Expression of Gal beta 1-4GlcNAc sequences by human gastrointestinal neoplasms and their precursors as detected by Erythrina cristagalli and Erythrina corallodendron lectins

Baldus, Stephan; Park, Y; Kotlarek, G; Hell, K; Fischer, Rainer

doi:10.3892/ijo.9.1.43

Cited by 3 publications

(4 citation statements)

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“…This process is associated with cell dedifferentiation, since less differentiated adenocarcinomas are CGL-negative. These observation confirm our conclusion that aberrant glycoprotein glycosylation accompanies neoplastic cell transformation [2].…”

Section: Resultssupporting

confidence: 80%

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Cell localization of mucin-type receptors assayed with novel GalNac/Gal-specific lectin from sea musselCrenomytilus grayanus in human colon tumors

et al. 1999

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Section: Resultssupporting

confidence: 80%

“…In mucins, carbohydrate chains constitute about 80% of the total molecular weight (400-1000 kD). The behavior and the role of Pacific Institute of Bioorganic Chemistry, Far-Eastern Division of the Russian Academy of Medical Sciences, Vladivostok mucin-type glycoproteins in tumor transformation remained obscure [2,7].…”

Section: Cancermentioning

confidence: 99%

Cell localization of mucin-type receptors assayed with novel GalNac/Gal-specific lectin from sea musselCrenomytilus grayanus in human colon tumors

et al. 1999

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“…In this context, it seems to be of special interest that galectin-3 binds preferentially to oligosaccharides which substitute mucin antigens produced by metastatic tumor cells [38], e.g. polylactosamine sequences strongly expressed by gastrointestinal neoplasms [39]. Such mechanisms might promote cell-cell adhesion of tumor cells as well as their growth pattern.…”

Section: Discussionmentioning

confidence: 99%

Increased Galectin-3 Expression in Gastric Cancer: Correlations with Histopathological Subtypes, Galactosylated Antigens and Tumor Cell Proliferation

Baldus¹,

Zirbes²,

Weingarten³

et al. 2000

Tumor Biology

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Galectin-3 represents an endogenous galactoside-binding lectin which may be involved in tumor cell adhesion and proliferation. In order to evaluate its biological significance in human gastric cancer, we investigated its expression in the stomach of a large series of patients (n = 193) by immunohistochemical staining with the monoclonal antibody Mac-2. Compared to normal tissues, primary gastric adenocarcinomas showed a slight increase in galectin-3 expression. However, there was no correlation of membrane-bound and cytoplasmic galectin-3 with histopathological differentiation parameters (according to the WHO and Laurén classifications) or tumor progression (as documented by pTNM staging). Nuclear galectin-3 reactivity was significantly stronger in diffuse-type cancer compared to the intestinal-type tumors. Galectin-3 binds to terminal GalNAcα(1–3) bound to polylactosamine chains and related glycotopes. Therefore, the strong coexpression of membrane/cytoplasmic galectin-3 with Griffonia simplicifolia agglutinin I (GSA I) binding sites (Galα1–3Gal-, GalNAcα–) on carcinoma cells seems to be interesting. On the other hand, nuclear galectin-3 immunoreactivity did not correlate with the incidence of Ki-67-positive tumor cells. A prognostic value of galectin-3 regarding patient survival could not be established.

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“…Various studies have shown altered carbohydrate composition in colorectal adenomas and carcinomas. For example, Baldus et al (1996) showed the signifi-cance of the lectins obtained from Erythrina cristagalli (ECA) and Erythrina corallodendron (EcorA), both known to recognize Gal ␤ 1-4 GlcNac residues, which are biosynthetic precursors of ABH and Lewis blood group antigens, also related to tumor-associated carbohydrate antigens. Altered lectin binding in colorectal tumors has also been reported.…”

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confidence: 99%

Differential Expression of Sialic Acid and N-acetylgalactosamine Residues on the Cell Surface of Intestinal Epithelial Cells According to Normal or Metastatic Potential

Redondo

Nakamura

Souza

et al. 2004

J Histochem Cytochem.

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In this study we investigated the levels of expression of sialic acid and N-acetylgalactosamine residues on the cell surface of a normal intestinal epithelium cell line, IEC-6, and in two colon adenocarcinoma cell lines with different metastatic potential, Caco-2 and HCT-116. Glycoprotein expression was estimated initially by cytochemistry with WGA and HPA lectins and biochemistry with isolated plasma membrane fractions of the cells. Fluorescence and electron microscopic analyses revealed differences in the expression profile of carbohydrates recognized by the lectins used on the cell surface of IEC-6, Caco-2, and HCT-116 cells. Lectin blotting identified a range of eight HPA-binding glycoprotein bands with molecular weights of 16-66 kD in Caco-2 cells, six glycoproteins of 16-36 kD, and three protein bands of 35, 24, and 21 kD in IEC-6 cells. A minor band of 66 kD and a major one of 50 kD for WGA-binding glycoproteins were observed in IEC-6 cells and seven glycoproteins of 18-97 kD in Caco-2 and HCT-116 cells but with a visible higher expression of these glycoproteins in the latter. Furthermore, significant quantitative difference in levels of expression of WGA- but not of HPA-binding glycoconjugates was noted, as analyzed by high-resolution scanning electron microscopy using backscattered electron images of cells incubated with gold-labeled lectins.

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Expression of Gal beta 1-4GlcNAc sequences by human gastrointestinal neoplasms and their precursors as detected by Erythrina cristagalli and Erythrina corallodendron lectins

Cited by 3 publications

References 0 publications

Cell localization of mucin-type receptors assayed with novel GalNac/Gal-specific lectin from sea musselCrenomytilus grayanus in human colon tumors

Cell localization of mucin-type receptors assayed with novel GalNac/Gal-specific lectin from sea musselCrenomytilus grayanus in human colon tumors

Increased Galectin-3 Expression in Gastric Cancer: Correlations with Histopathological Subtypes, Galactosylated Antigens and Tumor Cell Proliferation

Differential Expression of Sialic Acid and N-acetylgalactosamine Residues on the Cell Surface of Intestinal Epithelial Cells According to Normal or Metastatic Potential

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