Expression and function of galectin-3, a β-galactoside-binding lectin, in human monocytes and macrophages

Fu-Tong Liu, D. K. Hsu, R. I. Zuberi, I. Kuwabara, E. Y. Chi, W. R. Henderson

Research output: Contribution to journalArticle

294 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1016-1028
Number of pages13
JournalAmerican Journal of Pathology
Volume147
Issue number4
StatePublished - 1995

Fingerprint

Galectin 3
Galactosides
Lectins
Monocytes
Macrophages
Galectins
Histocytochemistry
Glycoconjugates
Calcium Ionophores
Calcimycin
Lactose
Surface Antigens
Superoxides
Interferons
Immunoglobulin E
Lipopolysaccharides
Electron Microscopy

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

Cite this

Liu, F-T., Hsu, D. K., Zuberi, R. I., Kuwabara, I., Chi, E. Y., & Henderson, W. R. (1995). Expression and function of galectin-3, a β-galactoside-binding lectin, in human monocytes and macrophages. American Journal of Pathology, 147(4), 1016-1028.

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 journalArticle

Liu, F-T, Hsu, DK, Zuberi, RI, Kuwabara, I, Chi, EY & Henderson, WR 1995, 'Expression and function of galectin-3, a β-galactoside-binding lectin, in human monocytes and macrophages', American Journal of Pathology, vol. 147, no. 4, pp. 1016-1028.
Liu, Fu-Tong ; Hsu, D. K. ; Zuberi, R. I. ; Kuwabara, I. ; Chi, E. Y. ; Henderson, W. R. / Expression and function of galectin-3, a β-galactoside-binding lectin, in human monocytes and macrophages. In: American Journal of Pathology. 1995 ; Vol. 147, No. 4. pp. 1016-1028.
@article{8133d1d2e8d24c8599f981876814e9a3,
title = "Expression and function of galectin-3, a β-galactoside-binding lectin, in human monocytes and macrophages",
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.",
author = "Fu-Tong Liu and Hsu, {D. K.} and Zuberi, {R. I.} and I. Kuwabara and Chi, {E. Y.} and Henderson, {W. R.}",
year = "1995",
language = "English (US)",
volume = "147",
pages = "1016--1028",
journal = "American Journal of Pathology",
issn = "0002-9440",
publisher = "Elsevier Inc.",
number = "4",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0028874589&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028874589&partnerID=8YFLogxK

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 -