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Enhanced blood coagulation and fibrinolysis in mice lacking histidine‐rich glycoprotein (HRG)
Author(s) -
TSUCHIDASTRAETEN N.,
ENSSLEN S.,
SCHÄFER C.,
WÖLTJE M.,
DENECKE B.,
MOSER M.,
GRÄBER S.,
WAKABAYASHI S.,
KOIDE T.,
JAHNENDECHENT W.
Publication year - 2005
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1111/j.1538-7836.2005.01238.x
Subject(s) - glycoprotein , coagulation , hemostasis , biology , microbiology and biotechnology , immunology , medicine , chemistry
Summary. Histidine‐rich glycoprotein (HRG) is a serum protein belonging to the cystatin superfamily. HRG may play a regulatory role in hemostasis and innate immunity. However, this role is uncertain because of a lack of rigorous testing in an animal model. We generated mice lacking the translation start point of exon 1 of the Hrg gene, effectively resulting in a null mutation ( Hrg –/– ). The mice were viable and fertile but had no HRG in their blood. Antithrombin activity in the plasma of Hrg –/– mice was higher than in the plasma of heterozygous Hrg +/– or wild‐type Hrg +/+ mice. The prothrombin time was shorter in Hrg –/– mice than in Hrg +/– and Hrg +/+ mice. Bleeding time after tail tip amputation in Hrg –/– mice was shorter than in Hrg +/+ mice. The spontaneous fibrinolytic activity in clotted blood of Hrg –/– mice was higher than in Hrg +/+ mice. These findings suggest that HRG plays a role as both an anticoagulant and an antifibrinolytic modifier, and may regulate platelet function in vivo .