Serum sialyl Tn as an independent predictor of poor prognosis in patients with epithelial ovarian cancer.

Kobayashi, Hiroshi; Terao, Toshihiko; Kawashima, Y

doi:10.1200/jco.1992.10.1.95

Cited by 131 publications

(72 citation statements)

References 11 publications

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“…On the other hand, adenocarcinomas of several epithelial organs frequently express STn. Moreover, expression of STn by colon cancers and ovarian cancers has been associated with a poor survival (Itzkowitz et al, 1990;Kobayashi et al, 1992). This suggests that STn expression by cancer cells plays an important role in the biology of the tumour.…”

Section: Discussionmentioning

confidence: 99%

Mucin-associated sialosyl-Tn antigen expression in gastric cancer correlates with an adverse outcome

Werther

Rivera-MacMurray²,

Bruckner³

et al. 1994

Br J Cancer

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The expression of sialosyl-Tn (STn) antigen was evaluated by immunohistochemistry in primary gastric cancers. Twenty-one of 31 (68%) gastric cancers expressed STn, regardless of tumour location, stage or histological type. Eighty-one per cent of patients with STn-positive tumours died of their disease or had recurrent cancer, compared with 20% of patients with STn-negative tumours (P < 0.002). STn may be a useful prognostic marker in patients with gastric cancer. Images Figure 1

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Section: Discussionmentioning

confidence: 99%

Mucin-associated sialosyl-Tn antigen expression in gastric cancer correlates with an adverse outcome

Werther

Rivera-MacMurray²,

Bruckner³

et al. 1994

Br J Cancer

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“…elevated levels of urinary IGF-2 in urothelial carcinoma of the bladder (62) and it is not unlikely that these changes are accompanied by aberrant O-glycan profiles. The sialyl-Tn antigen (Neu5Ac␣2-6GalNAc␣-O-Ser/Thr) is a rare glycoepitope in normal tissue but high expression levels are known to occur in ovarian (63), gastric (64), colorectal (65) and pancreatic (66) carcinomas. Existing evidence also indicates that O-glycan occupancy is increased in cancer cells (67,68).…”

Section: Discussionmentioning

confidence: 99%

Human Urinary Glycoproteomics; Attachment Site Specific Analysis of N- and O-Linked Glycosylations by CID and ECD

Halim

Nilsson

Rüetschi

et al. 2012

Molecular & Cellular Proteomics

141

151

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“…Sialyl-Tn is a disaccharide found frequently on a variety of cancers and is known to be a useful diagnostic marker (39,40). High expression of this antigen is associated with a poor prognosis in most cancers studied (39,(41)(42)(43). With regard to ␣2-3-linked sialic acids, fucose (Fuc) residues are frequently found attached to the underlying GlcNAc.…”

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confidence: 99%

New Aspects of Siglec Binding Specificities, Including the Significance of Fucosylation and of the Sialyl-Tn Epitope

Linden¹,

Varki

2000

Journal of Biological Chemistry

154

135

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The siglecs (sialic acid-binding immunoglobulin superfamily lectins) are immunoglobulin superfamily members recognizing sialylated ligands. Most prior studies of siglec specificities focused on ␣2-3-and ␣2-6-sialyllactos(amin)es and on one or two of the siglecs at a time. Here, we explore several new aspects of specificities of the first six reported siglecs, using sialylated glycans presented in multivalent form, on synthetic polyacrylamide backbones, or on mucin polypeptides. First, we report that binding of siglec-1 (sialoadhesin), siglec-3 (CD33), siglec-4a (myelin-associated glycoprotein), and siglec-5 to ␣2-3 sialyllactosamine is affected markedly by the presence of an ␣1-3-linked fucose. Thus, while siglecs may not interfere with selectin-mediated recognition, fucosylation could negatively regulate siglec binding. Second, in contrast to earlier studies, we find that siglec-3 prefers ␣2-6-sialyllactose. Third, siglec-5 binds ␣2-8-linked sialic acid, making it the siglec least specific for linkage recognition. Fourth, siglecs-2 (CD22), -3, -5, and -6 (obesity-binding protein 1) showed significant binding to sialyl-Tn (Neu5Ac␣2-6-GalNAc), a tumor marker associated with poor prognosis. Fifth, siglec-6 is an exception among siglecs in not requiring the glycerol side chain of sialic acid for recognition. Sixth, all siglecs require the carboxyl group of sialic acid for binding. Finally, the presentation of the sialyl-Tn epitope and/or more extended structures that include this motif may be important for optimal recognition by the siglecs. This was concluded from studies using ovine, bovine, and porcine submaxillary mucins and Chinese hamster ovary cells transfected with ST6GalNAc-I and/or the mucin polypeptide MUC1.The siglecs (sialic acid-binding immunoglobulin superfamily lectins)1 are a class of Ig superfamily proteins (1) which show binding activity to specific glycan structures containing sialic acid (1-5). Sialic acids are acidic monosaccharides frequently found at the outer end of secreted and cell surface glycoconjugates (5-8), a good location for recognition by lectins such as the siglecs. To date, six different members of this family of lectins have been characterized (1, 2, 9 -14), and a recent paper describes a potential seventh member (15). The siglecs share overall structural characteristics, with an NH 2 -terminal V-set Ig domain followed by varying numbers of C2-set Ig domains. Siglec-1 (sialoadhesin, Sn) is the largest member, with 17 extracellular Ig domains, whereas siglec-3 (CD33) is the smallest, with only 2 of these domains. Each siglec has its own unique tissue distribution and specific phosphorylation sites on the cytosolic tail, indicating that each has specific functions mediated by the lectin activity. The latter suggestion is substantiated by the fact that each siglec seems to display distinctive specificities for recognition of sialic acid linkages. However, for most siglecs only a limited sampling of the wide array of sialylated glycans found in nature have been examined, primarily ...

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Serum sialyl Tn as an independent predictor of poor prognosis in patients with epithelial ovarian cancer.

Abstract: We conclude that a positive STN-antigen level in sera is an independent predictor of poor prognosis in ovarian cancer.

Cited by 131 publications

References 11 publications

Mucin-associated sialosyl-Tn antigen expression in gastric cancer correlates with an adverse outcome

Mucin-associated sialosyl-Tn antigen expression in gastric cancer correlates with an adverse outcome

Human Urinary Glycoproteomics; Attachment Site Specific Analysis of N- and O-Linked Glycosylations by CID and ECD

New Aspects of Siglec Binding Specificities, Including the Significance of Fucosylation and of the Sialyl-Tn Epitope

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