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

Research output: Contribution to journal › Article › peer-review

20 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	786-792
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	127
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(85)80012-7
Publication status	Published - Mar 29 1985

Bibliographical note

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

Access to Document

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

Cite this

@article{df35057e1d01449c8bb6f3a21bf226b2,

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.",

author = "Murphy, {P. R.} and Breckenridge, {W. C.} and Lazier, {C. B.}",

note = "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.",

year = "1985",

month = mar,

day = "29",

doi = "10.1016/S0006-291X(85)80012-7",

language = "English",

volume = "127",

pages = "786--792",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Binding of oxygenated cholesterol metabolites to antiestrogen binding sites from chicken liver

AU - Murphy, P. R.

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.

PY - 1985/3/29

Y1 - 1985/3/29

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=0021839478&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021839478&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(85)80012-7

DO - 10.1016/S0006-291X(85)80012-7

M3 - Article

C2 - 3985957

AN - SCOPUS:0021839478

SN - 0006-291X

VL - 127

SP - 786

EP - 792

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

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

Abstract

Bibliographical note

ASJC Scopus Subject Areas

Access to Document

Other files and links

Fingerprint

Cite this