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Blood, 15 February 2002, Vol. 99, No. 4, pp. 1224-1229
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Adhesion of human platelets to serum amyloid A
Simcha Urieli-Shoval,
George Shubinsky,
Reinhold P. Linke,
Mati Fridkin,
Israel Tabi, and
Yaacov Matzner
From the Hematology Unit, Hadassah University Hospital,
Mount Scopus, Jerusalem, Israel; the Flow Cytometry Unit, Hematology
Laboratory and Institute of Hematology, Soroka University Medical
Center, Beer-Sheva, Israel; the Max-Planck-Institut für
Biochemie, Martinsried, Germany; and the Department of Organic
Chemistry, Weizmann Institute of Science, Rehovot, Israel.
Serum amyloid A (SAA) is an acute phase reactant, and its level in
the blood is elevated to 1000-fold in response of the body to trauma,
infection, inflammation, and neoplasia. SAA was reported to inhibit
platelet aggregation and to induce adhesion of leukocytes. This study
looked at adhesion of human platelets to SAA. Immobilized SAA supported
the adhesion of human washed platelets; level of adhesion to SAA was
comparable to fibronectin and lower than to fibrinogen. Adhesion to SAA
was further enhanced by Mn2+ and the physiological agonist,
thrombin. Platelet adhesion to SAA was completely abolished by anti-SAA
antibody. SAA-induced adhesion was inhibited by antibodies against the
integrin receptor  IIb 3, by the peptide GRGDSP and by SAA-derived
peptide containing YIGSR-like and RGD-like adhesion motifs (amino acids
29 to 42). Adhesion was not inhibited by control immunoglobulin G, by
antibody against the integrin receptor V3, by the peptide GRGESP,
and by SAA-derived peptide that includes incomplete RGD motif.
SAA-derived peptide 29 to 42 also inhibited platelet adhesion to
fibronectin. Transfected human melanoma cells expressing IIb3
adhered to SAA, whereas transfected cells expressing V3 did not.
By using flow cytometry, the IIb3 cells displayed significantly
higher levels of binding of soluble SAA than the V3 cells. These
data indicate that human platelets specifically adhere to SAA in an RGD- and IIb3-dependent manner. Thus, SAA may play a role in modulating platelet adhesion at vascular injury sites by sharing platelet receptors with other platelet-adhesive proteins.
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