Binding of radioiodinated human von Willebrand factor to Bernard-Soulier, thrombasthenic and von Willebrand's disease platelets
| Autor: | J. H. Troll, John D. Olson, T. Funicella, S. S. Tang, D. M. Peterson, Joel L. Moake |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Adult
Male congenital hereditary and neonatal diseases and abnormalities medicine.medical_specialty Time Factors Adolescent Iodine Radioisotopes chemistry.chemical_compound Thrombasthenia Von Willebrand factor Von willebrand hemic and lymphatic diseases Internal medicine von Willebrand Factor medicine Humans Platelet Ristocetin Binding Sites biology Chemistry Syndrome Hematology Blood Coagulation Factors von Willebrand Diseases Agglutination (biology) Endocrinology Giant platelets Immunology biology.protein Female Blood Platelet Disorders sense organs circulatory and respiratory physiology |
| Zdroj: | Thrombosis Research. 19:21-27 |
| ISSN: | 0049-3848 |
| DOI: | 10.1016/0049-3848(80)90400-4 |
| Popis: | The ristocetin-induced binding of purified human 125 I-von Willebrand factor (vWF) polymers to formalinized and fresh washed giant platelets from three Bernard-Soulier syndrome (BSS) patients (two different families) was 0%, 1–2% and 7–18%, respectively, compared to normal platelets prepared at the same time, under the same conditions, and adjusted to the same final platelet counts. This abnormal 125 I-vWF binding was associated with absent BSS platelet agglutination in response to ristocetin and human vWF, and to bovine vWF alone (without ristocetin). Thus, it is defective attachment of exogenous vWF which prevents vWF-mediated agglutination of BSS platelets, rather than defective platelet-to-platelet contact subsequent to vWF-BSS platelet binding. In contrast to BSS platelets, there was normal to increased ristocetin-induced binding of 125 I-vWF to platelets prepared from two clinically normal heterozygous parents of BSS patients, two patients with thrombasthenia, and two individuals with von Willebrand's disease. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|