Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Human platelets possess receptors for a lymphokine: demonstration of high specific receptors for HuIFN-gamma

Journal Article · · J. Immunol.; (United States)
OSTI ID:6937421
This report demonstrates that /sup 125/I-recombinant human interferon-gamma (/sup 125/I-rHuIFN-gamma) binds to high-affinity specific receptors on human platelets. Scatchard analysis of binding data indicates the presence of homogeneous sites estimated in the order of 150 to 200, with an apparent equilibrium dissociation constant, Kd, of 2 X 10(-10) M. The binding of /sup 125/I-rHuIFN-gamma to platelet membrane was inhibited by unlabeled rHuIFN-gamma but not by unlabeled rHuIFN-alpha or unlabeled rHuIFN-beta. High affinity binding sites for HuIFN-alpha were not detectable. Cross-linking of /sup 125/I-rHuIFN-gamma to platelet membrane proteins with the use of a bifunctional agent (DSS) yielded a predominant complex of 100,000 +/- 5,000 daltons on SDS-PAGE autoradiography, which confirms the presence of specific receptors for IFN-gamma. Two faint bands of lower m.w., 70,000 and 90,000, could also be visualized. Cross-linking of /sup 125/I-rHuIFN-alpha to platelet surface could not be demonstrated by using the same procedures. This is the first time that a receptor for a lymphokine (IFN-gamma) has been demonstrated on human platelets. These findings are consistent with data already published, suggesting an interrelationship between IFN and platelet function.
Research Organization:
Institut Curie, Paris, France
OSTI ID:
6937421
Journal Information:
J. Immunol.; (United States), Journal Name: J. Immunol.; (United States) Vol. 3; ISSN JOIMA
Country of Publication:
United States
Language:
English