How specific are nuclear "receptors" for thyroid hormones?
The presence of "high-affinity-saturable" binding sites for thyroid hormones of similar characteristics not only in isolated nuclei but in all the major extranuclear cellular components, as well as the failure of cytosol to promote nuclear binding, invalidates the analogy with steroid hormone receptors and necessitates a more critical assessment of the physiological relevance of current approaches to binding of thyroid hormone in vitro nuclear preparations.
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002462:Cell Membrane / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism*; D002843:Chromatin / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000648:ultrastructure; D008862:Microsomes, Liver / Q000378:metabolism; D008930:Mitochondria, Liver / Q000378:metabolism; D051381:Rats; D011956:Receptors, Cell Surface; D013963:Thyroid Hormones / Q000378:metabolism*; D014284:Triiodothyronine / Q000378:metabolism
D002843:Chromatin; D011956:Receptors, Cell Surface; D013963:Thyroid Hormones; D014284:Triiodothyronine