Biomaterial Database

Nuclear receptors for L-triiodothyronine in quail liver. 1984

R T Weirich, and F M McNabb

Binding studies were conducted using in vitro-labeled quail liver nuclei to identify and characterize receptors for L-triiodothyronine (T3). Saturation binding experiments were analyzed by Scatchard analysis and indicated a single class of high-affinity, limited-capacity T3 binding sites. These receptors exhibited binding specificity as demonstrated by competition experiments between labeled T3 and unlabeled thyroid hormones or hormone analogs. Binding specificity was virtually identical in quail and rat liver nuclei. Thus, apparent differences between mammals and birds, in regard to the biological potency of T4 versus T3, are not apparent at the level of the nuclear T3 receptor.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008099	Liver	A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.	Livers
D008297	Male		Males
D011784	Quail	Common name for two distinct groups of BIRDS in the order GALLIFORMES: the New World or American quails of the family Odontophoridae and the Old World quails in the genus COTURNIX, family Phasianidae.	Quails
D011956	Receptors, Cell Surface	Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.	Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D011988	Receptors, Thyroid Hormone	Specific high affinity binding proteins for THYROID HORMONES in target cells. They are usually found in the nucleus and regulate DNA transcription. These receptors are activated by hormones that leads to transcription, cell differentiation, and growth suppression. Thyroid hormone receptors are encoded by two genes (GENES, ERBA): erbA-alpha and erbA-beta for alpha and beta thyroid hormone receptors, respectively.	Diiodotyrosine Receptors,Receptors, Diiodotyrosine,Receptors, Thyroxine,Receptors, Triiodothyronine,T3 Receptors,T4 Receptors,Thyroid Hormone Receptors,Thyroxine Receptors,Triiodothyronine Receptors,DIT Receptors,Diiodotyrosine Receptor,MIT Receptors,Monoiodotyrosine Receptors,Receptors, DIT,Receptors, MIT,Receptors, Monoiodotyrosine,Receptors, T3,Receptors, T4,T3 Receptor,T4 Receptor,Thyroid Hormone Receptor,Thyroxine Receptor
D002467	Cell Nucleus	Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)	Cell Nuclei,Nuclei, Cell,Nucleus, Cell
D003370	Coturnix	A genus of BIRDS in the family Phasianidae, order GALLIFORMES, containing the common European and other Old World QUAIL.	Japanese Quail,Coturnix japonica,Japanese Quails,Quail, Japanese,Quails, Japanese
D003918	Dextrothyroxine	The dextrorotary isomer of the synthetic THYROXINE.	D-Thyroxine,Dextrothyroxine Sodium,Choloxin,D-T4 Thyroid Hormone,Sodium Dextrothyroxine,D Thyroxine
D000375	Aging	The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time.	Senescence,Aging, Biological,Biological Aging