Galectin-3 promotes adhesion of human neutrophils to laminin

Ichiro Kuwabara, Fu-Tong Liu

Research output: Contribution to journalArticle

253 Citations (Scopus)

Abstract

Galectin-3 is a member of a growing family of animal lectins composed of three domains, with the amino-terminal half consisting of a short segment followed by tandem repeats, and the carboxyl-terminal half representing the carbohydrate-recognition domain. Previously, we have shown that galectin-3 binds to the surface of human neutrophils and is capable of activating these cells. We have now studied the effect of exogenous galectin-3 on adhesion of human neutrophils to laminin-coated microtiter plates and found that this lectin promotes the adhesion in a dose-dependent manner. The effect was dependent on the lectin's carbohydrate-binding function, as well as its amino-terminal region. The galectin-3-induced adhesion was reduced significantly in the presence of EDTA, even though Ca2+ and Mg2+ are not required for the lectin binding, and the adhesion was significantly less at 4°C, as compared with 37°C. Galectin-3 also induced neutrophil adhesion to fibronectin, which is not recognized by the lectin, but much higher concentrations of the lectin were required, and the effect is completely dependent on Ca2+ and Mg2+. We conclude that galectin-3 induces neutrophil adhesion to laminin through a combination of two distinct mechanisms: 1) the lectin bridges neutrophils to laminin, in a carbohydrate- dependent and Ca2+-, Mg2+-independent manner, and 2) the lectin induces activation of neutrophils, in the presence of the divalent cations, resulting in the positive regulation of other cell adhesion molecules and enhanced adhesion to laminin. The results suggest that galectin-3 may play a role in the traversing of neutrophils through the basement membrane at inflammation sites.

Original languageEnglish (US)
Pages (from-to)3939-3944
Number of pages6
JournalJournal of Immunology
Volume156
Issue number10
StatePublished - May 15 1996

Fingerprint

Galectin 3
Laminin
Lectins
Neutrophils
Carbohydrates
Neutrophil Activation
Tandem Repeat Sequences
Divalent Cations
Cell Adhesion Molecules
Fibronectins
Basement Membrane
Edetic Acid
Inflammation

ASJC Scopus subject areas

  • Immunology

Cite this

Kuwabara, I., & Liu, F-T. (1996). Galectin-3 promotes adhesion of human neutrophils to laminin. Journal of Immunology, 156(10), 3939-3944.

Galectin-3 promotes adhesion of human neutrophils to laminin. / Kuwabara, Ichiro; Liu, Fu-Tong.

In: Journal of Immunology, Vol. 156, No. 10, 15.05.1996, p. 3939-3944.

Research output: Contribution to journalArticle

Kuwabara, I & Liu, F-T 1996, 'Galectin-3 promotes adhesion of human neutrophils to laminin', Journal of Immunology, vol. 156, no. 10, pp. 3939-3944.
Kuwabara I, Liu F-T. Galectin-3 promotes adhesion of human neutrophils to laminin. Journal of Immunology. 1996 May 15;156(10):3939-3944.
Kuwabara, Ichiro ; Liu, Fu-Tong. / Galectin-3 promotes adhesion of human neutrophils to laminin. In: Journal of Immunology. 1996 ; Vol. 156, No. 10. pp. 3939-3944.
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