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Analysis of the Role of Type 1 Core O-Glycans in the Binding of Anti-MUC1 Antibodies by Cytofluorometry and Synthetic Peptide/Glycopeptide Binding Inhibition Studies

Authors
  • Reddish, Mark A.
  • Suresh, Mavanur R.
  • Koganty, R. Rao
  • Fortier, Sandra
  • Baronic, Laurie
  • Berg, Ann
  • Longenecker, B. Michael
Type
Published Article
Journal
Tumor Biology
Publisher
SAGE Publications
Publication Date
Dec 08, 1997
Volume
19
Issue
1
Pages
57–66
Identifiers
DOI: 10.1159/000056505
Source
Karger
Keywords
License
Green
External links

Abstract

A panel of 56 MAbs submitted to the ISOBM TD-4 (MUC1) Workshop were analysed in two systems. These systems were designed to screen for peptide type 1 core O-glycan-related reactivities. Using synthetic MUC1 mucin-related peptides and glycopeptides, the panel of MAbs were tested for relative binding affinities to type 1 core O-glycan-substituted MUC1 structures. These studies utilized a competitive binding format with a native human adenocarcinoma-derived mucin as a solid phase. This system allows for analysis of the type 1 core glycoform subspecificity of each MAb. The second approach taken in parallel, utilized MCF-7 (BrCa) and OVCAR (OVCa) cell lines which were grown in the presence or absence of phenyl-N-acetylgalactosaminide (p-gal), a blocker of mucin O-linked glycosylation. These cells were analysed by FACS to examine the role these same glycan substitutions play with regard to either the diagnostic or therapeutic application of these MAbs. By FACS analysis there was a consistent increased ‘epitope exposure’ for peptide-specific MAbs binding in the presence of p-gal. In addition, a single MAb (TD-4 #150) is interpreted to react with a type 1 core O-glycan, probably with Tn, TF or STn specificity.

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