Thyroid hormone binding to putative nuclear receptors in human mononuclear blood cells.

Abstract

Nuclear protein extracts from mononuclear cells in normal subjects, subjects with the clinical syndrome of thyroid hormone resistance and cultured B lymphocytes bound thyroxine (T4) Ka; 1 . 3-3 . 5 X 10(9) m-1) and triiodothyronine (T3) (Ka; 1 . 2-3 . 9 X 10(9) m-1) with similar affinities. When an extra wash step was introduced, the maximum specific binding of T4 and T3 was reduced by 75% and binding was abolished by three washes. These data suggest binding is to a serum protein contaminant present in the mononuclear cell preparation.

• Authors: G F Maberly, C J Eastman, H C Smith, K Waite, T J Wilke
• Journal: The Australian journal of experimental biology and medical science (Aust J Exp Biol Med Sci) Vol. 60 Issue Pt 1 Pg. 113-5 (Feb 1982) ISSN: 0004-945X [Print] Australia
• PMID: 6284102 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Receptors, Cell Surface
• Receptors, Thyroid Hormone
• Triiodothyronine
• Thyroxine

Topics

• Adolescent
• Adult
• Cell Nucleus (metabolism)
• Female
• Humans
• Lymphocytes (metabolism, ultrastructure)
• Male
• Receptors, Cell Surface (metabolism)
• Receptors, Thyroid Hormone
• Thyroid Diseases (blood)
• Thyroxine (metabolism)
• Triiodothyronine (metabolism)