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Increased binding to ADP‐stimulated platelets and aggregation effect of the dysfibrinogen Oslo I as compared with normal fibrinogen
Author(s) -
Thorsen L. I.,
Brosstad F.,
Solum N. O.,
Stormorken H.
Publication year - 1986
Publication title -
scandinavian journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0036-553X
DOI - 10.1111/j.1600-0609.1986.tb00829.x
Subject(s) - fibrinogen , platelet , chemistry , fibrin , platelet aggregation , biochemistry , thrombin , cofactor , polymerization , biophysics , enzyme , medicine , immunology , organic chemistry , biology , polymer
Interactions of the dysfibrinogen Oslo I with platelets were investigated. This fibrinogen is a Bβ‐chain variant with faster than normal fibrin monomer polymerization. Fibrinogen Oslo I acted more efficiently in ADP‐induced platelet aggregation, and bound to gel‐filtered platelets with a higher affinity constant than did normal fibrinogen. At all concentrations more fibrinogen molecules became bound per platelet with the dysfibrinogen than with normal fibrinogen, both when the fibrinogens were tested separately or as a mixture using 125 I or 131 I to label the two types. At high concentrations this was probably due to ligand polymerization of the dysfibrinogen. These observations indicate that the increased cofactor function in platelet aggregation may be related to the increased affinity of the dysfibrinogen for the platelets.