2024
Both enantiomers of β-aminoisobutyric acid BAIBA regulate Fgf23 via MRGPRD receptor by activating distinct signaling pathways in osteocytes
Sakamoto E, Kitase Y, Fitt A, Zhu Z, Awad K, Brotto M, White K, Welc S, Bergwitz C, Bonewald L. Both enantiomers of β-aminoisobutyric acid BAIBA regulate Fgf23 via MRGPRD receptor by activating distinct signaling pathways in osteocytes. Cell Reports 2024, 43: 114397. PMID: 38935499, PMCID: PMC11350516, DOI: 10.1016/j.celrep.2024.114397.Peer-Reviewed Original ResearchActivate distinct signaling pathwaysSignaling pathwayFibroblast growth factor 23Urinary phosphate excretionReceptor type DInduce FGF23Urine phosphateElevated FGF23Phosphate excretionFGF23L-BAIBAExercise-induced increasePhosphate homeostasisSclerostinPhosphate metabolismReceptorsD-enantiomerBonePathway
1997
Residues in the Membrane-spanning and Extracellular Loop Regions of the Parathyroid Hormone (PTH)-2 Receptor Determine Signaling Selectivity for PTH and PTH-related Peptide*
Bergwitz C, Jusseaume S, Luck M, Jüppner H, Gardella T. Residues in the Membrane-spanning and Extracellular Loop Regions of the Parathyroid Hormone (PTH)-2 Receptor Determine Signaling Selectivity for PTH and PTH-related Peptide*. Journal Of Biological Chemistry 1997, 272: 28861-28868. PMID: 9360953, DOI: 10.1074/jbc.272.46.28861.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell MembraneCOS CellsCyclic AMPHistidineHumansIsoleucineMolecular Sequence DataMutagenesis, Site-DirectedParathyroid HormoneParathyroid Hormone-Related ProteinPeptide FragmentsProteinsReceptor, Parathyroid Hormone, Type 2Receptors, Parathyroid HormoneSequence Homology, Amino AcidSignal TransductionConceptsPTH-2 receptorPTH-1 receptorParathyroid hormoneCOOH-terminal portionCOS-7 cellsCassette substitutionsPTH 1Membrane-spanningPoint mutationsTransmembrane helix 3Helix 3Divergent residuesPTHCOS-7Receptor selectivityResidues 5ReceptorsPTH-related peptideFunctional interactionsPTHrP-(1-36Receptor DetermineReceptor chimerasCAMP responseExtracellular loop 2PTH-2
1996
Full Activation of Chimeric Receptors by Hybrids between Parathyroid Hormone and Calcitonin EVIDENCE FOR A COMMON PATTERN OF LIGAND-RECEPTOR INTERACTION*
Bergwitz C, Gardella T, Flannery M, Potts J, Kronenberg H, Goldring S, Jüppner H. Full Activation of Chimeric Receptors by Hybrids between Parathyroid Hormone and Calcitonin EVIDENCE FOR A COMMON PATTERN OF LIGAND-RECEPTOR INTERACTION*. Journal Of Biological Chemistry 1996, 271: 26469-26472. PMID: 8900113, DOI: 10.1074/jbc.271.43.26469.Peer-Reviewed Original ResearchConceptsParathyroid hormoneG protein-coupled receptorsProtein-coupled receptorsReceptor chimerasPTH receptorFamily of G protein-coupled receptorsLigand-receptor interactionsPatterns of ligand-receptor interactionsCalcitoninParathyroid hormone receptorReceptorsCommon patternChimeric receptorsHormoneHybrid ligandsAmino acid sequence homologyFull activationSame family
1991
Specific, high-affinity binding sites for angiotensin II on Mycoplasma hyorhinis
Bergwitz C, Madoff S, Abou-Samra A, Ju¨ppner H. Specific, high-affinity binding sites for angiotensin II on Mycoplasma hyorhinis. Biochemical And Biophysical Research Communications 1991, 179: 1391-1399. PMID: 1718269, DOI: 10.1016/0006-291x(91)91727-t.Peer-Reviewed Original ResearchConceptsAngiotensin II receptorsAngiotensin IIII receptorsHigh-affinity binding sitesAngiotensin II bindingOpossum kidney cellsCGP 42112ADuP 753Angiotensin IIIStrains of Mycoplasma hyorhinisAngiotensin IHuman angiotensin IIM. hominisHigh affinityKidney cellsBinding sitesII bindingMycoplasma hyorhinisSpecific bindingReceptorsStrains of M. hominisAntagonist DuP 753Fold decreaseSensitive to bacitracin