| pubmed-article:2566603 | pubmed:abstractText | Histidine-rich glycoprotein (HRGP), a human plasma and platelet protein, interacts with multiple ligands in vitro, including heparin, plasminogen, thrombospondin, and fibrinogen/fibrin. In this study, the binding of HRGP to human T lymphocytes was characterized. The binding was specific, concentration-dependent, saturable, and reversible. Scatchard plot analysis revealed two classes of binding sites: the high affinity class had an apparent dissociation constant (Kd) of 1.92 X 10(-8) M, with 0.92 X 10(4) sites/cell, and the low affinity class had a Kd of 4.97 X 10(-7) M, with 3.7 X 10(4) sites/cell. HRGP binding to T cells in the presence of HRGP-depleted serum was comparable to that observed in buffer. Dot-blot analysis showed that HRGP bound to specific T cell proteins. Using both HRGP affinity chromatography and immunoprecipitation with affinity-purified anti-HRGP IgG, a major 56-kDa HRGP-binding protein in surface labeled T cell lysates was demonstrated. The 56-kDa protein was shown not to be related to the CD2 molecule on T cells. The binding characteristics of HRGP to T lymphocytes indicate a specific ligand-receptor interaction. This is the first demonstration of HRGP binding to a cell surface, and its binding to human T cells may play an important role in T lymphocyte biology. | lld:pubmed |
