Premium
Dissociation between fibrinogen and fibrin interaction with platelets in patients with different subtypes of Glanzmann's thrombasthenia: studies in an ex vivo perfusion chamber model
Author(s) -
Hainaud Patricia,
Brouland JeanPhilippe,
André Patrick,
Simoneau Guy,
Bal dit Sollier Claire,
Drouet Ludovic,
Caen Jacques,
Bellucci Sylvia
Publication year - 2002
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1046/j.1365-2141.2002.03966.x
Subject(s) - fibrin , platelet , ex vivo , thrombasthenia , thrombus , fibrinogen , von willebrand factor , platelet adhesiveness , medicine , platelet membrane glycoprotein , pathology , immunology , chemistry , biochemistry , in vitro , platelet aggregation
Summary. To explore the possible role of a residual or variant α IIb β 3 integrin (α IIb β 3 ) in thrombogenesis, we used a new ex vivo perfusion chamber model to examine blood from patients with different subtypes of Glanzmann's thrombasthenia (GT). Non‐anticoagulated blood was perfused through capillaries coated with type III collagen for 4·5 min (shear rate: 1600/s). Platelet deposition was quantified as platelet adhesion and mean thrombus size volume; fibrin and von Willebrand Factor (VWF) were specifically revealed by immunohistochemistry. In two patients with variant and in one patient with type II GT, platelet adhesion was maximal and we observed an unexpected formation of thrombi that were smaller than normal in size. These thrombi were surrounded by a thick meshwork that displayed a strong staining for fibrin and VWF. In two patients with heterozygous GT, platelet adhesion and thrombogenesis were normal. In two patients with type I GT, there was no thrombus formation, although platelet adhesion was also maximal. These data suggest the existence of a substitute pathway for thrombogenesis mediated by fibrin and possibly α IIb β 3 (α IIb β 3 at a reduced level, as in type II, and/or abnormal) as this fibrin network was not observed in type I GT with no α IIb β 3 . These interactions might facilitate haemostasis and even lead to thrombosis under certain favourable conditions. Furthermore, these data might have pharmacological relevance to the development of anti‐α IIb β 3 antithrombotic agents.