Journal article
Effect of low-density lipoprotein on the expression of high affinity Fcγ receptors
Biochimica et biophysica acta. Molecular cell research, v 1011(2), pp 102-109
1989
PMID: 2523738
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
A substrain of the human monocyte-like cell line U937, which is a cholesterol auxotroph, was used to study the effect of cellular cholesterol depletion on the expression of the type I Fc receptor for IgG (FcγRI). Measurement of FcγRI expression was performed by immunofluorescence and flow cytometry using the monoclonal antibody (mAb) 32.2, which is specific for an epitope on FcγRI, and monomeric IgG
2a, which binds to the ligand binding site of FcγRI. Incubation of these cells for 24 h in growth medium containing delipidated fetal calf serum depletes cellular cholesterol without affecting growth or viability. While incubation of U937 cells with human interferon-γ (IFN-γ) increased FcγRI expression, cholesterol depletion after cell growth in media containing delipidated serum and IFN-γ resulted in reduced binding of both mAb 32.2 and IgG
2a. A significant decrease in the number of cell surface binding sites, as measured by mean fluorescence intensity, was observed after cholesterol depletion. Supplementation of the delipidated serum medium with pure cholesterol in an ethanol/bovine serum albumin mixture, which replenished cellular cholesterol and supported growth, failed to restore antibody binding significantly. In contrast, low-density lipoprotein (LDL) which also delivered cholesterol to the cells restored binding both in terms of the number of the reactive cells and cell surface receptor density. High-density lipoprotein (HDL
3), which does not deliver cholesterol to the cells, showed results similar to those obtained with pure cholesterol. This indicates that either LDL cholesterol is better utilized for membrane synthesis than pure cholesterol or that LDL provides another component, in addition to cholesterol, which is required for expression of FcγRI, but not for growth. These studies indicate a role for LDL in regulating the expression of FcγRI on the cell surface.
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Details
- Title
- Effect of low-density lipoprotein on the expression of high affinity Fcγ receptors
- Creators
- R.D. Bigler - Hahnemann University HospitalH.M. Brown - Hahnemann University HospitalP.M. Guyre - Dartmouth CollegeS. Lund-Katz - Drexel UniversityL. Scerbo - Hahnemann University HospitalM. Esfahani - Hahnemann University Hospital
- Publication Details
- Biochimica et biophysica acta. Molecular cell research, v 1011(2), pp 102-109
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1989U667200002
- Scopus ID
- 2-s2.0-0024541798
- Other Identifier
- 991019184045204721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics