Binding of oxygenated cholesterol metabolites to antiestrogen binding sites from chicken liver

P. R. Murphy; W. C. Breckenridge; C. B. Lazier

doi:10.1016/S0006-291X(85)80012-7

Binding of oxygenated cholesterol metabolites to antiestrogen binding sites from chicken liver

P. R. Murphy, W. C. Breckenridge, C. B. Lazier

Medicine

Medicine

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20 Citas (Scopus)

Resumen

High affinity (K_D 2-4 nM) binding sites (AEBS) for the triphenylethylene antiestrogen, tamoxifen, are found in chicken liver cytosol preparations. These sites exhibit affinity for triphenylethylene derivatives typical of those reported for AEBS in other systems. Although steroids and cholesterol do not compete for the sites, certain oxygenated cholesterol metabolites, particularly 7-ketocholesterol, do so. Hot ethanol extracts of chicken and human serum contain AEBS inhibitory activity. This activity is chromatographically heterogeneous, but a sterol-containing fraction has been isolated in which the 7-ketocholesterol concentration can account for the AEBS inhibitory activity of the fraction.

Idioma original	English
Páginas (desde-hasta)	786-792
Número de páginas	7
Publicación	Biochemical and Biophysical Research Communications
Volumen	127
N.º	3
DOI	https://doi.org/10.1016/S0006-291X(85)80012-7
Estado	Published - mar. 29 1985

Nota bibliográfica

Funding Information:
ACKNOWLEDGMENTS: Grant support was from the Medical Research Council of Canada and the National Cancer Institute of Canada. Technical help by Kim Lonergan is gratefully acknowledged.

ASJC Scopus Subject Areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Binding of oxygenated cholesterol metabolites to antiestrogen binding sites from chicken liver",

abstract = "High affinity (KD 2-4 nM) binding sites (AEBS) for the triphenylethylene antiestrogen, tamoxifen, are found in chicken liver cytosol preparations. These sites exhibit affinity for triphenylethylene derivatives typical of those reported for AEBS in other systems. Although steroids and cholesterol do not compete for the sites, certain oxygenated cholesterol metabolites, particularly 7-ketocholesterol, do so. Hot ethanol extracts of chicken and human serum contain AEBS inhibitory activity. This activity is chromatographically heterogeneous, but a sterol-containing fraction has been isolated in which the 7-ketocholesterol concentration can account for the AEBS inhibitory activity of the fraction.",

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AU - Breckenridge, W. C.

AU - Lazier, C. B.

N1 - Funding Information: ACKNOWLEDGMENTS: Grant support was from the Medical Research Council of Canada and the National Cancer Institute of Canada. Technical help by Kim Lonergan is gratefully acknowledged.

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AB - High affinity (KD 2-4 nM) binding sites (AEBS) for the triphenylethylene antiestrogen, tamoxifen, are found in chicken liver cytosol preparations. These sites exhibit affinity for triphenylethylene derivatives typical of those reported for AEBS in other systems. Although steroids and cholesterol do not compete for the sites, certain oxygenated cholesterol metabolites, particularly 7-ketocholesterol, do so. Hot ethanol extracts of chicken and human serum contain AEBS inhibitory activity. This activity is chromatographically heterogeneous, but a sterol-containing fraction has been isolated in which the 7-ketocholesterol concentration can account for the AEBS inhibitory activity of the fraction.

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Binding of oxygenated cholesterol metabolites to antiestrogen binding sites from chicken liver

Resumen

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ASJC Scopus Subject Areas

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