Expression of galectin-3-reactive ligands in squamous cancer and normal epithelial cells as a marker of differentiation.

J. Plzák, K. Smetana, E. Hrdlicková, R. Kodet, Z. Holíková, Fu-Tong Liu, B. Dvoránkova, H. Kaltner, J. Betka, H. J. Gabius

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Abstract

The definition of biological markers for oropharynx and larynx cancer is essential to predict their clinical behavior. Since cellular glycans play an important role in biological information transfer, we have employed an endogenous lectin, galectin-3, to examine in primary squamous carcinomas, lymph node metastases, and physiological squamous epithelia whether glycans recognized by this lectin are altered in relation to the state of differentiation. The expression of galectin-3 was concomitantly evaluated by immunohistochemistry using the A1D6 monoclonal antibody. In addition, other antibodies were used for the detection of cytokeratins and desmosomal proteins (desmoplakin-1 and desmoglein). The results show the expression of galectin-3-reactive ligands in moderately/highly differentiated carcinomas only in areas exhibiting a high level of keratinization. Except for one patient out of 14, metastatic cells in lymph nodes expressed no accessible binding sites for galectin-3. No galectin-3-reactivity was detected in the basal cell layer of all studied normal epithelia (which contains the proliferating cells). The suprabasal layers were positive in epidermis and epithelium of tongue and cornea and negative in epithelium of palatine tonsil. The tumor cells expressed galectin-3 with an intensity positively correlated with tumor differentiation. The position of galectin-3-reactive sites colocalized with the two tested desmosomal proteins. However, presence of these proteins was also detected in areas of tumor and suprabasal layers of tonsil epithelium where no binding reactivity for galectin-3 was found. The present study showed that expression of galectin-3-reactive glycoligands is differentiation-dependent in normal as well as malignant squamous cells. Colocalization of galectin-3-reactive sites with desmosomal proteins (desmoplakin-1 and desmoglein) suggests an association of the galectin-3 ligand(s) with the cell surface, pointing to a potential participation of galectin-3 in mediation of intercellular contacts in these tumor types.

Original languageEnglish (US)
Pages (from-to)59-64
Number of pages6
JournalInternational Journal of Oncology
Volume19
Issue number1
StatePublished - Jul 2001
Externally publishedYes

Fingerprint

Galectin 3
Differentiation Antigens
Epithelial Cells
Ligands
Neoplasms
Epithelium
Desmogleins
Desmoplakins
Palatine Tonsil
Lectins
Polysaccharides
Catalytic Domain
Proteins
Lymph Nodes
Oropharyngeal Neoplasms
Laryngeal Neoplasms
Keratins
Tongue
Epidermis
Cornea

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

Plzák, J., Smetana, K., Hrdlicková, E., Kodet, R., Holíková, Z., Liu, F-T., ... Gabius, H. J. (2001). Expression of galectin-3-reactive ligands in squamous cancer and normal epithelial cells as a marker of differentiation. International Journal of Oncology, 19(1), 59-64.

Expression of galectin-3-reactive ligands in squamous cancer and normal epithelial cells as a marker of differentiation. / Plzák, J.; Smetana, K.; Hrdlicková, E.; Kodet, R.; Holíková, Z.; Liu, Fu-Tong; Dvoránkova, B.; Kaltner, H.; Betka, J.; Gabius, H. J.

In: International Journal of Oncology, Vol. 19, No. 1, 07.2001, p. 59-64.

Research output: Contribution to journalArticle

Plzák, J, Smetana, K, Hrdlicková, E, Kodet, R, Holíková, Z, Liu, F-T, Dvoránkova, B, Kaltner, H, Betka, J & Gabius, HJ 2001, 'Expression of galectin-3-reactive ligands in squamous cancer and normal epithelial cells as a marker of differentiation.', International Journal of Oncology, vol. 19, no. 1, pp. 59-64.
Plzák, J. ; Smetana, K. ; Hrdlicková, E. ; Kodet, R. ; Holíková, Z. ; Liu, Fu-Tong ; Dvoránkova, B. ; Kaltner, H. ; Betka, J. ; Gabius, H. J. / Expression of galectin-3-reactive ligands in squamous cancer and normal epithelial cells as a marker of differentiation. In: International Journal of Oncology. 2001 ; Vol. 19, No. 1. pp. 59-64.
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abstract = "The definition of biological markers for oropharynx and larynx cancer is essential to predict their clinical behavior. Since cellular glycans play an important role in biological information transfer, we have employed an endogenous lectin, galectin-3, to examine in primary squamous carcinomas, lymph node metastases, and physiological squamous epithelia whether glycans recognized by this lectin are altered in relation to the state of differentiation. The expression of galectin-3 was concomitantly evaluated by immunohistochemistry using the A1D6 monoclonal antibody. In addition, other antibodies were used for the detection of cytokeratins and desmosomal proteins (desmoplakin-1 and desmoglein). The results show the expression of galectin-3-reactive ligands in moderately/highly differentiated carcinomas only in areas exhibiting a high level of keratinization. Except for one patient out of 14, metastatic cells in lymph nodes expressed no accessible binding sites for galectin-3. No galectin-3-reactivity was detected in the basal cell layer of all studied normal epithelia (which contains the proliferating cells). The suprabasal layers were positive in epidermis and epithelium of tongue and cornea and negative in epithelium of palatine tonsil. The tumor cells expressed galectin-3 with an intensity positively correlated with tumor differentiation. The position of galectin-3-reactive sites colocalized with the two tested desmosomal proteins. However, presence of these proteins was also detected in areas of tumor and suprabasal layers of tonsil epithelium where no binding reactivity for galectin-3 was found. The present study showed that expression of galectin-3-reactive glycoligands is differentiation-dependent in normal as well as malignant squamous cells. Colocalization of galectin-3-reactive sites with desmosomal proteins (desmoplakin-1 and desmoglein) suggests an association of the galectin-3 ligand(s) with the cell surface, pointing to a potential participation of galectin-3 in mediation of intercellular contacts in these tumor types.",
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AU - Liu, Fu-Tong

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