Binding of thyroxine to human plasma low density lipoprotein through specific interaction with apolipoprotein B (apoB-100)

Biochimie
S BenvengaJ Robbins

Abstract

Human plasma low density lipoprotein (LDL), which binds 0.2% of plasma T4, was shown to interact with the hormone through its protein moiety, apolipoprotein B-100. LDL and LDL2, the major subfraction of LDL, were found to have 3 equivalent binding sites for T4 with Ka = 2.5 x 10(6) M-1. Photoaffinity labeling of LDL with inner ring-labeled [125I]T4, followed by SDS-PAGE or agarose-SDS-PAGE of the labeled products, revealed that apoB-100 and its proteolytic cleavage products, apoB-74 and apoB-26, bound [125I]T4. In the presence of 1 or 10 microM T4, labeling was decreased in 7 separate experiments by 40-53% or 65-86%, respectively, consistent with a Ka of approximately 10(6) M-1. Binding of T4 to apoB-100 associated with VLDL was also demonstrated by photoaffinity labeling. The observed thyroid hormone binding property of lipid-complexed apoB-100 and the knowledge that receptors for the apolipoprotein exist in various tissues suggest a possible physiological role in thyroid hormone transport.

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Citations

Aug 24, 2002·Thyroid : Official Journal of the American Thyroid Association·Salvatore BenvengaFrancesco Trimarchi
Jan 1, 1994·Thyroid : Official Journal of the American Thyroid Association·S BenvengaJ Robbins
Aug 1, 1997·Thyroid : Official Journal of the American Thyroid Association·S Benvenga
Aug 1, 1993·Trends in Endocrinology and Metabolism : TEM·S Benvenga, J Robbins
Feb 23, 2010·Journal of Lipid Research·Juan GuevaraNatalia Valentinova Guevara
Apr 20, 2019·Frontiers in Endocrinology·Barbara K Stepien, Wieland B Huttner
May 1, 1992·The American Journal of Physiology·P J Babin

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