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Histidine‐rich glycoprotein binding to activated human platelets
Author(s) -
Lerch P. G.,
Nydegger U. E.,
Kuyas C.,
Haeberli A.
Publication year - 1988
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 - 10.1111/j.1365-2141.1988.tb02467.x
Subject(s) - platelet , thrombin , biochemistry , chemistry , glycoprotein , divalent , cytochalasin b , platelet activation , ligand (biochemistry) , microbiology and biotechnology , biology , receptor , cell , immunology , organic chemistry
Specific binding of purified histidine rich glycoprotein (HRGP) to human platelets stimulated with either bisdiazoniumbenzidine‐crosslinked immunoglobulin G (BDB‐IgG), with thrombin or with collagen was dose‐ and divalent cation dependent. A 5–10‐fold increase of platelet bound 125 I‐HRGP was obtained when 0.5–0.8 × 10 9 platelets/ml were activated with 100 μg BDB‐IgG/ml, 0.1 U thrombin/ml or 15 μg collagen/ml. At maximal binding tested 16000 molecules of HRGP became bound per platelet, but saturation was not achieved. Such platelet inhibitors as acetylsalicylic acid, prostaglandin E 1 and cytochalasin B reduced the capacity of platelets to bind ligand, and by kinetic experiments involving enzymatic digestion of radiolabelled bound HRGP the ligand revealed to remain surface bound rather than being taken up to inner parts of the cell.