Immunoelectron microscopic localization of galectin‐3, an IgE binding protein, in human mast cells and basophils

Shirley S. Craig, Priya Krishnaswamy, Anne‐Marie A. Irani, Christopher L. Kepley, Fu-Tong Liu, Lawrence B. Schwartz

Research output: Contribution to journalArticlepeer-review

49 Scopus citations


Galectin‐3 is an endogenous soluble lectin within the family called galectins that bind β‐galactosides. Homologs of the protein isolated from different sources were previously designated as IgE‐binding protein (ϵBP), CBP35, CPB30, Mac‐2, RL‐29, RLL, L‐29, and HL‐29. All are now renamed galectin‐3. This lectin is widely distributed in cells and tissues of mice, rats, dogs, hamsters, and humans. Light microscopic immunohistochemistry and ultrastructural immunogold labeling methods were used to determine the distribution of galectin‐3 in human mast cells of several organs, in mast cells developed in vitro from human fetal liver cells, and in human peripheral blood basophils. Immunolabeling for the protein was observed in mast cells from all sources and in basophils. The lectin was detected in the nucleus and/or the cytoplasm. The nuclear labeling was over heterochromatin whereas euchromatin was unlabeled. Cytoplasmic labeling was concentrated over secretory granules. The intensity of staining generally was greater in mast cells of skin when compared with that of mast cells in other locations and with that of basophils. Studies have indicated that in mast cells galectin‐3 may be involved in promoting their adhesion to basal laminae. In this study the localization of galectin‐3 in the secretory granules of human mast cells and basophils suggests that these cells may release this lectin when activated to degranulate. © 1995 Wiley‐Liss, Inc.

Original languageEnglish (US)
Pages (from-to)211-219
Number of pages9
JournalThe Anatomical Record
Issue number2
StatePublished - 1995


  • Basophil
  • Epsilon binding protein
  • Immunogold
  • Lectin
  • Mast cell

ASJC Scopus subject areas

  • Anatomy


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