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Deficiency of P62, a putative collagen receptor, in platelets from a patient with defective collagen‐induced platelet aggregation
Author(s) -
Ryo Ryukichi,
Yoshida Akinori,
Sugano Wataru,
Yasunaga Mutsumi,
Nakayama Katsuji,
Saigo Katsuyasu,
Adachi Masashi,
Yamaguchi Nobuo,
Okuma Minoru
Publication year - 1992
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830390107
Subject(s) - platelet , ristocetin , gpvi , chemistry , thrombin , collagen receptor , calcium , medicine , endocrinology , thrombospondin , adenosine diphosphate , coagulation , receptor , immunology , platelet activation , biochemistry , integrin , platelet aggregation , enzyme , metalloproteinase
Recently, we described a platelet antibody against a putative collagen receptor (P62), which was found in a patient with idiopathic thrombocytopenic purpura (ITP) (Blood 69:1712). We now report a deficiency of the P62 receptor in a young man whose platelets showed defective collagen‐induced platelet aggregation. He had a mild bleeding tendency and slight thrombocytopenia. The results of coagulation and fibrinolysis studies were normal. The patient's platelets were partially unresponsive to collagen, although aggregation in response to ADP, thrombin, ristocetin, and calcium ionophore (A23187) was almost normal. Adhesion of his platelets to bovine collagen was markedly reduced. Addition of collagen caused no synthesis of thromboxane (TX)B 2 , in platelet rich plasma (PRP) from this patient. Furthermore, collagen produced no rise of cytosolic free calcium ([Ca 2+ ]i) in fura2‐loaded platelets. In contrast, thrombin caused TXB 2 , formation and an increase of [Ca 2+ ]i in his platelets. These results suggest defective interaction between the platelets and collagen. The lgG from the ITP‐patient induced irreversible aggregation in normal PRP, but caused no aggregation of the young man's platelets. Immunoblot studies showed that normal platelets had antigens with a molecular weight of 62 KDa under reducing conditions and of 57 KDa under nonreducing conditions. In contrast, the young man's platelets had no P62 band, although GPla/lla and thrombospondin were normally present. These results indicate that impaired collagen‐induced aggregation in the patient's platelets was due to a deficiency of P62 and confirm that P62 may play a crucial role as a collagen receptor in platelet activation.