Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver

Lack of sensitivity to alkaline phosphatase when compared with that of glucocorticoid receptor

Michael S. Denison, Lynn M. Vella, Allan B. Okey

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Rat hepatic cytosol was treated with alkaline phosphatase in order to determine if dephosphorylation altered the ability of Ah receptor to bind 2,3,7,8-[3H]tetrachlorodibenzo-p-dioxin (TCDD). Glucocorticoid receptor was studied for comparison. As previously had been shown in other laboratories, treatment of cytosol with purified alkaline phosphatase dramatically reduced the subsequent ability of glucocorticoid receptor to bind hormone. However, alkaline phosphatase had no effect on the ability of Ah receptor to bind [3H]TCDD. If either glucocorticoid receptor or Ah receptor was occupied by its ligand prior to exposure to alkaline phosphatase there was no loss in ligand binding capacity. Crude alkaline phosphatase (containing some protease activity) substantially reduced the ability of glucocorticoid receptor to bind hormone and shifted the sedimentation position of the glucocorticoid receptor from ≈8 S to ≈2 S. Crude alkaline phosphatase did not reduce the ability of Ah receptor to bind [3H]TCDD and did not alter sedimentation of the 9 S [3H]TCDD. Ah receptor complex. Although the Ah receptor appears to be a member of the steroid receptor superfamily, the lack of effect of alkaline phosphatase on Ah receptor (compared to the sensitivity of glucocorticoid receptor) highlights another significant difference in molecular characteristics between the Ah receptor and the receptors for steroid hormones.

Original languageEnglish (US)
Pages (from-to)458-465
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume273
Issue number2
DOIs
StatePublished - 1989
Externally publishedYes

Fingerprint

Aryl Hydrocarbon Receptors
Glucocorticoid Receptors
Liver
Alkaline Phosphatase
Rats
Steroid Receptors
Hormones
Sedimentation
Cytosol
Steroid hormones
Ligands
Peptide Hydrolases
1,4-dioxin
Polychlorinated Dibenzodioxins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver : Lack of sensitivity to alkaline phosphatase when compared with that of glucocorticoid receptor. / Denison, Michael S.; Vella, Lynn M.; Okey, Allan B.

In: Archives of Biochemistry and Biophysics, Vol. 273, No. 2, 1989, p. 458-465.

Research output: Contribution to journalArticle

@article{69f4705dc62c45febecdd6405b540786,
title = "Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver: Lack of sensitivity to alkaline phosphatase when compared with that of glucocorticoid receptor",
abstract = "Rat hepatic cytosol was treated with alkaline phosphatase in order to determine if dephosphorylation altered the ability of Ah receptor to bind 2,3,7,8-[3H]tetrachlorodibenzo-p-dioxin (TCDD). Glucocorticoid receptor was studied for comparison. As previously had been shown in other laboratories, treatment of cytosol with purified alkaline phosphatase dramatically reduced the subsequent ability of glucocorticoid receptor to bind hormone. However, alkaline phosphatase had no effect on the ability of Ah receptor to bind [3H]TCDD. If either glucocorticoid receptor or Ah receptor was occupied by its ligand prior to exposure to alkaline phosphatase there was no loss in ligand binding capacity. Crude alkaline phosphatase (containing some protease activity) substantially reduced the ability of glucocorticoid receptor to bind hormone and shifted the sedimentation position of the glucocorticoid receptor from ≈8 S to ≈2 S. Crude alkaline phosphatase did not reduce the ability of Ah receptor to bind [3H]TCDD and did not alter sedimentation of the 9 S [3H]TCDD. Ah receptor complex. Although the Ah receptor appears to be a member of the steroid receptor superfamily, the lack of effect of alkaline phosphatase on Ah receptor (compared to the sensitivity of glucocorticoid receptor) highlights another significant difference in molecular characteristics between the Ah receptor and the receptors for steroid hormones.",
author = "Denison, {Michael S.} and Vella, {Lynn M.} and Okey, {Allan B.}",
year = "1989",
doi = "10.1016/0003-9861(89)90505-5",
language = "English (US)",
volume = "273",
pages = "458--465",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin in rat liver

T2 - Lack of sensitivity to alkaline phosphatase when compared with that of glucocorticoid receptor

AU - Denison, Michael S.

AU - Vella, Lynn M.

AU - Okey, Allan B.

PY - 1989

Y1 - 1989

N2 - Rat hepatic cytosol was treated with alkaline phosphatase in order to determine if dephosphorylation altered the ability of Ah receptor to bind 2,3,7,8-[3H]tetrachlorodibenzo-p-dioxin (TCDD). Glucocorticoid receptor was studied for comparison. As previously had been shown in other laboratories, treatment of cytosol with purified alkaline phosphatase dramatically reduced the subsequent ability of glucocorticoid receptor to bind hormone. However, alkaline phosphatase had no effect on the ability of Ah receptor to bind [3H]TCDD. If either glucocorticoid receptor or Ah receptor was occupied by its ligand prior to exposure to alkaline phosphatase there was no loss in ligand binding capacity. Crude alkaline phosphatase (containing some protease activity) substantially reduced the ability of glucocorticoid receptor to bind hormone and shifted the sedimentation position of the glucocorticoid receptor from ≈8 S to ≈2 S. Crude alkaline phosphatase did not reduce the ability of Ah receptor to bind [3H]TCDD and did not alter sedimentation of the 9 S [3H]TCDD. Ah receptor complex. Although the Ah receptor appears to be a member of the steroid receptor superfamily, the lack of effect of alkaline phosphatase on Ah receptor (compared to the sensitivity of glucocorticoid receptor) highlights another significant difference in molecular characteristics between the Ah receptor and the receptors for steroid hormones.

AB - Rat hepatic cytosol was treated with alkaline phosphatase in order to determine if dephosphorylation altered the ability of Ah receptor to bind 2,3,7,8-[3H]tetrachlorodibenzo-p-dioxin (TCDD). Glucocorticoid receptor was studied for comparison. As previously had been shown in other laboratories, treatment of cytosol with purified alkaline phosphatase dramatically reduced the subsequent ability of glucocorticoid receptor to bind hormone. However, alkaline phosphatase had no effect on the ability of Ah receptor to bind [3H]TCDD. If either glucocorticoid receptor or Ah receptor was occupied by its ligand prior to exposure to alkaline phosphatase there was no loss in ligand binding capacity. Crude alkaline phosphatase (containing some protease activity) substantially reduced the ability of glucocorticoid receptor to bind hormone and shifted the sedimentation position of the glucocorticoid receptor from ≈8 S to ≈2 S. Crude alkaline phosphatase did not reduce the ability of Ah receptor to bind [3H]TCDD and did not alter sedimentation of the 9 S [3H]TCDD. Ah receptor complex. Although the Ah receptor appears to be a member of the steroid receptor superfamily, the lack of effect of alkaline phosphatase on Ah receptor (compared to the sensitivity of glucocorticoid receptor) highlights another significant difference in molecular characteristics between the Ah receptor and the receptors for steroid hormones.

UR - http://www.scopus.com/inward/record.url?scp=0024429754&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024429754&partnerID=8YFLogxK

U2 - 10.1016/0003-9861(89)90505-5

DO - 10.1016/0003-9861(89)90505-5

M3 - Article

VL - 273

SP - 458

EP - 465

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 2

ER -