Minimally modified low density lipoprotein induces monocyte chemotactic protein 1 in human endothelial cells and smooth muscle cells
| Autor: | Alan M. Fogelman, Susan D. Cushing, Mary C. Territo, Farhad Parhami, Judith A. Berliner, Colin J. Schwartz, M Navab, Anthony J. Valente, Ross G. Gerrity |
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| Rok vydání: | 1990 |
| Předmět: |
Endothelium
Transcription Genetic Cell Molecular Sequence Data Biology In Vitro Techniques Sulfur Radioisotopes Monocytes Muscle Smooth Vascular chemistry.chemical_compound Methionine medicine Humans RNA Messenger Aorta Cells Cultured Chemokine CCL2 Multidisciplinary Base Sequence Chemotactic Factors Monocyte Biological activity Chemotaxis DNA Blotting Northern Molecular biology In vitro Lipoproteins LDL Chemotaxis Leukocyte medicine.anatomical_structure chemistry Biochemistry Cell culture Low-density lipoprotein RNA Endothelium Vascular Oligonucleotide Probes Oxidation-Reduction Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 87(13) |
| ISSN: | 0027-8424 |
| Popis: | After exposure to low density lipoprotein (LDL) that had been minimally modified by oxidation (MM-LDL), human endothelial cells (EC) and smooth muscle cells (SMC) cultured separately or together produced 2- to 3-fold more monocyte chemotactic activity than did control cells or cells exposed to freshly isolated LDL. This increase in monocyte chemotactic activity was paralleled by increases in mRNA levels for a monocyte chemotactic protein 1 (MCP-1) that is constitutively produced by the human glioma U-105MG cell line. Antibody that had been prepared against cultured baboon smooth muscle cell chemotactic factor (anti-SMCF) did not inhibit monocyte migration induced by the potent bacterial chemotactic factor f-Met-Leu-Phe. However, anti-SMCF completely inhibited the monocyte chemotactic activity found in the media of U-105MG cells, EC, and SMC before and after exposure to MM-LDL. Moreover, monocyte migration into the subendothelial space of a coculture of EC and SMC that had been exposed to MM-LDL was completely inhibited by anti-SMCF. Anti-SMCF specifically immunoprecipitated 10-kDa and 12.5-kDa proteins from EC. Incorporation of [35S]methionine into the immunoprecipitated proteins paralleled the monocyte chemotactic activity found in the medium of MM-LDL stimulated EC and the levels of MCP-1 mRNA found in the EC. We conclude that (i) SMCF is in fact MCP-1 and (ii) MCP-1 is induced by MM-LDL. |
| Databáze: | OpenAIRE |
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