4 edition of Affinity labelling and cloning of steroid and thyroid hormone receptors found in the catalog.
Includes bibliographies and index.
|Statement||edited by H. Gronemeyer.|
|Series||Ellis Horwood series in biomedicine,|
|LC Classifications||QP572.S7 A343 1988|
|The Physical Object|
|Pagination||322 p. ;|
|Number of Pages||322|
|LC Control Number||88197299|
in: Gronemeyer H. Affinity Labelling and Cloning of Steroid and Thyroid Hormone Receptors, Ellis Horwood Series in Biomedicine. VCH Publishers, Cited by: The mechanisms of action of thyroid hormone (TH), characterized by multiple physiological activities, proposed over the last 80 years are a reflection of the progression of our knowledge about eukaryotic signalling processes. The cumulative knowledge gained raises the question as to what is so special about the action of this hormone. The discovery in the s that TH receptors Cited by:
Steroid hormone receptors are found in the nucleus, cytosol, and also on the plasma membrane of target cells. They are generally intracellular receptors (typically cytoplasmic or nuclear) and initiate signal transduction for steroid hormones which lead to changes in gene expression over a time period of hours to days. The best studied steroid hormone receptors are members of . Thyroid hormone (T3) receptor (TR) mediates the effects of T3 on organ metabolism and animal development. There are two TR genes, TRα and TRβ, in all vertebrates.
Recently, O'Malley and co-workers used a yeast two-hybrid system to clone a putative factor that enhanced transcriptional activation for steroid hormone receptors, which they called steroid receptor coactivator-1 (SRC-1) (Fig). This protein also associates with several other members of the nuclear hormone receptor superfamily, including TRs. In , the first TRH receptor (TRH-R), later named type 1 TRH receptor, TRH 1, was cloned from a mouse pituitary tumor cDNA library and then orthologous receptors were cloned from a number of different species including rat [5,20], chicken, cow, catostomus commersoni and humans [7,14]. The human TRH receptor, TRHR), is % and %.
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Affinity labelling and cloning of steroid and thyroid hormone receptors. Weinheim, Federal Republic of Germany: VCH Verlagsgesellschaft ; Chichester, England: Ellis Horwood ; New York, NY, USA: Distribution, USA and Canada, VCH Publishers, The selectivity of the labeling process derives from the selective interaction of the affinity probe with the binding site.
The labeling of receptors for hormones generally requires that a very small quantity of protein, generally present as a very minor component in a heterogeneous binding preparation, undergo covalent interaction with the affinity by: 1.
Vitam Horm. ; Affinity labeling of receptors for steroid and thyroid hormones. Katzenellenbogen JA, Katzenellenbogen BS. PMID:Cited by: Affinity labelling of steroid hormone receptors. Gronemeyer H, Govindan MV. Affinity labelling techniques have proved indispensable for the study of reversible biological recognition systems, since they conserve ligand-receptor interaction by covalent by: Affinity labelling of receptors with chemically reactive steroid hormones The chemical structure of steroid derivatives commonly used in electrophilic affinity labelling is Cited by: Abstract.
The possibility that several pathways are involved in the multiplicity of thyroid hormone physiological influences led to searches for the occurrence of T3 extra nuclear receptors. The existence of a direct T3 mitochondrial pathway is now well established. The demonstration that TRα1 mRNA encodes not only a nuclear thyroid hormone receptor Cited by: 3.
In: “Affinity labelling and cloning of steroid and thyroid hormone receptors: techniques, application and functional analysis” (H. Gronemeyer, Ed. Author: H. Gronemeyer, V. Kumar, S. Green, M. Bocquel, L. Tora, M. Meyer, J. Eul, P. Chambon. In: “ Affinity labelling and cloning of steroid and thyroïd hormone receptors: techniques, application and functional analysis ” (H.
Gronemeyer, Ed.), Ellis Horwood Publ. Author: H. Gronemeyer, V. Kumar, S. Green, M. Bocquel, L. Tora, M. Meyer, J. Eul, P. Chambon. steroid Biochem. Vol. 24, No. Printed in Great Britain 1, pp./86 $+ Pergamon Press Ltd AFFINITY-LABELING STEROIDS AS BIOLOGICALLY ACTIVE PROBES OF ANTIGLUCOCORTICOID HORMONE ACTION S.
STONEY SIMONS JR* and PATRICIA A. MILLER Laboratory of Chemistry, NIADDK, National Institutes of Health, Bethesda, MDU.S.A. Summaryhe role of the glucocorticoid receptor Cited by: In this book Gronemeyer brings together a wealth of information on the affinity labelling and cloning of steroid and thyroid receptors transcriptional regulatory proteins which belong to subgroups of a superfamily of nuclear receptor genes.
Specific affinity-labelling reagents for steroid receptors have become valuable tools for the detection, isolation and characterization. We have cloned a novel member of the nuclear receptor superfamily.
The cDNA of clone 29 was isolated from a rat prostate cDNA library and it encodes a protein of amino acid residues with a calculated molecular weight of by: Steroid hormone receptor coactivators are involved in enhancing the transcriptional signal of the steroid hormone receptors following ligand binding.
Steroid receptor coactivator-1 (SRC1), the founding member of the SRC family (also called the p family, based on their similar sizes of kDa), was originally identified as an interacting protein with the progesterone receptor. Work on “receptors” for other steroid hormones progressed in parallel, mainly by injecting the labeled hormone to the intact animal, preparing tissue extracts (chick oviduct for progesterone, rat uterus for estrogens, prostate for androgens, liver for glucocorticoids) and looking for bound steroid with tedious procedures such as autoradiography Cited by: 9.
Affinity labelling and cloning of steroid and thyroid hormone receptors. VCH/Ellis Horwood, Chichester, (). Affinity labelling of a partially purified ecdysteroid receptor with a bromoacetylated OH-ecdysone derivative.
Gronemeyer, H. () Affinity labelling and cloning of steroid and thyroid hormone receptors. Horwood, Chichester, UK Google Scholar Mendel, D.B. & Orti, E.
() Isoform composition and stoichiometry of the~ 90 kDa heat shock protein associated with glucocorticoid by: 2. These studies report the characterization of two new TRβ isoforms, which are generated by alternative mRNA splicing and are expressed in tissue-specific patterns which alter with changes in thyroid status.
TRβ3 is a novel receptor, and TRδβ3 is a potent dominant negative antagonist that binds T 3 with high affinity. We demonstrate that TR2 orphan receptor (TR2) may induce transactivation activities via an AGGTCA-like-direct-repeat-4 consensus thyroid hormone response element (DR4-TRE) system.
TR2 showed a slightly greater binding affinity than thyroid hormone receptor α1 (TRα1)/retinoid X receptor α (RXRα) heterodimer with Kds nM and nM, Cited by: 1. Author(s): Gronemeyer,H(Hinrich) Title(s): Affinity labelling and cloning of steroid and thyroid hormone receptors/ edited by H.
Gronemeyer. Tipton Department o Biochemistry f Trinity College Dublin, Ireland Affinity Labelling and Cloning of Steroid and Thyroid Hormone Receptors edited by H. Gronemeyer. VCH Publishers, New York/Weinheim,pp., ISBN 0. We have identified a region within the steroid binding domain of the mouse estrogen receptor that is required for both receptor dimerization and high affinity DNA binding.
Analysis of sequences in this region revealed that a heptad repeat of hydrophobic residues was conserved in all members of the nuclear receptor superfamily. Single amino acid substitutions of residues Cited by:. Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor.
Cell. Mar 23; 60 (6)– Danielian PS, White R, Lees JA, Parker MG. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors.In the preceding paper we reported the synthesis of affinity matrices containing 3,5,3'-triiodo-L-thyronine (T 3) linked via its amino group and the diactivated ester of glutaric acid to the free amino groups of report describes the optimization of this system for the purification of the intranuclear thyroid hormone by: Thus, receptors for steroid hormones, as well as for thyroid hormones and retinoic acid, differ from the receptors described in previous chapters, which are located in the plasma membrane and utilize a signal transduction process (second messenger) to deliver the regulatory signal within the responsive by: