The Steroid/Thyroid Hormone Receptor Family and Gene Regulation: Proceedings of the 2nd International CBT Symposium Stockholm, Sweden, November 4-5, 1

ISBN-13: 9783034854689 / Angielski / Miękka / 2014 / 371 str.

J. Carlstedt-Duke

Opis

The Second International CBT (Center for Biotechnology) Synposium was held in Stockholm November 4-5 1988 and had the title "The steroid/thyroid hoITIDne receptor family and gene regulation". This meeting contained contributions from most leading laboratories within the field of steroid/thyroid hOITIDne receptors and gave a very exciting perspective on the dynamic development of this i:ntx>rt. ant research field. Today all known steroid hoITIDne receptors have been cloned and sequenced and novel members of this supergene family are constantly being discovered. Sane of these new receptors remain to be characterized regarding the nature of their ligand. Access to probes for steroid receptors has enabled studies on mechanisms of regulation of receptor gene expression. Deletion and II'Altational analysis of steroid receptor cDNAs followed by expression in cells together with suitable reporter genes has yielded a detailed knowledge about the functional significance of the various domains the receptors are composed of. In certain cases, steroid resistance in patients have been shown to be due to point mutations in the corresponding steroid receptor genes resulting in non-functional receptors. The availability of receptor cDNAs also makes it possible to express receptors at high levels in procaryotic and eucaryotic cells. It is e. g. possible to express the DNA-binding domain of the glucocorticoid receptor in E. coli as a fusion protein with protein A which interacts specifically with DNA. Such studies are necessary for production of sufficient quantities of receptors to allow crystallization and X-ray crystallography for detailed structural information.

Spis treści

Receptor Structure.- The Contributions of the Steroid Receptor Superfamily to Development, Physiology and Medicine.- Cooperative Interactions of Steroid Receptors at Their Target Enhancers.- The Association of the Glucocorticoid Receptor with Mr 90,000 Heat Shock Protein and Tubulin.- Functional Domains of Steroid Hormone Receptors.- Thyroid Hormone Receptor Interactions with DNA.- Structure and Intranuclear Dynamics of Androgen Receptors.- Structural Analysis of the Glucocorticoid Receptor Protein.- Speculations on the Role of the 90 kDa Heat Shock Protein in Glucocorticoid Receptor Transport and Function.- Growth Inhibition of CEM Cells by Glucocorticoids: c-myc down Regulation, and the Topology of the Glucocorticoid Receptor.- The Vitamin D3 Receptor and Its Chromosomal Gene.- The Thyroid Hormone Receptor/c-erbA Protein and its Viral Homologue P75gag-v-erbA.- Characterization of the Human Androgen Receptor.- Characterization of New Members of the Steroid Receptor Super-Family.- Gene Regulation by Receptors.- Recriprocal Regulation of Pepck Gene and Gene 33 Transcription by Insulin.- Repression of Gene Expression by Glucocorticoid Receptor through Interference with cAMP Responsive Enhancers.- Steroid Transactivation at a Promoter Organized in a Specifically-Positioned Array of Nucleosomes.- Glucocorticoid Regulated Sorting of Cell Surface Glycoproteins: Evidence for a Glucocorticoid Regulated Trafficking Gene.- Interaction of a Steroid Hormone Receptor with DNA: Molecular Model and Kinetic Analysis.- Receptor Localisation and Distribution.- Neural Gonadal Steroid Receptors and Actions: Chemical Anatomy of the Ventromedial Hypothalamus in Relation to Sexual Differentiation and Sexual Behavior.- Structure, Function and Cellular Distribution of Mammalian Progesterone Receptors.- Cellular Localization of Estrogen and Progestin Receptors in the Macaque Reproductive System.- Do Receptor-Associated Nuclear Proteins Explain Earliest Steps of Steroid Hormone Function?.- Ligand Structure.- Steroid Molecular Structure, Receptor Binding and Hormone Action.- An Analysis of the Steroid Binding Domain of Receptors and of Ligand Structure and Binding Affinity.