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Epithelium-specific surface glycoprotein of Mr 34,000 is a widely distributed human carcinoma marker.
An epithelial cell surface antigen is described which is defined by monoclonal antibody HEA125 (IgG1). The antibody was raised against the colon carcinoma cell line HT-29. Under reducing conditions HEA125 immunoprecipitates a surface glycoprotein of Mr 34,000 which was designated Egp34. The antigen...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Nature Publishing Group
1987
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2002400/ https://www.ncbi.nlm.nih.gov/pubmed/2449234 |
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author | Moldenhauer, G. Momburg, F. Möller, P. Schwartz, R. Hämmerling, G. J. |
author_facet | Moldenhauer, G. Momburg, F. Möller, P. Schwartz, R. Hämmerling, G. J. |
author_sort | Moldenhauer, G. |
collection | PubMed |
description | An epithelial cell surface antigen is described which is defined by monoclonal antibody HEA125 (IgG1). The antibody was raised against the colon carcinoma cell line HT-29. Under reducing conditions HEA125 immunoprecipitates a surface glycoprotein of Mr 34,000 which was designated Egp34. The antigen does not contain disulfide-linked subunits. A slightly different migration behavior under non-reducing conditions (Mr 39,000) may be due to intrachain disulfide bonds. After enzymatic cleavage of N-linked carbohydrate residues the apparent molecular weight of the antigen was 29,000. Egp34 is a major cell surface component of HT-29 cells (10(6) molecules per cell). No antigen could be detected in the sera of colorectal cancer patients. A panel of malignant cell lines and normal cells was studied for surface expression of the antigen. 17/17 carcinoma lines of 6 different origins expressed the antigen, whereas 16/16 melanoma, neuroblastoma, sarcoma and lymphoma/leukaemia were unreactive as it was the case for normal fibroblasts and blood cells. Immunoperoxidase staining of frozen tissue sections with HEA125 demonstrated the presence of Egp34 in almost all normal epithelia and tumours derived therefrom. No reactivity with non-epithelial tissues was observed. Undifferentiated carcinomas of various origins homogeneously expressed Egp34. Therefore, HEA125 may become a valuable tool for the immunohistochemical diagnosis of carcinoma. IMAGES: |
format | Text |
id | pubmed-2002400 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1987 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-20024002009-09-10 Epithelium-specific surface glycoprotein of Mr 34,000 is a widely distributed human carcinoma marker. Moldenhauer, G. Momburg, F. Möller, P. Schwartz, R. Hämmerling, G. J. Br J Cancer Research Article An epithelial cell surface antigen is described which is defined by monoclonal antibody HEA125 (IgG1). The antibody was raised against the colon carcinoma cell line HT-29. Under reducing conditions HEA125 immunoprecipitates a surface glycoprotein of Mr 34,000 which was designated Egp34. The antigen does not contain disulfide-linked subunits. A slightly different migration behavior under non-reducing conditions (Mr 39,000) may be due to intrachain disulfide bonds. After enzymatic cleavage of N-linked carbohydrate residues the apparent molecular weight of the antigen was 29,000. Egp34 is a major cell surface component of HT-29 cells (10(6) molecules per cell). No antigen could be detected in the sera of colorectal cancer patients. A panel of malignant cell lines and normal cells was studied for surface expression of the antigen. 17/17 carcinoma lines of 6 different origins expressed the antigen, whereas 16/16 melanoma, neuroblastoma, sarcoma and lymphoma/leukaemia were unreactive as it was the case for normal fibroblasts and blood cells. Immunoperoxidase staining of frozen tissue sections with HEA125 demonstrated the presence of Egp34 in almost all normal epithelia and tumours derived therefrom. No reactivity with non-epithelial tissues was observed. Undifferentiated carcinomas of various origins homogeneously expressed Egp34. Therefore, HEA125 may become a valuable tool for the immunohistochemical diagnosis of carcinoma. IMAGES: Nature Publishing Group 1987-12 /pmc/articles/PMC2002400/ /pubmed/2449234 Text en https://creativecommons.org/licenses/by/4.0/This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Research Article Moldenhauer, G. Momburg, F. Möller, P. Schwartz, R. Hämmerling, G. J. Epithelium-specific surface glycoprotein of Mr 34,000 is a widely distributed human carcinoma marker. |
title | Epithelium-specific surface glycoprotein of Mr 34,000 is a widely distributed human carcinoma marker. |
title_full | Epithelium-specific surface glycoprotein of Mr 34,000 is a widely distributed human carcinoma marker. |
title_fullStr | Epithelium-specific surface glycoprotein of Mr 34,000 is a widely distributed human carcinoma marker. |
title_full_unstemmed | Epithelium-specific surface glycoprotein of Mr 34,000 is a widely distributed human carcinoma marker. |
title_short | Epithelium-specific surface glycoprotein of Mr 34,000 is a widely distributed human carcinoma marker. |
title_sort | epithelium-specific surface glycoprotein of mr 34,000 is a widely distributed human carcinoma marker. |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2002400/ https://www.ncbi.nlm.nih.gov/pubmed/2449234 |
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