{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,4]],"date-time":"2025-11-04T15:39:14Z","timestamp":1762270754517},"reference-count":17,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":7431,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1984,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Experiments were conducted to determine the extent and variability of collagen degradation in human fetal lung fibroblasts. Cells were incubated with [<jats:sup>14<\/jats:sup>C]proline, and degradation was measured by determining the hydroxy[<jats:sup>14<\/jats:sup>C]proline in a low molecular weight fraction relative to total hydroxy[<jats:sup>14<\/jats:sup>C]proline. Average (basal) degradation in stationary phase HFL\u20101 cells incubated for 8 h was 16 \u00b1 3%, and substantial alterations in the composition of the labeling medium, e.g., omitting serum and varying pH between 6.8 and 7.8, had no effect. Organic buffers slightly lowered degradation in a manner that was independent of pH. Collagen degradation in two other lung cell lines, Wl\u201038 and IMR\u201090, did not differ from the level in HFL\u20101. Degradation was significantly higher (23 \u00b1 5%) in HFL\u20101 cultures labeled for 24 h rather than 8 h, and pulse\u2010washout experiments showed that the rate of degradation was not uniform: after an 8\u2010h pulse, 11% of the hydroxy [<jats:sup>14<\/jats:sup>C]proline in the medium was in the low molecular weight fraction, but 31% was in this fraction after a 16\u2010h washout. The lack of effect of either serum deprivation or elevated pH suggests that lysosomal proteases have no direct role in basal degradation; however, NH<jats:sub>4<\/jats:sub>Cl decreased the enhanced degradation observed in ascorbate deficiency to basal level, indicating that abnormal molecules synthesized under those conditions are degraded by lysosomal proteases. The appearance of small hydroxy[<jats:sup>14<\/jats:sup>C]proline\u2010containing molecules was inhibited by \u03b1\u03b1\u2032dipyridyl and cycloheximide in a dose\u2010dependent and reversible manner, demonstrating that their production depends on enzymatic hydroxylation of proline and protein synthesis.<\/jats:p>","DOI":"10.1002\/jcp.1041210119","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T14:17:16Z","timestamp":1109427436000},"page":"152-158","source":"Crossref","is-referenced-by-count":27,"title":["Collagen degradation in human lung fibroblasts: Extent of degradation, role of lysosomal proteases, and evaluation of an alternate hypothesis"],"prefix":"10.1002","volume":"121","author":[{"given":"Robert S.","family":"Bienkowski","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0024-3205(81)90444-6"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.79.12.3838"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(83)90338-7"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.77.8.4746"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj2140001"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/276413a0"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(81)90382-1"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2787(80)90228-2"},{"key":"e_1_2_1_10_1","doi-asserted-by":"crossref","first-page":"7721","DOI":"10.1016\/S0021-9258(18)32239-7","article-title":"Synthesis of a shortened pro\u2010\u03b12(I) chain and decreased synthesis of pro\u2010\u03b12(I) chains in a proband with osteogenesis imperfecta","volume":"258","author":"de Wet W. 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