Abstract
A family of β-galactoside-binding animal lectins has recently been designated as galectins. One member of this family, galectin-3, has been known as εBP for its IgE-binding activity and as Mac-2, a macrophage surface antigen, CBP35, CBP30, L-29, and L-34. Although much information has accumulated on the expression of this lectin in murine macrophages and human monocytic cell lines, little is known about the expression and function of this protein in normal human monocytes/macrophages. We now report that galectin-3 is expressed in normal human peripheral blood monocytes and its level increases dramatically as human monocytes differentiate into macrophages upon culturing in vitro. Immunoblot analysis showed that there was a 5-fold increase in the level of galectin-3 after 1 day of culture and greater than a 12-fold increase after 5 days. Immunocytochemical analysis confirmed this progressive increase of galectin-3 expression in cultured monocytes. Immunogold cytochemistry/electron microscopy analysis revealed that galectin-3 was expressed on the surface of human monocytes and that tire level of cell surface galectin-3 increased progressively as these cells differentiated into macrophages. The level of galectin-3 in human monocytes/macrophages was modulated by stimuli such as lipopolysaccharide and interferon-γ, and galectin-3 was secreted when monocytes were stimulated by calcium ionophore A23187. Soluble galectin-3 caused superoxide release front human monocytes; this activity was dependent on the lectin property of galectin-3, as it was inhibitable by lactose. Thus, galectin-3 may modulate the function of this cell type in an autocrine or paracrine fashion through binding to cell surface glycoconjugates.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1016-1028 |
| Number of pages | 13 |
| Journal | American Journal of Pathology |
| Volume | 147 |
| Issue number | 4 |
| State | Published - 1995 |
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ASJC Scopus subject areas
- Pathology and Forensic Medicine
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Expression and function of galectin-3, a β-galactoside-binding lectin, in human monocytes and macrophages. / Liu, Fu-Tong; Hsu, D. K.; Zuberi, R. I.; Kuwabara, I.; Chi, E. Y.; Henderson, W. R.
In: American Journal of Pathology, Vol. 147, No. 4, 1995, p. 1016-1028.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Expression and function of galectin-3, a β-galactoside-binding lectin, in human monocytes and macrophages
AU - Liu, Fu-Tong
AU - Hsu, D. K.
AU - Zuberi, R. I.
AU - Kuwabara, I.
AU - Chi, E. Y.
AU - Henderson, W. R.
PY - 1995
Y1 - 1995
N2 - A family of β-galactoside-binding animal lectins has recently been designated as galectins. One member of this family, galectin-3, has been known as εBP for its IgE-binding activity and as Mac-2, a macrophage surface antigen, CBP35, CBP30, L-29, and L-34. Although much information has accumulated on the expression of this lectin in murine macrophages and human monocytic cell lines, little is known about the expression and function of this protein in normal human monocytes/macrophages. We now report that galectin-3 is expressed in normal human peripheral blood monocytes and its level increases dramatically as human monocytes differentiate into macrophages upon culturing in vitro. Immunoblot analysis showed that there was a 5-fold increase in the level of galectin-3 after 1 day of culture and greater than a 12-fold increase after 5 days. Immunocytochemical analysis confirmed this progressive increase of galectin-3 expression in cultured monocytes. Immunogold cytochemistry/electron microscopy analysis revealed that galectin-3 was expressed on the surface of human monocytes and that tire level of cell surface galectin-3 increased progressively as these cells differentiated into macrophages. The level of galectin-3 in human monocytes/macrophages was modulated by stimuli such as lipopolysaccharide and interferon-γ, and galectin-3 was secreted when monocytes were stimulated by calcium ionophore A23187. Soluble galectin-3 caused superoxide release front human monocytes; this activity was dependent on the lectin property of galectin-3, as it was inhibitable by lactose. Thus, galectin-3 may modulate the function of this cell type in an autocrine or paracrine fashion through binding to cell surface glycoconjugates.
AB - A family of β-galactoside-binding animal lectins has recently been designated as galectins. One member of this family, galectin-3, has been known as εBP for its IgE-binding activity and as Mac-2, a macrophage surface antigen, CBP35, CBP30, L-29, and L-34. Although much information has accumulated on the expression of this lectin in murine macrophages and human monocytic cell lines, little is known about the expression and function of this protein in normal human monocytes/macrophages. We now report that galectin-3 is expressed in normal human peripheral blood monocytes and its level increases dramatically as human monocytes differentiate into macrophages upon culturing in vitro. Immunoblot analysis showed that there was a 5-fold increase in the level of galectin-3 after 1 day of culture and greater than a 12-fold increase after 5 days. Immunocytochemical analysis confirmed this progressive increase of galectin-3 expression in cultured monocytes. Immunogold cytochemistry/electron microscopy analysis revealed that galectin-3 was expressed on the surface of human monocytes and that tire level of cell surface galectin-3 increased progressively as these cells differentiated into macrophages. The level of galectin-3 in human monocytes/macrophages was modulated by stimuli such as lipopolysaccharide and interferon-γ, and galectin-3 was secreted when monocytes were stimulated by calcium ionophore A23187. Soluble galectin-3 caused superoxide release front human monocytes; this activity was dependent on the lectin property of galectin-3, as it was inhibitable by lactose. Thus, galectin-3 may modulate the function of this cell type in an autocrine or paracrine fashion through binding to cell surface glycoconjugates.
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M3 - Article
C2 - 7573347
AN - SCOPUS:0028874589
VL - 147
SP - 1016
EP - 1028
JO - American Journal of Pathology
JF - American Journal of Pathology
SN - 0002-9440
IS - 4
ER -