Journal article
Lipoproteins upregulate high affinity FC receptors in human monocytes
Biochemical and biophysical research communications, v 191(2), pp 610-616
1993
PMID: 8461017
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Plasma lipoproteins have been implicated in immunoregulation. Here we report that LDL and VLDL up-regulate high affinity Fc receptors (FcγRI) in normal human monocytes. Adherent monocytes were cultured for 4 days in media containing fetal calf serum or delipidated serum. Immunofluorescence analysis showed a significant decrease in percentage of FcγRI-positive cells from 85 ± 3 in medium containing normal serum to 54 ± 9 in medium containing delipidated serum. The decrease in the fraction of cells expressing FcγRI was parallel to a decrease in the average number of receptor molecules per cell as indicated by a decrease in the mean value fluorescence intensity from 234 ± 20 to 112 ± 14. The inhibition of FcγRI expression was overcome by addition to the culture medium of LDL or VLDL. Since pure cholesterol is ineffective, it is proposed that these lipoproteins deliver a component(s) such as apolipoprotein B-100 which triggers a signal leading to up-regulation of FcγRI in monocytes and macrophages.
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Details
- Title
- Lipoproteins upregulate high affinity FC receptors in human monocytes
- Creators
- M Esfahani - Drexel University, Biochemistry/Biological Chemistry [Historical]R. D Bigler - Drexel University, Biochemistry/Biological Chemistry [Historical]J. L Alfieri - Drexel University, Biochemistry/Biological Chemistry [Historical]E Gressen - Drexel University, Biochemistry/Biological Chemistry [Historical]S LUND-KATZ - Drexel University, Biochemistry/Biological Chemistry [Historical]L Scerbo - Drexel University, Biochemistry/Biological Chemistry [Historical]
- Publication Details
- Biochemical and biophysical research communications, v 191(2), pp 610-616
- Publisher
- Elsevier
- Number of pages
- 7
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry/Biological Chemistry [Historical]; College of Medicine; Chemistry
- Web of Science ID
- WOS:A1993KT12800042
- Scopus ID
- 2-s2.0-0027185915
- Other Identifier
- 991019183966204721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics