| RRC ID |
6586
|
| Author |
Ohta T, Ikemoto Y, Usami A, Koide T, Wakabayashi S.
|
| Title |
High affinity interaction between histidine-rich glycoprotein and the cell surface type ATP synthase on T-cells.
|
| Journal |
Biochim Biophys Acta
|
| 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 Fcgamma receptors do not participate in this cellular event. In the present study, we identified the alpha-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 alpha- and beta-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 beta-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.
|
| Volume |
1788(5)
|
| Pages |
1099-107
|
| Published |
2009-5-1
|
| DOI |
10.1016/j.bbamem.2009.03.005
|
| PII |
S0005-2736(09)00078-9
|
| PMID |
19285951
|
| MeSH |
Amino Acid Sequence
Biophysical Phenomena
Cell Line
Cell Membrane / metabolism
Chromatography, Affinity
Humans
Mitochondria / enzymology
Molecular Sequence Data
Peptide Fragments / chemistry
Peptide Fragments / genetics
Peptide Fragments / metabolism
Peptide Mapping
Protein Binding
Protein Subunits
Proteins / chemistry
Proteins / genetics
Proteins / metabolism*
Proton-Translocating ATPases / chemistry
Proton-Translocating ATPases / genetics
Proton-Translocating ATPases / metabolism*
T-Lymphocytes / metabolism*
|
| IF |
3.411
|
| Times Cited |
13
|
|
WOS Category
|
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| Human and Animal Cells |
MOLT-4 |
