Binding Characteristics of Human Lactoferrin to the Human Monocytic Leukemia Cell Line THP-1 Differentiated into macrophages

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概要

• 論文の詳細を見る

• The characteristics of the binding of human lactoferrin (LF) to the cells of a human monocytic leukemia cell line, THP-1,were investigated. ^<125>I-Labeled LF (^<125>I-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 ^<125>I-LF to THP-1 macrophages indicated that high and low affinity receptor sites (K_d=0.57×10^<-6> and 3.7×10^<-6>M, respectively) are present on the cells. The number of these high and low affinity receptor sites were 2.4×10^6,and 2.5×10^6 per cell, respectively. Removal of iron from ^<125>I-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, and analogous structure being present in the poly-N-acetyllactosaminyl chains of LF, also partially inhibited the binding of ^<125>I-LF to the THP-1 macrophages. When poly-N-acetyllactosaminyl saccharide chains of ^<125>I-LF were cleaved by endo β-galactosidase, the binding of ^<125>I-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 Galβ1-4GlcNAcβ1-3Gal, 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.

• 社団法人日本薬学会の論文
• 1996-02-15

著者

• 別府 正敏

  東京薬大 公衆衛生学

• 別府 正敏

  東京薬科大学

• 別府 正敏

  東京医科大学 小児科学

• EDA Shigetoshi

  School of Pharmacy, Tokyo University of Pharmacy and Life Science

• KIKUGAWA Kiyomi

  School of Pharmacy, Tokyo University of Pharmacy and Life Science

• BEPPU Masatoshi

  School of Pharmacy, Tokyo University of Pharmacy and Life Science

• Eda Shigetoshi

  School Of Pharmacy Tokyo University Of Pharmacy And Life Science

• 菊川 清見

  東薬大・薬・衛生化学

• Beppu M

  Tokyo College Of Pharmacy

• Beppu Masatoshi

  School Of Pharmacy Tokyo University Of Pharmacy And Life Sciences

• Beppu Masatoshi

  School Of Pharmacy Tokyo Univ. Of Pharmacy And Life Sciences

• Kikugawa Kiyomi

  School Of Pharmacy Tokyo University Of Pharmacy And Life Science

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