Literature DB >> 496915

Changes in the sensitivity of chick fibroblasts to Ricinus lectin (RCA I) toxicity in relation to the stage of embryo development.

B Bernard, M Aubery, R Bourrillon.   

Abstract

The toxic effect of Ricinus lectin RCA I, as estimated by the inhibition of [3H]leucine incorporation, was investigated on chick-embryo fibroblasts at different stages of development. There appeared to be a differential susceptibility of chick-embryo fibroblasts to lectin RCA I. Fibroblasts from 16-day embryos were the most sensitive to its toxic effect in terms of both concentration and time, and cells from 8-day embryos were the least sensitive. This differential sensitivity to the toxic effect of lectin RCA I was closely related to the binding of the lectin: fibroblasts from 16-day embryos had more binding sites (1.5 x 10(7)/cell) with a high affinity than did 12-day (0.45 x 10(7)/cell) or 8-day embryos (0.2 x 10(7)/cell). Studies on the specificity and the removal of bound lectin RCA I by D-galactose indicated that the lectin binding was necessary but not sufficient in itself to cause the toxic effect and that the lectin needed to enter the cells in order to be toxic. The amount of lectin RCA I needed to induce a 50-60% toxicity enters fibroblasts of 16-day embryos more rapidly than those of 12- and 8-day embryos.

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Year:  1979        PMID: 496915      PMCID: PMC1161231          DOI: 10.1042/bj1820033

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  17 in total

1.  Mechanism of cell entry and toxicity of an affinity- purified lectin from Ricinus communis and its differential effects on normal and virus-transformed fibroblasts.

Authors:  G L Nicolson; M Lacorbiere; T R Hunter
Journal:  Cancer Res       Date:  1975-01       Impact factor: 12.701

2.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

3.  The interaction of Ricinus communis agglutinin with normal and tumor cell surfaces.

Authors:  G L Nicolson; J Blaustein
Journal:  Biochim Biophys Acta       Date:  1972-05-09

4.  Cell surface changes occurring during sea urchin embryonic development monitored by quantitative agglutination with plant lectins.

Authors:  S W Krach; A Green; G L Nicolson; S B Oppenheimer
Journal:  Exp Cell Res       Date:  1974-03-15       Impact factor: 3.905

5.  Different biological properties of the two constituent peptide chains of ricin, a toxic protein inhibiting protein synthesis.

Authors:  S Olsnes; A Pihl
Journal:  Biochemistry       Date:  1973-07-31       Impact factor: 3.162

6.  Protein labeling by acetylation.

Authors:  I R Miller; H Great
Journal:  Biopolymers       Date:  1972       Impact factor: 2.505

7.  Toxic proteins inhibiting protein synthesis.

Authors:  S Olsnes
Journal:  Naturwissenschaften       Date:  1972-11

8.  Interactions of embryonic and fetal neural retina cells with carbohydrate-binding phytoagglutinins: cell surface changes with dfferentiation.

Authors:  S J Kleinschuster; A A Moscona
Journal:  Exp Cell Res       Date:  1972-02       Impact factor: 3.905

9.  Structure and toxicity of pure ricinus agglutinin.

Authors:  E Saltvedt
Journal:  Biochim Biophys Acta       Date:  1976-12-21

10.  Plaque formation and isolation of pure lines with poliomyelitis viruses.

Authors:  R DULBECCO; M VOGT
Journal:  J Exp Med       Date:  1954-02       Impact factor: 14.307

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  2 in total

1.  Structure and stability of Ricinus communis haemagglutinin.

Authors:  J P Frénoy; A T Tran; R Bourrillon
Journal:  Biochem J       Date:  1986-11-15       Impact factor: 3.857

2.  Side effects of Ricinus lectin (RCA 120) on nucleic acid synthesis in chick embryo fibroblasts.

Authors:  B Bernard; C Berjonneau; P Codogno; J Font; M Aubery
Journal:  Experientia       Date:  1983-02-15
  2 in total

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