Differential response of adherent and unanchored melanoma cells to bromodeoxyuridine evidenced by specific lectin‐binding protein changes

The possible differential response of adherent and nonadherent cells of the same tumor type to pyrimidine analogues has been investigated. We show that bromodeoxyuridine (BUdR) increases interactions of attached cells with their substrate without markedly affecting the cell adhesion properties of th...

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Veröffentlicht in:International journal of cancer 1989-05, Vol.43 (5), p.841-844
Hauptverfasser: Rieber, Manuel, Rieber, Mary S., Urbina, Cecilia, Lira, Renée
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container_issue 5
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container_title International journal of cancer
container_volume 43
creator Rieber, Manuel
Rieber, Mary S.
Urbina, Cecilia
Lira, Renée
description The possible differential response of adherent and nonadherent cells of the same tumor type to pyrimidine analogues has been investigated. We show that bromodeoxyuridine (BUdR) increases interactions of attached cells with their substrate without markedly affecting the cell adhesion properties of the same cells when these are not anchored. However, evidence for an adhesion‐independent response of both cell types to BUdR has been obtained with lectin binding assays using 125I‐labelled Lens culinaris agglutinin (LCA). This revealed a greatly increased binding of LCA to a large glycoconjugate in all cultures exposed to the halogenated pyrimidine. Attachment‐dependent effects of BUdR were manifested in flattened cells by a greater LCA‐binding to a 240‐kDa protein and by increased interaction of 125labelled wheat‐germ agglutinin (WGA) with a 200‐kDa protein and a large glycoconjugate sharply defined in electrophoresis. Although both tumor cell aggregates and anchored cells exhibit detectable responses to pyrimidine analogues such as BUdR, the corresponding effects are thus manifested unequally in cells with different adhesion properties.
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We show that bromodeoxyuridine (BUdR) increases interactions of attached cells with their substrate without markedly affecting the cell adhesion properties of the same cells when these are not anchored. However, evidence for an adhesion‐independent response of both cell types to BUdR has been obtained with lectin binding assays using 125I‐labelled Lens culinaris agglutinin (LCA). This revealed a greatly increased binding of LCA to a large glycoconjugate in all cultures exposed to the halogenated pyrimidine. Attachment‐dependent effects of BUdR were manifested in flattened cells by a greater LCA‐binding to a 240‐kDa protein and by increased interaction of 125labelled wheat‐germ agglutinin (WGA) with a 200‐kDa protein and a large glycoconjugate sharply defined in electrophoresis. 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We show that bromodeoxyuridine (BUdR) increases interactions of attached cells with their substrate without markedly affecting the cell adhesion properties of the same cells when these are not anchored. However, evidence for an adhesion‐independent response of both cell types to BUdR has been obtained with lectin binding assays using 125I‐labelled Lens culinaris agglutinin (LCA). This revealed a greatly increased binding of LCA to a large glycoconjugate in all cultures exposed to the halogenated pyrimidine. Attachment‐dependent effects of BUdR were manifested in flattened cells by a greater LCA‐binding to a 240‐kDa protein and by increased interaction of 125labelled wheat‐germ agglutinin (WGA) with a 200‐kDa protein and a large glycoconjugate sharply defined in electrophoresis. 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subjects Animals
Antineoplastic agents
Biological and medical sciences
Bromodeoxyuridine - pharmacology
Cell Line
General aspects
Medical sciences
Melanoma, Experimental - immunology
Melanoma, Experimental - pathology
Mice
Molecular Weight
Pharmacology. Drug treatments
Receptors, Mitogen - analysis
Receptors, Mitogen - drug effects
Receptors, Mitogen - isolation & purification
Tumor Cells, Cultured - cytology
Tumor Cells, Cultured - drug effects
Tumor Cells, Cultured - immunology
title Differential response of adherent and unanchored melanoma cells to bromodeoxyuridine evidenced by specific lectin‐binding protein changes
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