Autor: |
T Massamiri, P S Tobias, L K Curtiss |
Jazyk: |
angličtina |
Rok vydání: |
1997 |
Předmět: |
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Zdroj: |
Journal of Lipid Research, Vol 38, Iss 3, Pp 516-525 (1997) |
Druh dokumentu: |
article |
ISSN: |
0022-2275 |
DOI: |
10.1016/S0022-2275(20)37259-X |
Popis: |
The interaction of lipopolysaccharide binding protein (LBP) with apolipoprotein (apo)A-I on high density lipoproteins (HDL) was studied in solid phase ligand binding assays with a biotinylated LBP-specific antibody. The association was dependent on LBP concentration and enhanced in the presence of lipopolysaccharide (LPS). Maximal enhancement was measured at an LPS/LBP molar ratio of 6. To identify regions on apoA-I that participate directly or indirectly in the interaction between LBP and HDL, we attempted to inhibit LBP association with a panel of mapped apoA-I-specific monoclonal antibodies. Whereas some antibodies were effective inhibitors, others were not, even though they bound apoA-I. Furthermore, selected apoA-I synthetic peptides inhibited the antibody-mediated interference of the HDL/LBP interaction. Although no specific mechanism can be defined for the basis of the inhibitory effects of the antibodies on the association of LBP with HDL, we identified a role for three unique regions on apoA-I between residues 1-31, 95-164, and 178-200. These results suggested that apoA-I is a key component in the association of LBP with HDL and may play an important role in the biologic activity of LPS/LBP complexes. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
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