Carbohydrates of the tumor cell surface

Smets, L. A.; Beek, Wim P. Van

doi:10.1016/0304-419x(83)90006-9

Cited by 92 publications

(52 citation statements)

References 77 publications

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“…Alterations in cell surface carbohydrate expression during neoplastic development have been frequently observed in man and animals (Feizi, 1985a;Feizi, 1985b;Hakomori, 1989;Smets & Van Beek, 1984;Yogeeswaran, 1983). This seems to hold true for mammary neoplasia (Franklin, 1983;Gooi et al, 1985a;Gooi et al, 1985b;Howard et al, 1981;McKenzie & Xing, 1990;Muller-Holzner et al, 1985;Taylor-Papadimitriou et al, 1990).…”

mentioning

confidence: 96%

Sequential alteration of peanut agglutinin binding-glycoprotein expression during progression of murine mammary neoplasia

Rak¹,

McEachern²,

Miller³

1992

Br J Cancer

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mentioning

confidence: 96%

Sequential alteration of peanut agglutinin binding-glycoprotein expression during progression of murine mammary neoplasia

Rak¹,

McEachern²,

Miller³

1992

Br J Cancer

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“…Given that the CDw75 epitope has been described as a membrane-associated antigen and alterations in the cell membrane glycoconjugates is a well-known tumor characteristic (25), only the preparations enriched in membrane-associated proteins were used for two-dimensional (2D) western blotting. Prior to 2D electrophoresis, the samples were subjected to a desalting step by ultrafiltration through 10 kDa molecular weight cut-off Amicon © Ultra-4 centrifugal filter units (Sigma-Aldrich; Merck KGaA), three times at 2,700 x g for 30 min at 4˚C.…”

Section: Two-dimensional Western Blottingmentioning

confidence: 99%

Identification of proteins with the CDw75 epitope in human colorectal cancer

2017

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Abstract. The CDw75 epitope is an α(2,6) sialylated antigen overexpressed in colorectal cancer (CRC), where its expression correlates with the progression of the disease. The CDw75 epitope is located mainly in N-glycoproteins, whose identity remains unknown. The aim of the present study was to identify proteins with the CDw75 epitope as a strategy to deepen the understanding of molecular pathogenesis of CRC and to identify novel biomarkers for this disease. For this purpose, a two-dimensional electrophoresis approach was employed. Protein spots in the gels were matched to the corresponding CDw75 positive spots in the immunoblotted polyvinylidene difluoride membranes, and further identification of the protein species was performed by mass spectrometry. Additionally, one-dimensional western blotting experiments were performed to verify the expression of these candidate proteins in the colorectal tissue and their coincidence in molecular mass with the CDw75-positive bands. The findings of the present study indicate that haptoglobin and the keratins 8 (K8) and 18 (K18) are proteins with the CDw75 epitope in the colorectal tissue from CRC patients and also suggest novel functions and cellular locations for these proteins in the colorectal tissue and in relation to CRC.

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“…About ten years ago, evidence began to accumulate that the carbohydrate structures of cell-surfdce glycoproteins and glycolipids became dramatically altered during both normal and abnormai cellular development (1)(2)(3)(4). Consistent changes in cell-surface carbohydrate structures have now been shown to accompany the development of human melanoma, neuroblastoma, and colorectal, gastric, and pancreatic carcinoma ( 5 ) .…”

Section: Introductionmentioning

confidence: 99%

Substrates for the differentiation of the N-acetylglucosaminytransferases. Synthesis of βDGlcNAc(1 → 2)αDMan(1 → 6)βDMan and βDGlcNAc(1 → 2)αDMan(1 → 6) [αDMan(1 → 3)]βDMan glycosides

Tahir¹,

Hindsgaul²

1986

Can. J. Chem.

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. 64, 1771 (1986). The trisaccharide P~GlcNAc(l+2)a~Man(l+6)p~Man (2) and the tetrasaccharide P~GlcNAc(l+2)a~Man(1+ 6 ) [ a~M a n ( l + 3 ) ] P~M a n (3) have been chemically synthesized as their 8-methoxycarbonyloctyl glycosides. Compounds 2 and 3, both partial structures of naturally occurring asparagine linked oligosaccharides, are designed to function as selective substrates in N-acetylglucosaminyltransferase assays.S. HASAN TAHIR and OLE HINDSGAUL. Can. J. Chem. 64. 1771Chem. 64. (1586. Faisant appel a des mCthodes chimiques, on a synthCtisC le trisaccharide (3-~GlcNAc(l+2)a~Man(l-6)P~Man 2 ainsi que le tktrasaccharide P-~GlcNAc(l+2)cr~Man(1+6)[a~Man(l-+3)] PDMan 3, tous les deux sous la forme de leur glycosides mCthoxycarbony1-8 octyles. Les composCs 2 et 3, qui sont des fractions d'asparagine qui l'on retrouve naturellement li&e a des oligosaccharides, ont CtC prCparCs pour servir de substrats s6lectifs dans des Ctudes sur la N-ac6tylglucosaminyltransfCrase.[Traduit par la revue]

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Carbohydrates of the tumor cell surface

Cited by 92 publications

References 77 publications

Sequential alteration of peanut agglutinin binding-glycoprotein expression during progression of murine mammary neoplasia

Sequential alteration of peanut agglutinin binding-glycoprotein expression during progression of murine mammary neoplasia

Identification of proteins with the CDw75 epitope in human colorectal cancer

Substrates for the differentiation of the N-acetylglucosaminytransferases. Synthesis of βDGlcNAc(1 → 2)αDMan(1 → 6)βDMan and βDGlcNAc(1 → 2)αDMan(1 → 6) [αDMan(1 → 3)]βDMan glycosides

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