| Autor: |
Kurushima H; Department of Medicine, University of California, San Diego, La Jolla 92093-0682, USA., Ramprasad M, Kondratenko N, Foster DM, Quehenberger O, Steinberg D |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of leukocyte biology [J Leukoc Biol] 2000 Jan; Vol. 67 (1), pp. 104-8. |
| DOI: |
10.1002/jlb.67.1.104 |
| Abstrakt: |
Macrosialin, the mouse homolog of human CD68, is a heavily glycosylated transmembrane protein found almost exclusively in macrophages. Its function remains uncertain. It has a high affinity for oxidized low-density lipoprotein (LDL) in ligand blots and antibodies against the human homolog, CD68, inhibit the binding of oxidized LDL to a human monocyte-derived cell line (THP-1). However, there is still controversy as to whether macrosialin, found predominantly in late endosomes, is expressed at all on the plasma membrane. The present studies, done in thioglycollate-elicited peritoneal macrophages, confirm that macrosialin is predominantly intracellular but show clearly that 10-15% of it is expressed on the cell surface. Exchange with intracellular pools occurs at an extremely high rate. The results are compatible with a surface function, including internalization of bound ligands or adhesion to surfaces. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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