0000000000331207

AUTHOR

Tatjana Haitina

showing 8 related works from this author

Pharmacological Characterization of Melanocortin Receptors in Fish Suggests an Important Role for ACTH

2005

The melanocortin (MC) receptor subtypes have distinctive characteristic binding profiles. We found that the trout and Fugu MC4 receptors have similar affinity for alpha-MSH and beta-MSH and a much higher affinity for ACTH than does the human MC4 receptor. The Fugu MC1 and the trout and Fugu MC5 receptors also have higher affinity for ACTH-derived peptides than alpha-, beta-, or gamma-MSH. It is tempting to speculate that ACTH-derived peptides may have played an important role as "original" ligands at the MC receptors, while the specificity of the different subtypes for the alpha-, beta-, and gamma-MSH peptides may have appeared at later stages during vertebrate evolution.

endocrine systemmedicine.medical_specialtyanimal structuresAlpha (ethology)BiologyGeneral Biochemistry Genetics and Molecular BiologyAdrenocorticotropic HormoneHistory and Philosophy of ScienceInternal medicinemedicineAnimalsHumansACTH receptorReceptorBeta (finance)G protein-coupled receptorintegumentary systemFuguReceptors MelanocortinGeneral NeurosciencefungiFishesMelanocortin 3 receptorCell biologyEndocrinologyMelanocortinhormones hormone substitutes and hormone antagonistsProtein BindingAnnals of the New York Academy of Sciences
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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
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Functional characterization of two melanocortin (MC) receptors in lamprey showing orthology to the MC1 and MC4 receptor subtypes

2007

Abstract Background The melanocortin (MC) receptors have a key role in regulating body weight and pigmentation. They belong to the rhodopsin family of G protein-coupled receptors (GPCRs). The purpose of this study was to identify ancestral MC receptors in agnathan, river lamprey. Results We report cloning of two MC receptors from river lamprey. The lamprey receptors, designated MCa and MCb, showed orthology to the MC1 and MC4 receptor subtypes, respectively. The molecular clock analysis suggested that lamprey MC receptor genes were not duplicated recently and diverged from each other more than 400 MYR ago. Expression and pharmacological characterization showed that the lamprey MCa receptor …

Pro-OpiomelanocortinSecond Messenger SystemsGene DuplicationProtein Interaction MappingCyclic AMPPetromyzonReceptorPhylogenyCell Line TransformedSkinGeneticsbiologyReceptors MelanocortinMelanocortin 3 receptorCell biologyOrgan SpecificityRhodopsinReceptor Melanocortin Type 4HagfishesMelanocortinReceptor Melanocortin Type 1Protein BindingResearch ArticleEvolutionRecombinant Fusion ProteinsMolecular Sequence DataBinding CompetitivePeptides CyclicEvolution Moleculargamma-MSHAdrenocorticotropic HormoneSpecies SpecificityMelanocortin receptorbeta-MSHQH359-425AnimalsHumansAmino Acid SequenceEcology Evolution Behavior and SystematicsGene LibraryG protein-coupled receptorBinding SitesSequence Homology Amino AcidFuguLampreybiology.organism_classificationPeptide FragmentsVisceraalpha-MSHbiology.proteinCosyntropinSequence Alignmenthuman activitiesBMC Evolutionary Biology
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Unusual genomic structure: melanocortin receptors in Fugu.

2005

The melanocortin (MC) receptors are found in five subtypes in mammals and chicken, while recent studies have shown that the Fugu (Takifugu rubripes) genome has only four MC receptors and the zebrafish genome has six subtypes. The MC3 receptor seems to be missing from the two closely related pufferfishes, Fugu and Tetraodon (Tetraodon nigroviridis). The MC2 and MC5 receptors in the pufferfish have introns. Moreover, these two receptors are found in a tandem that is remarkably conserved in several vertebrate species. Here, we speculate about the genomic origin of the MC receptors.

Geneticsmedicine.medical_specialtyGenomebiologyTakifugu rubripesFuguGeneral NeuroscienceReceptors MelanocortinfungiSequence Analysis DNATetraodon nigroviridisbiology.organism_classificationGeneral Biochemistry Genetics and Molecular BiologyMelanocortin 3 receptorTakifuguEndocrinologyHistory and Philosophy of ScienceInternal medicinemedicineAnimalsMelanocortinReceptorTetraodonG protein-coupled receptorAnnals of the New York Academy of Sciences
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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
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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
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Cloning of two melanocortin (MC) receptors in spiny dogfish

2004

We report the cloning and characterization of two melanocortin receptors (MCRs) from the spiny dogfish (Squalus acanthias) (Sac). Phylogenetic analysis shows that these shark receptors are orthologues of the MC3R and MC5R subtypes, sharing 65% and 70% overall amino acid identity with the human counterparts, respectively. The SacMC3R was expressed and pharmacologically characterized in HEK293 cells. The radioligand binding results show that this receptor has high affinity for adrenocorticotropic hormone (ACTH)-derived peptides while it has comparable affinity for alpha- and beta-melanocyte stimulating hormone (MSH), and slightly lower affinity for gamma-MSH when compared with the human ortho…

medicine.medical_specialtyGreen Fluorescent ProteinsMolecular Sequence DataCHO CellsAdrenocorticotropic hormoneBiologyPolymerase Chain ReactionBiochemistryCell LineRadioligand Assaygamma-MSHAdrenocorticotropic HormoneCricetinaeInternal medicineCyclic AMPEscherichia colimedicineAnimalsHumansPotencyBacteriophagesTissue DistributionAmino Acid SequenceMelanocyte-Stimulating HormonesCloning MolecularReceptorPhylogenyGene Librarychemistry.chemical_classificationSpiny dogfishDose-Response Relationship DrugSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionChinese hamster ovary cellHEK 293 cellsSequence Analysis DNAbiology.organism_classificationMolecular biologyIntronsAmino acidBlotting SouthernKineticsEndocrinologychemistryDogfishReceptor Melanocortin Type 4MelanocortinPeptidesReceptor Melanocortin Type 3European Journal of Biochemistry
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Evolutionary conservation of the structural, pharmacological, and genomic characteristics of the melanocortin receptor subtypes

2005

We have cloned melanocortin receptors (MCRs) from several species of fish. The MC4R and MC5R subtypes arose early in vertebrate evolution and their primary structure is remarkably conserved. Expression and pharmacological characterization of the MCRs in fish has revealed that they bind and respond to melanocortin peptides with high potency. Detailed characterization of the binding properties of the different subtypes suggests that MCRs in early vertebrates had preference for adrenocorticotropic hormone (ACTH) peptides, while the high sensitivity for the shorter proopiomelanocortin (POMC) products, such as the alpha-, beta-, and gamma-melanocyte-stimulating hormone (MSH), has appeared later,…

Melanocyte-stimulating hormonePhysiologyMolecular Sequence DataBiochemistryConserved sequenceEvolution MolecularCellular and Molecular NeuroscienceEndocrinologyProopiomelanocortinMelanocortin receptorbiology.animalAnimalsHumansAmino Acid SequenceReceptorConserved SequenceG protein-coupled receptorGeneticsbiologyReceptors MelanocortinVertebrateGenomicsStructural Homology Proteinbiology.proteinMelanocortinhormones hormone substitutes and hormone antagonistsPeptides
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