{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T20:51:53Z","timestamp":1792788713650,"version":"4.5.0"},"reference-count":82,"publisher":"The Endocrine Society","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,6,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Thyroid hormones are released from thyroglobulin (Tg) in lysosomes, which are impaired in infantile\/nephropathic cystinosis. Cystinosis is a lysosomal cystine storage disease due to defective cystine exporter, cystinosin. Cystinotic children develop subclinical and then overt hypothyroidism. Why hypothyroidism is the most frequent and earliest endocrine complication of cystinosis is unknown. We here defined early alterations in Ctns\u2212\/\u2212 mice thyroid and identified subcellular and molecular mechanisms. At 9 months, T4 and T3 plasma levels were normal and TSH was moderately increased (\u223c4-fold). By histology, hyperplasia and hypertrophy of most follicles preceded colloid exhaustion. Increased immunolabeling for thyrocyte proliferation and apoptotic shedding indicated accelerated cell turnover. Electron microscopy revealed endoplasmic reticulum (ER) dilation, apical lamellipodia indicating macropinocytic colloid uptake, and lysosomal cystine crystals. Tg accumulation in dilated ER contrasted with mRNA down-regulation. Increased expression of ER chaperones, glucose-regulated protein of 78 kDa and protein disulfide isomerase, associated with alternative X-box binding protein-1 splicing, revealed unfolded protein response (UPR) activation by ER stress. Decreased Tg mRNA and ER stress suggested reduced Tg synthesis. Coordinated increase of UPR markers, activating transcription factor-4 and C\/EBP homologous protein, linked ER stress to apoptosis. Hormonogenic cathepsins were not altered, but lysosome-associated membrane protein-1 immunolabeling disclosed enlarged vesicles containing iodo-Tg and impaired lysosomal fusion. Isopycnic fractionation showed iodo-Tg accumulation in denser lysosomes, suggesting defective lysosomal processing and hormone release. In conclusion, Ctns\u2212\/\u2212 mice showed the following alterations: 1) compensated primary hypothyroidism and accelerated thyrocyte turnover; 2) impaired Tg production linked to ER stress\/UPR response; and 3) altered endolysosomal trafficking and iodo-Tg processing. The Ctns\u2212\/\u2212 thyroid is useful to study disease progression and evaluate novel therapies.<\/jats:p>","DOI":"10.1210\/en.2014-1672","type":"journal-article","created":{"date-parts":[[2015,3,26]],"date-time":"2015-03-26T16:33:18Z","timestamp":1427387598000},"page":"2349-2364","source":"Crossref","is-referenced-by-count":43,"title":["A Mouse Model Suggests Two Mechanisms for Thyroid Alterations in Infantile Cystinosis: Decreased Thyroglobulin Synthesis Due to Endoplasmic Reticulum Stress\/Unfolded Protein Response and Impaired Lysosomal Processing"],"prefix":"10.1210","volume":"156","author":[{"given":"H. P.","family":"Gaide Chevronnay","sequence":"first","affiliation":[{"name":"Cell Biology Unit (H.P.G.C., V.J., P.V.D.S., Y.A., C.E.P., P.J.C.), de Duve Institute and Universit\u00e9 Catholique de Louvain, 1200 Brussels, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V.","family":"Janssens","sequence":"first","affiliation":[{"name":"Cell Biology Unit (H.P.G.C., V.J., P.V.D.S., Y.A., C.E.P., P.J.C.), de Duve Institute and Universit\u00e9 Catholique de Louvain, 1200 Brussels, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P.","family":"Van Der Smissen","sequence":"first","affiliation":[{"name":"Cell Biology Unit (H.P.G.C., V.J., P.V.D.S., Y.A., C.E.P., P.J.C.), de Duve Institute and Universit\u00e9 Catholique de Louvain, 1200 Brussels, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"X. H.","family":"Liao","sequence":"first","affiliation":[{"name":"Departments of Medicine (X.H.L., S.R.) The University of Chicago, Chicago, Illinois 60637;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Y.","family":"Abid","sequence":"first","affiliation":[{"name":"Cell Biology Unit (H.P.G.C., V.J., P.V.D.S., Y.A., C.E.P., P.J.C.), de Duve Institute and Universit\u00e9 Catholique de Louvain, 1200 Brussels, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"N.","family":"Nevo","sequence":"first","affiliation":[{"name":"INSERM, Unit\u00e9 1163 (N.N., C.A.), H\u00f4pital Necker-Enfants Malades and Universit\u00e9 Paris Descartes, Sorbonne Paris Cit\u00e9, Institut Imagine, 75015 Paris, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C.","family":"Antignac","sequence":"first","affiliation":[{"name":"INSERM, Unit\u00e9 1163 (N.N., C.A.), H\u00f4pital Necker-Enfants Malades and Universit\u00e9 Paris Descartes, Sorbonne Paris Cit\u00e9, Institut Imagine, 75015 Paris, France;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S.","family":"Refetoff","sequence":"first","affiliation":[{"name":"Departments of Medicine (X.H.L., S.R.) The University of Chicago, Chicago, Illinois 60637;"},{"name":"Pediatrics and Genetics (S.R), The University of Chicago, Chicago, Illinois 60637;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S.","family":"Cherqui","sequence":"first","affiliation":[{"name":"Department of Pediatrics (S.C.), Division of Genetics, University of California, San Diego, San Diego, California 92161"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C. E.","family":"Pierreux","sequence":"first","affiliation":[{"name":"Cell Biology Unit (H.P.G.C., V.J., P.V.D.S., Y.A., C.E.P., P.J.C.), de Duve Institute and Universit\u00e9 Catholique de Louvain, 1200 Brussels, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P. 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