PMID: 9422089Jan 9, 1998Paper

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

Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine
M ReddishB M Longenecker

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.

Citations

Nov 2, 1999·Micron : the International Research and Review Journal for Microscopy·J R Harris, J Markl
Feb 13, 2002·Hybridoma and Hybridomics·W QiR Madiyalakan
Nov 21, 2009·Molecular Diagnosis & Therapy·Aparna C Jotwani, Julie R Gralow

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