Searchable abstracts of presentations at key conferences in endocrinology

ea0026p368 | Signal transduction | ECE2011

Research resource for analysing functional data of glycoprotein hormone receptors: novel tools to gain deeper insights into molecular mechanisms

Kreuchwig A , Kleinau G , Kreuchwig F , Worth C L , Krause G

The sequence–structure–function-analysis of glycoprotein hormone receptors (SSFA-GPHR) database provides a comprehensive set of mutation data for the glycoprotein hormone receptors (covering the lutropin – (LHCGR), the follitropin (FSHR) and the thyrotropin receptor (TSHR)). Numerous databases present functional information along with pooled data from various public resources, but tools to analyse the molecular effects of genetic variations are as yet poorly pro...

ea0029p1007 | Male Reproduction | ICEECE2012

The homologous hormones lutropin and choriogonadotropin are interacting differently with the LH/CG receptor

Grzesik P. , Teichmann A. , Kreuchwig A. , Furkert J. , Rutz C. , Wiesner B. , Schulein R. , Gromoll J. , Krause G.

Activation of the human LH/CG receptor (LH/CGR) by lutropin (LH) and choriogonadotropin (CG) is essential in the human reproduction. Deletion of the Exon10 (LH/CGR-delExon10) resulting in a lack of 27 amino acids within the extracellular hinge-region of LH/CGR causes Leydig cell hypoplasia type II. To clarify why this deletion impairs LH but not CG action, we investigated the molecular determinants of LH/CGR activation elucidating the different behaviour of both hormones.<...

ea0026p369 | Signal transduction | ECE2011

Different and common transmembrane activation mechanisms between glycoprotein hormone receptors and other G-protein coupled receptors

Hoyer I , Kleinau G , Haas A K , Kreuchwig A , Grzesik P , Worth C L , Schuelein R , Krause G

The aim of our study is to identify signalling sensitive residue positions of the glycoprotein hormone receptors (GPHR), especially the thyrotropin receptor (TSHR) on the transmembrane helices (TMH) 5 and 6, knowing to be involved in GPCR activation. We performed modelling driven site-directed mutagenesis to pinpoint residues that are responsible for stabilization of active and inactive conformations of the TSHR.We highlight two amino acids that are high...