2012
Site-specific N-Linked Glycosylation of Receptor Guanylyl Cyclase C Regulates Ligand Binding, Ligand-mediated Activation and Interaction with Vesicular Integral Membrane Protein 36, VIP36*
Arshad N, Ballal S, Visweswariah SS. Site-specific N-Linked Glycosylation of Receptor Guanylyl Cyclase C Regulates Ligand Binding, Ligand-mediated Activation and Interaction with Vesicular Integral Membrane Protein 36, VIP36*. Journal Of Biological Chemistry 2012, 288: 3907-3917. PMID: 23269669, PMCID: PMC3567644, DOI: 10.1074/jbc.m112.413906.Peer-Reviewed Original ResearchMeSH KeywordsCell LineCell MembraneEndoplasmic ReticulumGastrointestinal HormonesGlycosylationHumansLigandsMannose-Binding LectinsMembrane Transport ProteinsNatriuretic PeptidesProtein BindingProtein FoldingProtein Structure, TertiaryReceptors, EnterotoxinReceptors, Guanylate Cyclase-CoupledReceptors, PeptideConceptsLigand bindingVesicular integral membrane proteinGuanylyl cyclase CIntegral membrane proteinsGlycosylation of proteinsHeat‐stable enterotoxin peptideLigand-mediated activationSite of glycosylationTissue-dependent mannerReceptor guanylyl cyclaseReceptor guanylyl cyclase CGlycan-mediated interactionsDifferent cell typesMembrane proteinsSystematic mutagenesisGlycosylation sitesCyclase CCGMP-dependent mannerExtracellular domainProtein 36Endoplasmic reticulumSurface localizationVIP36Cell typesST peptidesThe multiple and enigmatic roles of guanylyl cyclase C in intestinal homeostasis
Arshad N, Visweswariah SS. The multiple and enigmatic roles of guanylyl cyclase C in intestinal homeostasis. FEBS Letters 2012, 586: 2835-2840. PMID: 22819815, DOI: 10.1016/j.febslet.2012.07.028.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsColonic NeoplasmsCyclic GMPEnzyme ActivationFeeding BehaviorHomeostasisHumansIntestinesMiceReceptors, EnterotoxinReceptors, Guanylate Cyclase-CoupledReceptors, PeptideConceptsGuanylyl cyclase CCyclase CGut immune systemIntestinal epithelial cellsColon cell proliferationTravelers' diarrheaIntestinal homeostasisHeat-stable enterotoxinImmune systemActivation of GCIon secretionEpithelial cellsCell proliferationCausative agentDiarrheaIntracellular levelsFirst descriptionReceptorsRecent findingsFuture studiesHuman diseasesEnigmatic roleNew findingsDiseaseFindingsFamilial Diarrhea Syndrome Caused by an Activating GUCY2C Mutation
Fiskerstrand T, Arshad N, Haukanes BI, Tronstad RR, Pham KD, Johansson S, Håvik B, Tønder SL, Levy SE, Brackman D, Boman H, Biswas KH, Apold J, Hovdenak N, Visweswariah SS, Knappskog PM. Familial Diarrhea Syndrome Caused by an Activating GUCY2C Mutation. New England Journal Of Medicine 2012, 366: 1586-1595. PMID: 22436048, DOI: 10.1056/nejmoa1110132.Peer-Reviewed Original ResearchMeSH KeywordsChronic DiseaseCyclic GMPDiarrheaFemaleGenetic LinkageHeterozygoteHumansMaleMutation, MissensePedigreePolymorphism, Single NucleotideReceptors, EnterotoxinReceptors, Guanylate Cyclase-CoupledReceptors, PeptideSignal TransductionConceptsCystic fibrosis transmembrane regulatorEntire candidate regionCandidate regionsExons of genesHEK293T cellsAffected family membersCyclic guanosine monophosphateSingle nucleotide polymorphismsBacterial heat-stable enterotoxinsFamily membersMutant receptorsChromosome 12GC-C signalingMutant GcRecessive mutationsLinkage analysisTransmembrane regulatorFunctional studiesMissense mutationsGenetic variantsHeterozygous missense mutationMutationsExome sequencingGUCY2C mutationGenes
2009
Receptor guanylyl cyclase C (GC-C): regulation and signal transduction
Basu N, Arshad N, Visweswariah SS. Receptor guanylyl cyclase C (GC-C): regulation and signal transduction. Molecular And Cellular Biochemistry 2009, 334: 67-80. PMID: 19960363, DOI: 10.1007/s11010-009-0324-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsGastrointestinal TractGuanylate CyclaseHumansReceptors, EnterotoxinReceptors, Guanylate Cyclase-CoupledReceptors, PeptideSignal TransductionTissue Distribution