| RRC ID |
42895
|
| Author |
Matsunaga S, Xie Q, Kumano M, Niimi S, Sekizawa K, Sakakibara Y, Komba S, Machida S.
|
| Title |
Lectin-like oxidized low-density lipoprotein receptor (LOX-1) functions as an oligomer and oligomerization is dependent on receptor density.
|
| Journal |
Exp Cell Res
|
| Abstract |
Lectin-like oxidized low-density lipoprotein (LDL) receptor (LOX-1) exists as a homodimer formed by an intermolecular disulfide bond. Although the dimer is the minimum structural unit of LOX-1 on cell membranes, LOX-1 can form larger noncovalent oligomeric complexes. But, the functional unit of LOX-1 is not known. We quantitatively analyzed the correlation between cyan fluorescent protein-tagged LOX-1 expression and the fluorescence-labeled ligand (DiD-AcLDL) binding ability on each cell. The results clearly indicate that there is a threshold level of expression that enables LOX-1 to bind ligand. Above this threshold level, the ability of LOX-1 to bind ligand was proportional to its level of expression. Using the membrane impermeable crosslinker BS(3), we detected oligomers (primarily hexamers) only on the cell lines that stably expressed LOX-1 above the threshold level. In contrast, little oligomer or ligand binding was detected in cell lines expressing LOX-1 below the threshold level. Moreover, oligomerization was independent of ligand binding. These results indicate that the functional unit of LOX-1 is an oligomer and that oligomerization of LOX-1 is dependent on the receptor density on the plasma membrane.
|
| Volume |
313(6)
|
| Pages |
1203-14
|
| Published |
2007-4-1
|
| DOI |
10.1016/j.yexcr.2007.01.007
|
| PII |
S0014-4827(07)00021-3
|
| PMID |
17306253
|
| MeSH |
Animals
CHO Cells
Cell Membrane / metabolism*
Cricetinae
Cricetulus
Ligands
Protein Binding
Scavenger Receptors, Class E / metabolism*
Scavenger Receptors, Class E / physiology*
Transfection
|
| IF |
3.383
|
| Times Cited |
28
|
|
WOS Category
|
ONCOLOGY
CELL BIOLOGY
|
| Resource |
| Human and Animal Cells |
CHO |
