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Lectins from the Red Marine Algal Species Bryothamnion seaforthii and Bryothamnion triquetrum as Tools to Differentiate Human Colon Carcinoma Cells.

Pinto VP, Debray H, Dus D, Teixeira EH, de Oliveira TM, Carneiro VA, Teixeira AH, Filho GC, Nagano CS, Nascimento KS, Sampaio AH, Cavada BS - Adv Pharmacol Sci (2009)

Bottom Line: The carbohydrate-binding activity of the algal lectins from the closely related red marine algal species Bryothamnion triquetrum (BTL) and Bryothamnion seaforthii (BSL) was used to differentiate human colon carcinoma cell variants with respect to their cell membrane glyco-receptors.These lectins interacted with the cells tested in a dose-dependent manner.Moreover, the fluorescence spectra of both lectins clearly differentiated the cells used as shown by FACS profiles.

View Article: PubMed Central - PubMed

Affiliation: Curso de Medicina/Campus de Sobral, Universidade Federal do Ceará, Fortaleza 60020-181, Brazil.

ABSTRACT
The carbohydrate-binding activity of the algal lectins from the closely related red marine algal species Bryothamnion triquetrum (BTL) and Bryothamnion seaforthii (BSL) was used to differentiate human colon carcinoma cell variants with respect to their cell membrane glyco-receptors. These lectins interacted with the cells tested in a dose-dependent manner. Moreover, the fluorescence spectra of both lectins clearly differentiated the cells used as shown by FACS profiles. Furthermore, as observed by confocal microscopy, BTL and BSL bound to cell surface glycoproteins underwent intense internalization, which makes them possible tools in targeting strategies.

No MeSH data available.


Related in: MedlinePlus

Confocal microscopy showing the interaction of (a) Bryothamnion seaforthii lectin, BSL, and (b) Bryothamnion triquetrum lectin, BTL PITC, labeled (at 37°C for 1 hour) with EB3 colon carcinoma cells variant. In this assay lectins were used at 10 μg/mL. In each case the lectin uptake was strongly visualized.
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fig3: Confocal microscopy showing the interaction of (a) Bryothamnion seaforthii lectin, BSL, and (b) Bryothamnion triquetrum lectin, BTL PITC, labeled (at 37°C for 1 hour) with EB3 colon carcinoma cells variant. In this assay lectins were used at 10 μg/mL. In each case the lectin uptake was strongly visualized.

Mentions: Temperature variables (4°C and 37°C) were used to verify differences in the binding properties of PITC-lectins. This step was necessary since the binding of the lectin to the membrane elements is very likely to take place at 4°C, where the fluidity of the cell membrane is reduced and the energy consumed in the transport processes is limited. At 37°C, a strong interaction of the lectins with the glycocalix components usually induces their uptake and storage in acidic vacuoles such as the lysosomes [21]. The binding of the lectins observed by flow cytometry was confirmed by confocal analysis at 4°C and no differences in the labeling-patterns of BSL and BTL could be observed (Figure 2). Nonetheless, when the bioadhesive activity was evaluated at 37°C, some particularities were observed. In general, internalization was quite evident (Figure 3).


Lectins from the Red Marine Algal Species Bryothamnion seaforthii and Bryothamnion triquetrum as Tools to Differentiate Human Colon Carcinoma Cells.

Pinto VP, Debray H, Dus D, Teixeira EH, de Oliveira TM, Carneiro VA, Teixeira AH, Filho GC, Nagano CS, Nascimento KS, Sampaio AH, Cavada BS - Adv Pharmacol Sci (2009)

Confocal microscopy showing the interaction of (a) Bryothamnion seaforthii lectin, BSL, and (b) Bryothamnion triquetrum lectin, BTL PITC, labeled (at 37°C for 1 hour) with EB3 colon carcinoma cells variant. In this assay lectins were used at 10 μg/mL. In each case the lectin uptake was strongly visualized.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2990109&req=5

fig3: Confocal microscopy showing the interaction of (a) Bryothamnion seaforthii lectin, BSL, and (b) Bryothamnion triquetrum lectin, BTL PITC, labeled (at 37°C for 1 hour) with EB3 colon carcinoma cells variant. In this assay lectins were used at 10 μg/mL. In each case the lectin uptake was strongly visualized.
Mentions: Temperature variables (4°C and 37°C) were used to verify differences in the binding properties of PITC-lectins. This step was necessary since the binding of the lectin to the membrane elements is very likely to take place at 4°C, where the fluidity of the cell membrane is reduced and the energy consumed in the transport processes is limited. At 37°C, a strong interaction of the lectins with the glycocalix components usually induces their uptake and storage in acidic vacuoles such as the lysosomes [21]. The binding of the lectins observed by flow cytometry was confirmed by confocal analysis at 4°C and no differences in the labeling-patterns of BSL and BTL could be observed (Figure 2). Nonetheless, when the bioadhesive activity was evaluated at 37°C, some particularities were observed. In general, internalization was quite evident (Figure 3).

Bottom Line: The carbohydrate-binding activity of the algal lectins from the closely related red marine algal species Bryothamnion triquetrum (BTL) and Bryothamnion seaforthii (BSL) was used to differentiate human colon carcinoma cell variants with respect to their cell membrane glyco-receptors.These lectins interacted with the cells tested in a dose-dependent manner.Moreover, the fluorescence spectra of both lectins clearly differentiated the cells used as shown by FACS profiles.

View Article: PubMed Central - PubMed

Affiliation: Curso de Medicina/Campus de Sobral, Universidade Federal do Ceará, Fortaleza 60020-181, Brazil.

ABSTRACT
The carbohydrate-binding activity of the algal lectins from the closely related red marine algal species Bryothamnion triquetrum (BTL) and Bryothamnion seaforthii (BSL) was used to differentiate human colon carcinoma cell variants with respect to their cell membrane glyco-receptors. These lectins interacted with the cells tested in a dose-dependent manner. Moreover, the fluorescence spectra of both lectins clearly differentiated the cells used as shown by FACS profiles. Furthermore, as observed by confocal microscopy, BTL and BSL bound to cell surface glycoproteins underwent intense internalization, which makes them possible tools in targeting strategies.

No MeSH data available.


Related in: MedlinePlus