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Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation

A plastic adherent variant line (ESb-M) of a highly invasive and metastatic murine T cell lymphoma (ESb) was found to have lost its metastatic potential while still being tumorigenic in normal syngeneic hosts. The variant retained most of its ESb-derived antigenic and biochemical characteristics but...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1983
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2186915/
https://www.ncbi.nlm.nih.gov/pubmed/6848622
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description A plastic adherent variant line (ESb-M) of a highly invasive and metastatic murine T cell lymphoma (ESb) was found to have lost its metastatic potential while still being tumorigenic in normal syngeneic hosts. The variant retained most of its ESb-derived antigenic and biochemical characteristics but differed at binding sites for certain lectins with specificity for terminal N-acetylgalactosamine residues. Whereas such sites were masked by sialic acid on metastatic ESb cells, they became unmasked on the adherent variant line. Metastatic revertants of ESb-M cells did not express the respective lectin receptor sites because these were again masked by sialic acid. It is suggested that the masking of specific lectin receptors sites on the tumor cell surface is of crucial importance for metastatis. If freely exposed, these sites may change adherence characteristics of the cells possibly not only in vitro (to plastic) but also in vivo.
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spelling pubmed-21869152008-04-17 Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation J Exp Med Articles A plastic adherent variant line (ESb-M) of a highly invasive and metastatic murine T cell lymphoma (ESb) was found to have lost its metastatic potential while still being tumorigenic in normal syngeneic hosts. The variant retained most of its ESb-derived antigenic and biochemical characteristics but differed at binding sites for certain lectins with specificity for terminal N-acetylgalactosamine residues. Whereas such sites were masked by sialic acid on metastatic ESb cells, they became unmasked on the adherent variant line. Metastatic revertants of ESb-M cells did not express the respective lectin receptor sites because these were again masked by sialic acid. It is suggested that the masking of specific lectin receptors sites on the tumor cell surface is of crucial importance for metastatis. If freely exposed, these sites may change adherence characteristics of the cells possibly not only in vitro (to plastic) but also in vivo. The Rockefeller University Press 1983-01-01 /pmc/articles/PMC2186915/ /pubmed/6848622 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation
title Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation
title_full Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation
title_fullStr Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation
title_full_unstemmed Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation
title_short Metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation
title_sort metastatic potential severely altered by changes in tumor cell adhesiveness and cell-surface sialylation
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2186915/
https://www.ncbi.nlm.nih.gov/pubmed/6848622