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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

Analysis by flow cytometry of (a) Bryothamnion seaforthii lectin, BSL, and (b) Bryothamnion triquetrum lectin, BTL PITC, labeled. In this assay lectins were used at 10 μg/mL. (*) negative control BSA PITC-labeled.
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fig1: Analysis by flow cytometry of (a) Bryothamnion seaforthii lectin, BSL, and (b) Bryothamnion triquetrum lectin, BTL PITC, labeled. In this assay lectins were used at 10 μg/mL. (*) negative control BSA PITC-labeled.

Mentions: The PITC-labeled algal lectins BSL and BTL were allowed to interact with LS180, EB3, and three colon carcinoma cell variants (3LNLN, 5W, and 8W). Analysis by flow cytometry demonstrated that both PITC-labelled proteins were able to recognize cell membrane components in these cells (Table 1). The recognition of cell surface components indicates that these lectins were able to differentiate cancer cell variants (Figure 1). The shift in fluorescence intensity induced by the interaction of the PITC-lectins with the cell variants was quite similar, suggesting that the lectins bound to the cell surface may be anchored by the same component. It is interesting, however, that both lectins could differentiate the cells tested under the same experimental conditions. Analysis of the interaction, with regard to cell recognition, showed that BSL and BTL discriminated the cell variants.


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)

Analysis by flow cytometry of (a) Bryothamnion seaforthii lectin, BSL, and (b) Bryothamnion triquetrum lectin, BTL PITC, labeled. In this assay lectins were used at 10 μg/mL. (*) negative control BSA PITC-labeled.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

fig1: Analysis by flow cytometry of (a) Bryothamnion seaforthii lectin, BSL, and (b) Bryothamnion triquetrum lectin, BTL PITC, labeled. In this assay lectins were used at 10 μg/mL. (*) negative control BSA PITC-labeled.
Mentions: The PITC-labeled algal lectins BSL and BTL were allowed to interact with LS180, EB3, and three colon carcinoma cell variants (3LNLN, 5W, and 8W). Analysis by flow cytometry demonstrated that both PITC-labelled proteins were able to recognize cell membrane components in these cells (Table 1). The recognition of cell surface components indicates that these lectins were able to differentiate cancer cell variants (Figure 1). The shift in fluorescence intensity induced by the interaction of the PITC-lectins with the cell variants was quite similar, suggesting that the lectins bound to the cell surface may be anchored by the same component. It is interesting, however, that both lectins could differentiate the cells tested under the same experimental conditions. Analysis of the interaction, with regard to cell recognition, showed that BSL and BTL discriminated the cell variants.

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