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High affinity interaction between histidine-rich glycoprotein and the cell surface type ATP synthase on T-cells
- Source :
-
BBA: Biomembranes . May2009, Vol. 1788 Issue 5, p1099-1107. 9p. - Publication Year :
- 2009
-
Abstract
- Abstract: Histidine-rich glycoprotein (HRG) is a plasma protein implicated in the innate immune system. In recent studies, we showed that either HRG, or the Arg23-Lys66 glycopeptide derived from HRG, in concert with concanavalin A (Con A), promotes a morphological change and adhesion of the human leukemic T-cell line MOLT-4 to culture dishes, and that cell surface glycosaminoglycan or Fcγ receptors do not participate in this cellular event. In the present study, we identified the α-subunit of ATP synthase as one of the HRG-binding proteins on the surface of T-cells by HRG-derived glycopeptide affinity chromatography and by a peptide mass finger printing method. HRG specifically interacted with mitochondrial ATP synthase with a dissociation constant of 66 nM. The presence of α- and β-subunits of ATP synthase on the plasma membrane of MOLT-4 cell was demonstrated by immunofluorescent staining and FACS analysis. The HRG/Con A-induced morphological changes of MOLT-4 cells were specifically inhibited by a monoclonal antibody against the β-subunit of ATP synthase. These results strongly suggest that the cell surface ATP synthase functions as a binding protein for HRG on MOLT-4 cells, which is required for the morphological changes observed in MOLT-4 cells following treatment with HRG/Con A. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 00052736
- Volume :
- 1788
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- BBA: Biomembranes
- Publication Type :
- Academic Journal
- Accession number :
- 38322107
- Full Text :
- https://doi.org/10.1016/j.bbamem.2009.03.005