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Monoclonal Antibody Recognizing a Core Epitope on Mucin
Monoclonal antibody TH1 (IgM) was prepared by immunizing mice with deglycosylated (TFMSA-treated) cystic fibrosis mucin. TH1 reacted strongly with TFMSA treated cystic fibrosis mucin but not with the fully glycosylated mucin, indicating reactivity with a core mucin epitope. TH1 showed no reactivity...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
IOS Press
1998
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3850846/ https://www.ncbi.nlm.nih.gov/pubmed/9868597 http://dx.doi.org/10.1155/1998/678434 |
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author | Devine, Peter L. Quin, Rachel J. Shield, Paul W. Liew, Yew Wah Sheehan, John K. Thornton, David J. |
author_facet | Devine, Peter L. Quin, Rachel J. Shield, Paul W. Liew, Yew Wah Sheehan, John K. Thornton, David J. |
author_sort | Devine, Peter L. |
collection | PubMed |
description | Monoclonal antibody TH1 (IgM) was prepared by immunizing mice with deglycosylated (TFMSA-treated) cystic fibrosis mucin. TH1 reacted strongly with TFMSA treated cystic fibrosis mucin but not with the fully glycosylated mucin, indicating reactivity with a core mucin epitope. TH1 showed no reactivity with ovine mucin (98% of glycans as sialyl-Tn) but reacted strongly with desialylated ovine mucin, indicating the epitope for this mab was the Tn-antigen (O-linked GalNAc). However, TH1 showed no reactivity with Tn-positive red blood cells, and the binding of TH1 was not inhibited by GalNAc at 2.5 mg/ml, illustrating the importance of the peptide sequence to which the GalNAc is attached. TH1 stained the majority of cancers of the colon, lung, stomach, ovary, breast, and cervix, and the cellular distribution of this antigen in normal tissue suggested reactivity with immature mucin. This antibody appears to be a useful reagent for the detection of immature mucin. |
format | Online Article Text |
id | pubmed-3850846 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1998 |
publisher | IOS Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-38508462013-12-11 Monoclonal Antibody Recognizing a Core Epitope on Mucin Devine, Peter L. Quin, Rachel J. Shield, Paul W. Liew, Yew Wah Sheehan, John K. Thornton, David J. Dis Markers Other Monoclonal antibody TH1 (IgM) was prepared by immunizing mice with deglycosylated (TFMSA-treated) cystic fibrosis mucin. TH1 reacted strongly with TFMSA treated cystic fibrosis mucin but not with the fully glycosylated mucin, indicating reactivity with a core mucin epitope. TH1 showed no reactivity with ovine mucin (98% of glycans as sialyl-Tn) but reacted strongly with desialylated ovine mucin, indicating the epitope for this mab was the Tn-antigen (O-linked GalNAc). However, TH1 showed no reactivity with Tn-positive red blood cells, and the binding of TH1 was not inhibited by GalNAc at 2.5 mg/ml, illustrating the importance of the peptide sequence to which the GalNAc is attached. TH1 stained the majority of cancers of the colon, lung, stomach, ovary, breast, and cervix, and the cellular distribution of this antigen in normal tissue suggested reactivity with immature mucin. This antibody appears to be a useful reagent for the detection of immature mucin. IOS Press 1998 2002-06-07 /pmc/articles/PMC3850846/ /pubmed/9868597 http://dx.doi.org/10.1155/1998/678434 Text en Copyright © 1998 Hindawi Publishing Corporation. |
spellingShingle | Other Devine, Peter L. Quin, Rachel J. Shield, Paul W. Liew, Yew Wah Sheehan, John K. Thornton, David J. Monoclonal Antibody Recognizing a Core Epitope on Mucin |
title | Monoclonal Antibody Recognizing a Core Epitope on Mucin |
title_full | Monoclonal Antibody Recognizing a Core Epitope on Mucin |
title_fullStr | Monoclonal Antibody Recognizing a Core Epitope on Mucin |
title_full_unstemmed | Monoclonal Antibody Recognizing a Core Epitope on Mucin |
title_short | Monoclonal Antibody Recognizing a Core Epitope on Mucin |
title_sort | monoclonal antibody recognizing a core epitope on mucin |
topic | Other |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3850846/ https://www.ncbi.nlm.nih.gov/pubmed/9868597 http://dx.doi.org/10.1155/1998/678434 |
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