Search results for "thyroid epithelial cell"

showing 5 items of 5 documents

Arrestin-β-1 Physically Scaffolds TSH and IGF1 Receptors to Enable Crosstalk

2019

Endogenously expressed TSH receptors (TSHRs) on orbital fibroblasts of patients with Graves ophthalmopathy (GO) use crosstalk with IGF1 receptors (IGF1R) to synergistically stimulate secretion of hyaluronan (HA), a major component of GO pathology. We previously showed crosstalk occurred upstream of mitogen-activated protein kinase (ERK) phosphorylation. Because other G protein-coupled receptors engage arrestin-β-1 (ARRB1) and ERK, we tested whether ARRB1 was a necessary component of TSHR/IGF1R crosstalk. HA secretion was stimulated by the TSHR-stimulating monoclonal antibodies M22 and KSAb1, or immunoglobulins from patients with GO (GO-Igs). Treatment with M22, as previously shown, resulted…

0301 basic medicineMAPK/ERK pathwaymedicine.medical_specialty030209 endocrinology & metabolismStimulationReceptor tyrosine kinaseCell LineReceptor IGF Type 103 medical and health sciencesMice0302 clinical medicineEndocrinologyInternal medicinemedicineArrestinAnimalsHumansPhosphorylationProtein kinase AReceptorResearch ArticlesbiologyChemistryReceptors Thyrotropinbody regionsGraves OphthalmopathyCrosstalk (biology)030104 developmental biologyEndocrinologybeta-Arrestin 1Thyroid Epithelial CellsGene Knockdown Techniquesbiology.proteinPhosphorylationSignal Transduction
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TSH/IGF-1 Receptor Cross-Talk Rapidly Activates Extracellular Signal-Regulated Kinases in Multiple Cell Types

2017

We previously showed that thyrotropin (TSH)/insulinlike growth factor (IGF)-1 receptor cross-talk appears to be involved in Graves’ orbitopathy (GO) pathogenesis and upregulation of thyroid-specific genes in human thyrocytes. In orbital fibroblasts from GO patients, coadministration of TSH and IGF-1 induces synergistic increases in hyaluronan secretion. In human thyrocytes, TSH plus IGF-1 synergistically increased expression of the sodium-iodide symporter that appeared to involve ERK1/2 activation. However, the details of ERK1/2 activation were not known, nor was whether ERK1/2 was involved in this synergism in other cell types. Using primary cultures of GO fibroblasts (GOFs) and human thyr…

0301 basic medicinemedicine.medical_specialtyCell typeendocrine systemendocrine system diseasesMAP Kinase Signaling SystemThyrotropinPertussis toxinReceptor IGF Type 103 medical and health sciencesEndocrinologyDownregulation and upregulationInternal medicinemedicineHumansSecretionHyaluronic AcidInsulin-Like Growth Factor IPhosphorylationReceptorResearch ArticlesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3SymportersChemistryHEK 293 cellsReceptors ThyrotropinReceptor Cross-TalkFibroblastsSignalingGraves Ophthalmopathy030104 developmental biologyEndocrinologyHEK293 CellsThyroid Epithelial CellsSymporterPhosphorylationhormones hormone substitutes and hormone antagonistsEndocrinology
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Graves' Autoantibodies Exhibit Different Stimulating Activities in Cultures of Thyrocytes and Orbital Fibroblasts Not Reflected by Clinical Assays

2021

Background: The pathogenesis of Graves' hyperthyroidism (GH) and associated Graves' orbitopathy (GO) appears to involve stimulatory autoantibodies (thyrotropin receptor [TSHR]-stimulating antibodies [TSAbs]) that bind to and activate TSHRs on thyrocytes and orbital fibroblasts. In general, measurement of circulating TSHR antibodies by clinical assays correlates with the status of GH and GO. However, most clinical measurements of TSHR antibodies use competitive binding assays that do not distinguish between TSAbs and antibodies that bind to but do not activate TSHRs. Moreover, clinical assays for TSAbs measure stimulation of only one signaling pathway, the cyclic adenosine monophosphate (cAM…

AdultMaleendocrine systemmedicine.medical_specialtyendocrine system diseasesEndocrinology Diabetes and Metabolismmedicine.medical_treatmentGraves' diseaseThyrotropinStimulationEndocrinologyimmune system diseasesInternal medicinemedicineHumansSecretionImmunology Autoimmunity and Graves' OphthalmopathyAutoantibodiesbiologyKinaseChemistryFibroblastsMiddle Agedmedicine.diseaseGraves Diseaseeye diseasesIn vitroGraves OphthalmopathyEndocrinologyThyroid Epithelial Cellsbiology.proteinFemaleThyroglobulinSignal transductionAntibodyThyroid
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Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex.

2002

Folding and post-translational modification of the thyroid hormone precursor, thyroglobulin (Tg), in the endoplasmic reticulum (ER) of the thyroid epithelial cells is facilitated by several molecular chaperones and folding enzymes, such as BiP, GRP94, calnexin, protein disulfide isomerase, ERp72, and others. They have been shown to associate simultaneously and/or sequentially with Tg in the course of its maturation, thus forming large heterocomplexes in the ER of thyrocytes. Here we present evidence that such complexes include a novel member, an ER-resident lumenal protein, ERp29, which is present in all mammalian tissues with exceptionally high levels of expression in the secretory cells. …

Protein DenaturationProtein FoldingImmunoprecipitationmedicine.medical_treatmentBlotting WesternThyroid GlandThyrotropinBiologyEndoplasmic ReticulumLigandsBiochemistryThyroglobulinRats Sprague-DawleyCalnexinmedicineCentrifugation Density GradientAnimalsUreaSecretionProtein disulfide-isomeraseMolecular BiologyCells CulturedHeat-Shock ProteinsThyroid Epithelial CellsChromatographyEndoplasmic reticulumCell BiologyPrecipitin TestsRatsCross-Linking ReagentsBiochemistryLiverMicroscopy FluorescenceMicrosomes LiverProtein foldingThyroglobulinProtein BindingThe Journal of biological chemistry
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Xanthine dehydrogenase processes retinol to retinoic acid in human thyroid epitelial cells

2012

thyroid epithelial cellSettore BIO/10 - Biochimicaretinol
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