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Binding characteristics of human lactoferrin to the human monocytic leukemia cell line THP-1 differentiated into macrophages.

Abstract：

:The characteristics of the binding of human lactoferrin (LF) to the cells of a human monocytic leukemia cell line, THP-1, were investigated. 125I-Labeled LF (125I-LF) bound to THP-1 cells, and the binding increased markedly as the cells matured into macrophages (THP-1 macrophages) by stimulation with phorbol 12-myristate 13-acetate. Scatchard analysis of the binding of 125I-LF to THP-1 macrophages indicated that high and low affinity receptor sites (Kd = 0.57 x 10(-6) and 3.7 x 10(-6) M, respectively) are present on the cells. The number of these high and low affinity receptor sites were 2.4 x 10(6), and 2.5 x 10(6) per cell, respectively. Removal of iron from 125I-LF did not affect its binding to THP-1 macrophages, indicating that the binding is not dependent on Fe(III) ion. The binding of the labeled LF to THP-1 macrophages was markedly decreased following acetylation, suggesting that the amino residues of the polypeptide portion of LF play a major role in the binding. The binding of labeled LF was partially inhibited by the isolated whole oligosaccharides of LF, and by the isolated whole oligosaccharides of band 3 glycoprotein of human erythrocyte membrane which contain poly-N-acetyllactosaminyl saccharide chains, like the LF oligosaccharides. Their inhibitory activity did not depend on the terminal sialyl residues of the saccharide chains. Lacto-N-fucopentaose III and lacto-N-neotetraose, an analogous structure being present in the poly-N-acetyllactosaminyl chains of LF, also artially inhibited the binding of 125I-LF to the THP-1 macrophages. When poly-N-acetyllactosaminyl saccharide chains of 125I-LF were cleaved by endo beta-galactosidase, the binding of 125I-LF was partially reduced. These results suggest that binding of LF to THP-1 macrophages is primarily mediated by its protein component, but a short oligosaccharide structure, possibly Gal beta 1-4GlcNAc beta 1-3Gal, which is contained in the nonreducing terminal region of poly-N-acetyllactosaminyl saccharide chains of LF and band 3, and in lacto-N-fucopentaose III and lacto-N-neotetraose is also recognized by THP-1 macrophages, and this recognition partly contributes to the binding of LF to cells.

journal_name

Biol Pharm Bull

journal_title

Biological & pharmaceutical bulletin

authors

Eda S,Kikugawa K,Beppu M

doi

10.1248/bpb.19.167

subject

Has Abstract

pub_date

1996-02-01 00:00:00

pages

167-75

issue

eissn

0918-6158

issn

1347-5215

journal_volume

pub_type

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Binding characteristics of human lactoferrin to the human monocytic leukemia cell line THP-1 differentiated into macrophages.