXIa). FXI/PKA4 was made by replacing the FXI A4 domain with the A4 domain from prekallikrein (PK). A dimeric version of FXI/PKA4 (FXI/PKA4-Gly326) was prepared as a control. Activated FXI/PKA4 and FXI/PKA4-Gly326 activate factor IX with kinetic parameters similar to those of FXIa. In kaolin-triggered plasma clotting assays containing purified phospholipid, FXI/PKA4 and FXI/PKA4-Gly326 have coagulant activity similar to FXI. The surface of activated platelets is likely to be a physiologic site for reactions involving FXI/FXIa. In competition binding assays FXI/PKA4, FXI/PKA4-Gly326, and FXI have similar affinities for activated platelets (K(i) = 12-16 nM). In clotting assays in which phospholipid is replaced by activated platelets, the dimeric proteins FXI and FXI/PKA4-Gly326 promote coagulation similarly; however, monomeric FXI/PKA4 has greatly reduced activity. Western immunoblot analysis confirmed that activated monomeric FXI/PKA4 activates factor IX poorly in the presence of activated platelets. These findings demonstrate the importance of the dimeric state to FXI activity and suggest a novel model for factor IX activation in which FXIa binds to activated platelets by one chain of the dimer, while binding to factor IX through the other.