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Peroxisome proliferators and T3 operate by way of distinct receptors
Author(s) -
Castelein Hilde,
Declercq Peter E.,
Mannaerts Guy P.,
Baes Myriam I.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80474-9
Subject(s) - peroxisome proliferator , peroxisome , receptor , chemistry , microbiology and biotechnology , biochemistry , biology
Peroxisome proliferators and thyroid hormones have a number of common metabolic effects. The possibility that the signal transduction pathways of both groups of effectors converge at the receptor level was investigated. It was shown that T3, specifically bound to the rat thyroid β‐receptor, was not displaced to a significant extent by ciprofibrate or bezafibrate. No specific binding of T3 to the mouse peroxisome proliferator activated receptor could be demonstrated. In transactivation experiments peroxisome proliferators were unable to activate the thyroid receptor and T3 did not activate a chimeric receptor containing the ligand binding domain of the peroxisome proliferator activated receptor. It is concluded that peroxisome proliferators and thyroid hormone do not cross‐react at the level of their nuclear receptors.