@article{oai:nagasaki-u.repo.nii.ac.jp:00000915,
 author = {Okada, Masahiko and Tominaga, Norio and Honda, Goichi and Nishioka, Junji and Akita, Nobuyuki and Hayashi, Tatsuya and Suzuki, Koji and Moriuchi, Hiroyuki},
 issue = {12},
 journal = {Blood Advances},
 month = {Jun},
 note = {Thrombomodulin functions as an anticoagulant through thrombin binding and protein C activation. We herein report the first case of hereditary functional thrombomodulin deficiency presenting with recurrent subcutaneous hemorrhage and old cerebral infarction. The patient had a homozygous substitution of glycine by aspartate at amino acid residue 412 (Gly412Asp) in the thrombin-binding domain of the thrombomodulin gene (designated thrombomodulin-Nagasaki). In vitro assays using a recombinant thrombomodulin with the same mutation as the patient showed a total lack of thrombin binding and activation of protein C and thrombin-activatable fibrinolysis inhibitor (TAFI). Marked clinical and laboratory improvement was obtained with recombinant human soluble thrombomodulin therapy., Blood advances, 4(12), pp.2631-2639; 2020},
 pages = {2631--2639},
 title = {A case of thrombomodulin mutation causing defective thrombin binding with absence of protein C and TAFI activation},
 volume = {4},
 year = {2020}
}