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

Plzák, Jan; Smetana, Karel; Hrdlickova, Enkela; Kodet, Roman; Holíková, Zuzana; Liu, Fu‐Tong; Dvořánková, Barbora; Kaltner, Herbert; Betka, Jan; Gabius, Hans‐Joachim

doi:10.3892/ijo.19.1.59

Cited by 34 publications

(39 citation statements)

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“…g Atretic preantral follicles were negative for cleaved caspase-3 (positive cells belong to adjacent atretic antral follicles) but presented DNA fragmentation (h, arrows) and galectin-3 (i, arrowheads) in the granulosa cell layer . Bar length 50 m (a-f, a1, b1, f1), 10 m (g-i) staining proWles overlapping with lectin localization, even with prognostic relevance in head and neck tumors, or separate from each other (Gabius et al 1991;Plzák et al 2001Plzák et al , 2004Kübler et al 2008). As in this case, lectin secretion or transport are then required to let these sites become functional.…”

Section: Discussionmentioning

confidence: 93%

Cell-type-specific expression of murine multifunctional galectin-3 and its association with follicular atresia/luteolysis in contrast to pro-apoptotic galectins-1 and -7

Lohr

Kaltner

Lensch

et al. 2008

Histochem Cell Biol

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Galectin-3 is a multifunctional protein with modular design. A distinct expression profile was determined in various murine organs when set into relation to homodimeric galectins-1 and -7. Fittingly, the signature of putative transcription-factor-binding sites in the promoter region of the galectin-3 gene affords a toolbox for a complex combinatorial regulation, distinct from the respective sequence stretches in galectins-1 and -7. A striking example for cell-type specificity was the ovary, where these two lectins were confined to the surface epithelium. Immunohistochemically, galectin-3 was found in macrophages of the cortical interstitium between developing follicles and medullary interstitium, matching the distribution of the F4/80 antigen. With respect to atresia and luteolysis strong signals in granulosa cells of atretic preantral but not antral follicles and increasing positivity in corpora lutea upon regression coincided with DNA fragmentation. Labeled galectin-3 revealed lactose-inhibitable binding to granulosa cells. Also, slender processes of vital granulosa cells which extended into the zona pellucida were positive. This study demonstrates cell-type specificity and cycle-associated regulation for galectin-3 with increased presence in atretic preantral follicles and in late stages of luteolysis.

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Section: Discussionmentioning

confidence: 93%

Cell-type-specific expression of murine multifunctional galectin-3 and its association with follicular atresia/luteolysis in contrast to pro-apoptotic galectins-1 and -7

Lohr

Kaltner

Lensch

et al. 2008

Histochem Cell Biol

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“…Gal-3 and Gal-3-BS were expressed suprabasally, predominantly in intercellular contacts of suprabasal cells of keratinized epithelia (Plza´k et al 2000(Plza´k et al , 2001. In comparison to other markers, the binding profile resembles that of desmosomal proteins (desmoplakins, desmogleins) when determined by simultaneous staining at the single-cell level (Plza´k et al 2001).…”

Section: Squamous Cell Epithelia and Their Galectins Under Physiologimentioning

confidence: 95%

Nuclear presence of adhesion-/growth-regulatory galectins in normal/malignant cells of squamous epithelial origin

Smetana

Dvořánková

Chovanec

et al. 2005

Histochem Cell Biol

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Cellular activities in the regulation of growth or adhesion/migration involve protein (lectin)-carbohydrate recognition at the cell surface. Members of the galectin family of endogenous lectins additionally bind distinct intracellular ligands. These interactions with protein targets explain the relevance of their nuclear and cytoplasmic presence. Expression profiling for galectins and accessible binding sites is a histochemical approach to link localization with cellular growth properties. Non-cross-reactive antibodies for the homodimeric (proto-type) galectins-1, -2 and -7 and the chimera-type galectin-3 (Gal-3) as well as the biotinylated lectins were tested. This analysis was performed with the FaDu squamous carcinoma cell line and long-term cultured human and porcine epidermal cells as models for malignant and normal cells of squamous cell epithelial origin. A set of antibodies was added for phenotypic cell characterization. Strong nuclear and cytoplasmic signals of galectins and the differential reactivity of labeled galectins support the notion of their individual properties. The length of the period of culture was effective in modulating marker expression. Cytochemical expression profiling is a prerequisite for the selection of distinct proteins for targeted modulation of gene expression as a step toward functional analysis.

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“…This tool is an alternative to biotinylated lectins, which had been widely used to describe the distribution pattern of glycoconjugates in normalcy and malignancy. Indeed, biotinylated galectin-3 had been successfully used by different groups, following the pioneering work of Gabius and colleagues (Choufani et al 1999;Plzak et al 2001). Gal3/AP is an effective alternative to biotinylated galectin-3; the former, however, can be produced in a single step.…”

Section: Discussionmentioning

confidence: 99%

Biological Applications of a Chimeric Probe for the Assessment of Galectin-3 Ligands

Melo

Butera

Medeiros

et al. 2007

J Histochem Cytochem.

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(RC) S U M M A R Y b1-6 branching of N-linked oligosaccharides has been correlated with the progression of different cancers. The leukoagglutinins of Phaseolus vulgaris (L-PHA) have been used to study this pattern of glycosylation whose biological significance is incompletely understood. The animal lectin, galectin-3, also binds to structures recognized by L-PHA. To develop a functional tool for the in situ identification of this pattern of glycosylation, human galectin-3 was fused to bacterial alkaline phosphatase (gal3/AP). Gal3/AP recognized both A and B blood group saccharides (B.A) and lactosamine derivatives. Gal3/AP recognition depended at least in part on the N-linked oligosaccharides of different glycoproteins. The presence and distribution of galectin-3 ligands were analyzed in both murine and human normal and tumor samples. Loss of apical expression of galectin-3 ligands was commonly found in carcinomas. Endothelial and inflammatory cells were enriched in galectin-3 ligands as compared with tumor cells; thus, gal3/AP is a suitable tool for studying tumor microenvironments. Comparative analysis of both gal3/AP and L-PHA binding patterns indicated that although similar, these patterns are not identical. The probe developed was useful for several immunoenzymatic assays and will allow the physiological and clinical significance of the expression pattern of galectin-3 ligands to be established. This manuscript contains online supplemental material at http://www.jhc.org. Please visit this article online to view these materials. (J Histochem Cytochem 55:1015-1026, 2007

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

Cited by 34 publications

References 0 publications

Cell-type-specific expression of murine multifunctional galectin-3 and its association with follicular atresia/luteolysis in contrast to pro-apoptotic galectins-1 and -7

Cell-type-specific expression of murine multifunctional galectin-3 and its association with follicular atresia/luteolysis in contrast to pro-apoptotic galectins-1 and -7

Nuclear presence of adhesion-/growth-regulatory galectins in normal/malignant cells of squamous epithelial origin

Biological Applications of a Chimeric Probe for the Assessment of Galectin-3 Ligands

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