1992
DOI: 10.1016/0014-5793(92)81479-6
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Receptor mediated mineralocorticoid action in alga cell mutants

Abstract: The multiplication of Clr/nr~~&rt~orfns cells can be arrcstcd by the spirolactonc derivative RU 26752 and this is li~lly rcversiblc by the natural hormone nldosteronc. Continuous growth in the prcscnce of RU 26752 led to the isolation of a population subsequently resistant to the action of mincralocortoid analogucs. due possibly to the sclcclion of mutant cells. lmmunopbotochcmical cvidemx is provided Ibr a 52 kDa protein that possesses functional steroid and DNA binding domains. Alga cells thcrcrorc appear to… Show more

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Cited by 10 publications
(12 citation statements)
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“…RPE cytosol, equili brated with 20 nM 3H-RU 26752, was incu bated with 10 pg rabbit anti-MCR (+) or control (-) IgG, and the quantity precipi tated in the presence of goat antirabbit IgGagarose was determined in triplicate. The results are expressed as cpm/mg protein ± SE [16][17][18][26][27][28], The change in the conformation of the steroid-receptor complex in the presence of heat and/or high salt is a uni versal feature of the DNA-binding domain of the steroid receptor superfamily [1][2][3], Data in figure 3 show a three fold increase in the amount of radioactivity that could be eluted from DNA cellulose when 3H-RU 26752-RPE cytosol was allowed to stand at 25 °C for 45 min above the control level at 4°C. The radioactivity increased from 222 cpm/mg protein at 4°C to 642 cpm/mg protein after 45 min at 25°C.…”
Section: Resultsmentioning
confidence: 99%
“…RPE cytosol, equili brated with 20 nM 3H-RU 26752, was incu bated with 10 pg rabbit anti-MCR (+) or control (-) IgG, and the quantity precipi tated in the presence of goat antirabbit IgGagarose was determined in triplicate. The results are expressed as cpm/mg protein ± SE [16][17][18][26][27][28], The change in the conformation of the steroid-receptor complex in the presence of heat and/or high salt is a uni versal feature of the DNA-binding domain of the steroid receptor superfamily [1][2][3], Data in figure 3 show a three fold increase in the amount of radioactivity that could be eluted from DNA cellulose when 3H-RU 26752-RPE cytosol was allowed to stand at 25 °C for 45 min above the control level at 4°C. The radioactivity increased from 222 cpm/mg protein at 4°C to 642 cpm/mg protein after 45 min at 25°C.…”
Section: Resultsmentioning
confidence: 99%
“…This procedure increases affinity of Chfamydomonas protein for DNA cellulose [22,23], in close similarity with the animal steroid receptors ( Fig. 1; [29]).…”
Section: Receptor-mediated Transactivation Of Genesmentioning
confidence: 95%
“…R-5020 can also be covalently linked to the carrier in alga by a photochemical procedure, further suggesting structural and functional kinship with the ligand binding domain in animal steroid receptors [22,23].…”
Section: Receptor-mediated Transactivation Of Genesmentioning
confidence: 99%
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