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Nuclear Triiodothyronine Receptor in Differentiating Preadipocytes Cloned from Obese and Lean Mice^*

Laboratoire de Biochimie Medicate and Groupe U 38, INSERM, Faculté de Médecine 13385 Marseille Cedex 5, France

Address requests for reprints to: Dr. Alain Anselmet, Lab de Biochimie Medicale, Universite d’Aix-Marseille, Faculte de Medicine, 27 Boulevard Jean-Moulin, 13385 Marseille Cédex 5, France.

Abstract

The nuclear T₃ receptor was characterized in two T₃-responsive preadipocyte cell lines cloned from the epididymal fat pads of ob/ob adult mice (ob 17 cells) and their lean counterpart (HGFu cells). Isolated nuclei from confluent or differentiating cells bound [¹²⁵I]T₃ to one class of high affinity sites exhibiting kinetic properties, stereospecificity, and salt extractibility of the nuclear T₃ receptor. The solubilized T₃ binding sites behave like the hepatic nuclear T₃ receptor considering physicochemical and DNA binding properties. At confluence, no significant difference could be detected in equilibrium apparent affinity constant (K_a) and maximum binding capacity (MBC) for T₃ whether nuclei were prepared from cells originating from ob/ob mice [K_a: 1.7 ± (SE) 0.5 x 10¹⁰ M^–1; MBC: 432 ± 29 fmol/mg DNA] or from lean mice (K_a: 1.6 ± 0.2 x 10¹⁰ M^–1; MBC: 487 ± 39 fmol/mg DNA). MBC values were in the range found in several T₃-responsive tissues. This suggests that the primary defect in ob/ob mice is probably not at the level of the nuclear T₃ receptor. Furthermore, during differentiation into adipose cells in both cell series, and roughly paralleling the amplifying effect of T₃ on several lipogenic enzymes in the course of their development, the nuclear T₃ receptor concentration significantly increased, attaining about twice the initial values after completion of the differentiation without any significant change in the affinity for T₃. (Endocrinology 114: 450, 1984)

Footnotes

^* This work was supported in part by CNRS (LA 178 and ATP N° 141).

Received May 23, 1983.

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