An O-Acetylated Sialyl-Tn Is Involved in Ovarian Cancer-Associated Antigenicity

Toba, Shinya; Tenno, Mari; Kurosaka, Akira

doi:10.1006/bbrc.2000.2618

Cited by 10 publications

(4 citation statements)

References 27 publications

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“…The terminal epitope -Neu5Ac-(2→6)--D-GalpNAc-(1→ was described for the first time in human colon mucin, and is known as the sialyl-Tn-epitope [131,132]. O-acetylated sialyl-Tn was reported in ovarian cancer where the acetyl group had a critical function in recognition by antibodies [133]. For H. parainfluenzae strain T3T1 it is tempting to speculate that the oligosaccharide, through molecular mimicry, contributes to evading the human immune response.…”

Section: Discussionmentioning

confidence: 99%

Expression of a new disialyllacto structure in the lipopolysaccharide of non-typeable Haemophilus influenzae

Twelkmeyer

Burström

et al. 2011

Carbohydrate Research

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Section: Discussionmentioning

confidence: 99%

Expression of a new disialyllacto structure in the lipopolysaccharide of non-typeable Haemophilus influenzae

Twelkmeyer

Burström

et al. 2011

Carbohydrate Research

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“…Enzymatic treatments were carried out at 37°C in 50 mM sodium phosphate, pH 6.0 (S. pneumoniae, C. perfringens, A. ureafaciens) or 50 mM sodium acetate, pH 5.5 (Newcastle disease virus). Sialic acids were de-O-acetylated by alkaline hydrolysis as described by Toba et al (Toba et al, 2000). Briefly, 1-50 μg of total protein from human tears were treated with 0.2 M NaOH at 24°C for up to 120 min.…”

Section: Enzymatic Treatments and De-o-acetylationmentioning

confidence: 99%

Characterization of a carbohydrate epitope defined by the monoclonal antibody H185: sialic acid O-acetylation on epithelial cell-surface mucins

Argüeso

Sumiyoshi

2006

Glycobiology

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Sialic acids comprise a large family of derivatives of neuraminic acid containing methyl, acetyl, sulfate, and phosphate among other groups, which confer specific physicochemical properties (e.g., hydrophobicity and resistance to hydrolases) to the molecules carrying them. Several years ago, a monoclonal antibody, designated H185, was developed, which binds to cell membranes of human corneal, conjunctival, laryngeal, and vaginal epithelia and whose distribution is altered on the ocular surface of patients with keratinizing disease. Recent findings using immunoprecipitation and immunodepletion techniques have demonstrated that, in human corneal epithelial cells, the H185 antigen is carried by the membrane-associated mucin MUC16. In this study, we show that the H185 epitope on human corneal cells and in tear fluid is an O-acetylated sialic acid epitope that can be selectively hydrolyzed in an enzyme-concentration-dependent manner by sialidase from Arthrobacter ureafaciens and to a lesser extent by sialidases from Newcastle disease virus, Clostridium perfringens, and Streptococcus pneumoniae. Binding of the H185 antibody was impaired by treatment of tear fluid with a recombinant 9-O-acetylesterase from influenza C virus. Two O-acetyl derivatives, Neu5,7Ac(2) and Neu5,9Ac(2), were identified in human tear fluid by fluorometric high-performance liquid chromatography (HPLC) and electrospray mass spectrometry (MS). Immunoprecipitation of the H185 epitope from human corneal epithelial cells revealed that Neu5,9Ac(2) was the major derivative on the mucin isolate. These results indicate that exposed wet-surfaced epithelia are decorated with O-acetyl sialic acid derivatives on membrane-associated mucins and suggest that O-acetylation on cell surfaces may protect against pathogen infection by preventing degradation of membrane-associated mucins.

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“…The expression of Tn and sialyl Tn antigens have been observed on ovarian tumors and studies have also attempted to determine if monitoring the levels of these carbohydrate antigens in coordination with serum CA125 levels could be used to detect and monitor ovarian cancer progression (123, 124). Tn and sialyl Tn antigens have been detected on the O-linked glycans expressed on the ovarian tumor cell surface and these glycans have also been detected on MUC16 and other specific glycoproteins isolated from ovarian tumor cells (125).…”

Section: Glycoproteins and Immune Protectionmentioning

confidence: 99%