Homotypic Aggregation and Terminal Glycosylation of Cells from Dissociated Human Colorectal Tumor Tissue

Kemmner, Wolfgang; Schlag, Peter M.; Möller, Peter; Brossmer, Reinhard

doi:10.1159/000227013

Cited by 7 publications

(6 citation statements)

References 9 publications

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“…A similar finding was previously described by Kemmer et al [9], working with cells isolated from human colorectal adenocarcinomas. Considering all these results and our present observation on AAA reactivity, we can assume that in colorectal tumors, there may be an increased occurrence of fucose residues bound with linkages other than · (1,6).…”

Section: Discussionsupporting

confidence: 88%

“…Biochemical, histochemical and immunohistochemical studies have demonstrated differences between the glycoconjugates of normal and cancerous colorectal mucosa [5][6][7]. In this respect, changes in sialylation and fucosylation have been reported in malignant colorectal tumors and appear to be of great significance for the invasiveness and metastatic potential of tumoral cells [8][9][10].…”

Section: Introductionmentioning

confidence: 99%

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Immunohistochemical Analysis of Sialic Acid and Fucose Composition in Human Colorectal Adenocarcinoma

Fernández-Rodrı́guez¹,

Feijoo-Carnero

Merino-Trigo

et al. 2000

Tumor Biol

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The expression of different sialoglycoconjugates and fucoglycoconjugates in normal mucosa and adenocarcinoma samples from 43 colorectal cancer patients was investigated by using specific lectins and applying a semiquantitative analysis. A pronounced decrease in the intracellular binding of the Maackia amurensis lectin, which recognizes α(2,3)-linked sialic acid residues, was found in the tumoral tissue. In contrast, a significant increase in the staining with the Sambucus nigra lectin (SNA I), which binds to α(2,6)-linked sialic acid residues, was detected in the epithelial cells as well as in the mucins from tumors. No significant differences in the reactivity with the Aleuria aurantia lectin, which recognizes the sequence Fuc(α1,6)GlcNAc, between normal and malignant colorectal tissues were detected. Furthermore, the correlation between lectin-binding profiles and the prognosis of colorectal cancer patients was examined. After an average postoperative follow-up period of 31 months, patients with tumors showing a strong SNA I staining presented a greater probability of disease recurrence. This result suggests that the intensity of staining with SNA I could be a valid parameter for predicting recurrence in colorectal cancer.

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Section: Discussionsupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Immunohistochemical Analysis of Sialic Acid and Fucose Composition in Human Colorectal Adenocarcinoma

Fernández-Rodrı́guez¹,

Feijoo-Carnero

Merino-Trigo

et al. 2000

Tumor Biol

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“…A large amount of membrane-bound sialic acid promotes invasion [1,2], interferes with intercellular adhesion of freshly isolated colorectal carcinoma cells from surgical specimens [3], and stimulates platelet-aggregating to glycoproteins or glycolipids. For the synthesis of all known sialo-oligosaccharides, 10-12 sialyltransferases are necessary, some of which have been cloned successfully [11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Different sialyltransferase activities in human colorectal carcinoma cells from surgical specimens detected by specific glycoprotein and glycolipid acceptors

Kemmner

Krück

Schlag³

1994

Clin Exp Metast

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The amount and type of sialylation of tumor cell membranes depends on the activity of a number of different sialyltransferase enzymes. For the detection of specific activities in human colorectal carcinoma tissue several glycoprotein and glycolipid acceptors were used: desialylated fetuin, alpha 1-acid glycoprotein, beta 2-glycoprotein I, ovine submaxillaris mucin, and the gangliosides GM1, GM2, GM3 and GD1a. Because of their possible relevance for metastasis, precursors of Le(a) and Le(x) antigens, too, were employed, namely neoglycolipids produced by coupling LcOse4 or NeoLcOse4 oligosaccharides to L-alpha-phosphatidyl-ethanol-amine-dipalmitoyl. Our data indicate that human colorectal tumor tissue contains two highly active sialyltransferase enzymes, which are only weakly expressed in normal mucosa. These are a N-glycan-specific alpha 2,6-sialyltransferase, which was significantly increased in metastasizing tumors, and a Gal beta 1,3Gal-NAc-specific sialyltransferase, which was increased in tumors of early stages. A shift to enhanced alpha 2,6-sialylation of membrane glycoproteins during carcinogenesis was demonstrated by lectin ELISA analysis of magneto-bead separated tumor cells. Quantitative determination of specific sialyltransferase activities may be a sensitive tool for detection and monitoring of colon carcinoma.

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“…The presence of sialic acid at the terminal or near the terminal position underlies its importance in determining chemical and biological diversity, and characteristics of cell-surface and secreted glycoproteins [6]. Human and experimental model based studies have documented clinical significance of this sugar moiety [7,8]. Numerous investigators have reported possible relation of increased sialic acid levels with various malignancies [9][10][11].…”

mentioning

confidence: 99%

Tissue and serum α2-3- and α2-6-linkage specific sialylation changes in oral carcinogenesis

et al. 2007

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Increased sialylation of cell surface glycoconjugates is among the key molecular changes associated with malignant transformation and cancer progression. We investigated significance of linkage-specific sialylation changes in oral carcinogenesis. Tissue and serum levels of total sialic acid (TSA), linkage-specific sialyltransferases (ST) and sialoproteins were analyzed from patients with oral precancerous conditions (OPC) and oral cancer as well as the post-treatment follow-up blood samples of oral cancer patients. TSA levels were measured using a spectrophotometric method. The linkage-specific lectins, Sambusus nigra (SNA) and Maackia amurensis (MAM) detects alpha 2-6- and alpha 2-3-linked sialic acid, respectively, were used to analyze ST activity and sialoproteins. Malignant tissues showed significantly higher levels of TSA, reactivity of SNA and MAM, and alpha 2,3-ST activity compared to the adjacent normal tissues. alpha 2,6-ST was also higher in malignant tissues. Similarly, the marker levels were higher in precancerous tissues than their adjacent normal tissues. Serum levels of TSA, TSA/ total proteins, alpha 2-6-sialoproteins and alpha 2,6-ST were markedly increased in untreated oral cancer patients compared to the controls and OPC as well as responder (CR) patients. Serum levels of the markers were higher or comparable between untreated oral cancer patients and non-responders (NR). Serum levels of alpha 2-3-sialylation were elevated in non-responders compared with the responders. Further, the observed sialylation changes in tissue and serum were found to be associated with various clinicopathological features and disease progression. Thus, the data suggest potential utility of sialylation markers in early detection, prognostication and treatment monitoring of oral cancer.

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Homotypic Aggregation and Terminal Glycosylation of Cells from Dissociated Human Colorectal Tumor Tissue

Cited by 7 publications

References 9 publications

Immunohistochemical Analysis of Sialic Acid and Fucose Composition in Human Colorectal Adenocarcinoma

Immunohistochemical Analysis of Sialic Acid and Fucose Composition in Human Colorectal Adenocarcinoma

Different sialyltransferase activities in human colorectal carcinoma cells from surgical specimens detected by specific glycoprotein and glycolipid acceptors

Tissue and serum α2-3- and α2-6-linkage specific sialylation changes in oral carcinogenesis

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