@article{GorboulevAkhundovaLuziusetal.1992, author = {Gorboulev, Valentin and Akhundova, Aida and Luzius, Heike and Fahrenholz, Falk}, title = {Molecular cloning of substance P receptor cDNA from guinea-pig uterus}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59293}, year = {1992}, abstract = {A cDNA encoding guinea-pig uterine substance P (SP) receptor has been isolated using the homology screening approach. Northern blot analysis reveals that the corresponding mRNA, of approx. 4.8 kb, is expressed in all tissues tested, but predominantly in the uteri of non-pregnant animals; during pregnancy its expression is reduced. The guinea-pig SP receptor was expressed in COS-7 cells and demonstrated relative Iigand affinity in the order: SP >> neurokinin A > neurokinin B.}, subject = {Biologie}, language = {en} } @article{GorboulevAkhundovaBuechneretal.1992, author = {Gorboulev, Valentin and Akhundova, Aida and B{\"u}chner, Hubert and Fahrenholz, Falk}, title = {Molecular cloning of a new bombesin receptor subtype expressed in uterus during pregnancy}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59304}, year = {1992}, abstract = {The homology screening approach has been used to clone a new member of the guanine-nucleotidebinding-protein-coupled receptor superfamily from guinea pig uterus. The cloned cDNA encodes a 399-amino-acid protein and shows the highest amino acid similarity to members of the bombesin receptor family; 52\% and 47\% similarity to the gastrin-releasing-peptide (GRP) receptor and the neuromedin-B receptor, respectively. Bindingexperiments with the stably transfected LLC-PK1 cell line expressing the new receptor protein confmned the bombesin-like nature of the cloned receptor. The relative order ofligand affinity, GRP = neuromedin C >> neuromedin B, suggests that the cloned cDNA represents the GRP subtype rather than the neuromedin-B subtype of bombesin receptors. Northern-blot analysis of mRNA species from several guinea-pig tissues showed that the mRNA for the new bombesin receptor subtype is expressed mainly in uteri of pregnant animals.}, subject = {Biologie}, language = {en} } @article{GorboulevBuechnerAkhundovaetal.1993, author = {Gorboulev, Valentin and B{\"u}chner, Hubert and Akhundova, Aida and Fahrenholz, Falk}, title = {Molecular cloning and functional characterization of V2 [8-Iysine] vasopressin and oxytocin receptors from a pig kidney cell line (LLC-PK1)}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59311}, year = {1993}, abstract = {No abstract available}, subject = {Biologie}, language = {en} } @article{GruendemannGorboulevGambaryanetal.1994, author = {Gr{\"u}ndemann, Dirk and Gorboulev, Valentin and Gambaryan, Stepan and Veyhl, Maike and Koepsell, Hermann}, title = {Drug excretion mediated by a new prototype of polyspecific transporter}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59327}, year = {1994}, abstract = {CATIO~IC drugs of different types and structures (antihistaminics, antiarrhythmics, sedatives, opiates, cytostatics and antibiotics, for example) are excreted in mammals by epithelial cells of the renal proximal tubules and by hepatocytes in the liver1-4. In the proximal tubules, two functionally disparate transport systems are involved which are localized in the basolateral and luminal plasma membrane and are different from the previously identified neuronal monoamine transporters and A TP-dependent multidrug exporting proteins1-3,5-12. Here we report the isolation of a complementary DNA from rat kidney that encodes a 556-amino-acid membrane protein, OCT1, which has the functional characteristics of organic cation uptake over the basolateral membrane of renal proximal tubules and of organic cation uptake into hepatocytes. OCTl is not homologous to any other known protein and is found in kidney, liver and intestine. As OCTl translocates hydrophobic and hydrophilic organic cations of different structures, it is considered to be a new prolotype of polyspecific transporters that are important for drug elimination.}, subject = {Biologie}, language = {en} }