0000000000446852

AUTHOR

Malin C. Lagerström

showing 4 related works from this author

The evolutionary history and tissue mapping of GPR123: specific CNS expression pattern predominantly in thalamic nuclei and regions containing large …

2007

The Adhesion family of G protein-coupled receptors (GPCRs) includes 33 receptors and is the second largest GPCR family. Most of these proteins are still orphans and fairly little is known of their tissue distribution and evolutionary context. We report the evolutionary history of the Adhesion family protein GPR123 as well as mapping of GPR123 mRNA expression in mouse and rat using in situ hybridization and real-time PCR, respectively. GPR123 was found to be well conserved within the vertebrate lineage, especially within the transmembrane regions and in the distal part of the cytoplasmic tail, containing a potential PDZ binding domain. The real-time PCR data indicates that GPR123 is predomin…

Central Nervous SystemMaleModels MolecularNeuronal signal transductionPDZ domainGene ExpressionContext (language use)In situ hybridizationBiologyBiochemistryReceptors G-Protein-CoupledMiceCellular and Molecular NeuroscienceAnimalsHumansTissue DistributionRNA MessengerNeural Cell Adhesion MoleculesIn Situ HybridizationPhylogenyG protein-coupled receptorReverse Transcriptase Polymerase Chain ReactionPyramidal CellsSubiculumRatsCell biologySignal transductionSequence AlignmentNeuroscienceBinding domainJournal of Neurochemistry
researchProduct

Cloning, tissue distribution, pharmacology and three-dimensional modelling of melanocortin receptors 4 and 5 in rainbow trout suggest close evolution…

2004

The rainbow trout (Oncorhynchus mykiss) is one of the most widely used fish species in aquaculture and physiological research. In the present paper, we report the first cloning, 3D (three-dimensional) modelling, pharmacological characterization and tissue distribution of two melanocortin (MC) receptors in rainbow trout. Phylogenetic analysis indicates that these receptors are orthologues of the human MC4 and MC5 receptors. We created 3D molecular models of these rainbow trout receptors and their human counterparts. These models suggest greater divergence between the two human receptors than between their rainbow trout counterparts. The pharmacological analyses demonstrated that ACTH (adreno…

Models Molecularendocrine systemmedicine.medical_specialtyanimal structuresanimal diseasesMolecular Sequence DataAdrenocorticotropic hormoneBiologyKidneyBinding Competitivedigestive systemBiochemistryCell LineEvolution MolecularInternal medicinemedicineAnimalsHumansAmino Acid SequenceCloning MolecularBinding siteReceptorMolecular BiologyPhylogenyPharmacologyCloningBinding Sitesurogenital systemReceptors MelanocortinSequence Analysis DNACell BiologyCell biologyZincEndocrinologyReceptors CorticotropinOrgan SpecificityHypothalamusHormone receptorOncorhynchus mykissReceptor Melanocortin Type 4Rainbow troutMelanocortinSequence AlignmentResearch ArticleBiochemical Journal
researchProduct

High affinity agonistic metal ion binding sites within the melanocortin 4 receptor illustrate conformational change of transmembrane region 3.

2003

We created a molecular model of the human melanocortin 4 receptor (MC4R) and introduced a series of His residues into the receptor protein to form metal ion binding sites. We were able to insert micromolar affinity binding sites for zinc between transmembrane region (TM) 2 and TM3 where the metal ion alone was able to activate this peptide binding G-protein-coupled receptor. The exact conformation of the metal ion interactions allowed us to predict the orientation of the helices, and remodeling of the receptor protein indicated that Glu100 and Ile104 in TM2 and Asp122 and Ile125 in TM3 are directed toward a putative area of activation of the receptor. The molecular model suggests that a rot…

Protein ConformationAmino Acid MotifsPeptide bindingPlasma protein bindingTransfectionBiochemistryCell LineReceptors G-Protein-CoupledProtein structureCyclic AMPHumansPoint MutationBinding siteReceptorMolecular BiologyBinding SitesChemistryMembrane ProteinsCell BiologyMelanocortin 4 receptorCytosolic partZincBiochemistryBiophysicsReceptor Melanocortin Type 4MelanocortinProtein BindingThe Journal of biological chemistry
researchProduct

Origin of the prolactin-releasing hormone (PRLH) receptors: evidence of coevolution between PRLH and a redundant neuropeptide Y receptor during verte…

2004

We present seven new vertebrate homologs of the prolactin-releasing hormone receptor (PRLHR) and show that these are found as two separate subtypes, PRLHR1 and PRLHR2. Analysis of a number of vertebrate sequences using phylogeny, pharmacology, and paralogon analysis indicates that the PRLHRs are likely to share a common ancestry with the neuropeptide Y (NPY) receptors. Moreover, a micromolar level of NPY was able to bind and inhibit completely the PRLH-evoked response in PRLHR1-expressing cells. We suggest that an ancestral PRLH peptide started coevolving with a redundant NPY binding receptor, which then became PRLHR, approximately 500 million years ago. The PRLHR1 subtype was shown to have…

Prolactin-releasing hormoneGeneticsBase SequenceMolecular Sequence DataBiologyNeuropeptide Y receptorProlactinReceptors G-Protein-CoupledReceptors Neuropeptide YEvolution MolecularPhylogeneticsMolecular evolutionHormone receptorGene DuplicationGene duplicationVertebratesGeneticsAnimalsHumansReceptorPhylogenyGenomics
researchProduct