{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T14:02:55Z","timestamp":1770991375645,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2002,9,15]]},"abstract":"<jats:p>The CFTR (cystic fibrosis transmembrane conductance regulator) gene, defective in cystic fibrosis, codes for a polytopic apical membrane protein functioning as a chloride channel. Wild-type (wt) CFTR matures inefficiently and CFTR with a deletion of Phe-508 (F508del), the most frequent mutation, is substantially retained as a core-glycosylated intermediate in the endoplasmic reticulum (ER), probably due to misfolding that is recognized by the cellular quality control machinery involving molecular chaperones. Here, we overexpressed the heat-shock protein (Hsp) 70 chaperone in vivo and observed no changes in degradation rate of the core-glycosylated form, nor in the efficiency of its conversion into the fully glycosylated form, for either wt- or F508del-CFTR, contrary to previous in vitro studies on the affect of heat-shock cognate (Hsc) 70 on part of the first nucleotide-binding domain of CFTR. Co-transfection of Hsp70 with its co-chaperone human DnaJ homologue (Hdj)-1\/Hsp40, however, stabilizes the immature form of wt-CFTR, but not of F508del-CFTR, suggesting that these chaperones act on a wt-specific conformation. As the efficiency of conversion into the fully glycosylated form is not increased under Hsp70\/Hdj-1 overexpression, the lack of these two chaperones does not seem to be critical for CFTR maturation and ER retention. The effects of 4-phenylbutyrate and deoxyspergualin, described previously to interfere with Hsp70 binding, were also tested upon CFTR degradation and processing. The sole effect observed was destabilization of F508del-CFTR.<\/jats:p>","DOI":"10.1042\/bj20011717","type":"journal-article","created":{"date-parts":[[2002,7,28]],"date-time":"2002-07-28T21:38:53Z","timestamp":1027892333000},"page":"797-806","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":106,"title":["The human DnaJ homologue (Hdj)-1\/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70"],"prefix":"10.1042","volume":"366","author":[{"given":"Carlos M.","family":"FARINHA","sequence":"first","affiliation":[{"name":"Centro de Gen\u00e9tica Humana, Instituto Nacional de Sa\u00fade Dr. Ricardo Jorge, Av. Padre Cruz, 1649-016 Lisboa, Portugal"},{"name":"Departamento de Qu\u00edmica e Bioqu\u00edmica, Faculdade de Ci\u00eancias da Universidade de Lisboa, 1749-016 Lisboa, Portugal,"}]},{"given":"Paulo","family":"NOGUEIRA","sequence":"additional","affiliation":[{"name":"Observat\u00f3rio Nacional de Sa\u00fade, Instituto Nacional de Sa\u00fade Dr. Ricardo Jorge, 1649-016 Lisboa, Portugal"}]},{"given":"Filipa","family":"MENDES","sequence":"additional","affiliation":[{"name":"Centro de Gen\u00e9tica Humana, Instituto Nacional de Sa\u00fade Dr. Ricardo Jorge, Av. Padre Cruz, 1649-016 Lisboa, Portugal"}]},{"given":"Deborah","family":"PENQUE","sequence":"additional","affiliation":[{"name":"Centro de Gen\u00e9tica Humana, Instituto Nacional de Sa\u00fade Dr. Ricardo Jorge, Av. Padre Cruz, 1649-016 Lisboa, Portugal"}]},{"given":"Margarida D.","family":"AMARAL","sequence":"additional","affiliation":[{"name":"Centro de Gen\u00e9tica Humana, Instituto Nacional de Sa\u00fade Dr. Ricardo Jorge, Av. Padre Cruz, 1649-016 Lisboa, Portugal"},{"name":"Departamento de Qu\u00edmica e Bioqu\u00edmica, Faculdade de Ci\u00eancias da Universidade de Lisboa, 1749-016 Lisboa, Portugal,"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/366\/3\/797\/709826\/bj3660797.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/366\/3\/797\/709826\/bj3660797.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T12:22:16Z","timestamp":1637583736000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/366\/3\/797\/40381\/The-human-DnaJ-homologue-Hdj-1-heat-shock-protein"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,9,15]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2002,9,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20011717","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2002,9,15]]}}}