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Updated: Sep 26, 2026
A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 1, 2009
Galectin-3, an endogenous lectin, as a tool for monitoring cell differentiation in head and neck carcinomas with
Jan Betka1, Jan Plzák, Karel Smetana
1Department of Otorhinolaryngology and Head and Neck Surgery, 1st Faculty of Medicine, Faculty Hospital Motol, Prague, Czech Republic. Jan.Betka@lfmotol.cuni.cz
Objective:
Galectin-3 is an endogenous lectin that reacts with glycan epitopes of membrane and extracellular glycoproteins, including integrins, fibronectin, laminin and tetraspanins. Its expression, and also the presentation of its glycoligands, is controlled in a differentiation-dependent manner in squamous epithelia. The aim of this study was to monitor the carbohydrate-dependent binding of labeled galectin-3 to primary head and neck squamous cell carcinomas (from the tonsil, base of the tongue and larynx) and lymph node metastases.
Material And Methods:
Double labeling (using antibodies against desmoplakin-1, Ki-67 and cytokeratins) at the single-cell level was employed to cytologically characterize cells reacting with galectin-3.
Results:
Galectin-3 binds a non-proliferating pool of tumor cells. Colocalization of galectin-3 binding sites with desmosomal proteins may indicate a role for this endogenous lectin in the formation of intercellular contacts of the desmosomal type. Cytokeratin-10-positive tumor cells also presented galectin-3-reactive binding sites on the surface; however, cytokeratin-10-free cells were also recognized by this lectin.
Conclusion:
These findings intimate that galectin-3 may represent a new tool for monitoring the degree of cell differentiation in carcinomas originating from the transformation of squamous cell epithelia.
