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. 2009 Jun 1;20(11):2744–2754. doi: 10.1091/mbc.E08-11-1092

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© 2009 by The American Society for Cell Biology

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Figure 7. — Misfolded trimeric type I collagen is degraded by an autophagic-lysosomal pathway. (A) Collagen trimerization was analyzed by SDS-PAGE under nonreducing conditions followed by Western blotting with anti-proα1(I) (LF-41) antibody. (B) Mov13-derived cell lines were analyzed by Western blotting with antibodies against the proα1(I) and proα2(I) chains of type I collagen after treatment with proteasome or lysosome inhibitors. Mov13-WT cells carry the wild-type proα1 chain of type I collagen. Mov13-IAFS and Mov13-Arg cell lines carry proα1 chain mutations occurring in the C-propeptide and triple helix regions, respectively. S, supernatant; P, pellet. (C) Examination of polyubiquitination of type I collagen in Mov13 cells. Type I collagen proα1 chain was collected by immunoprecipitation and analyzed by Western blotting with antibodies against ubiquitin or proα1(I). (D) Solubility of the proα1(I) and proα2 (I) chains was examined by Western blotting. (E) The trimeric form of procollagen in Mov13-Arg cells increased in the detergent-insoluble fractions after treatment with bafilomycin A1. Cells were treated with or without bafilomycin A1 as a control, and SDS-PAGE was performed under nonreducing conditions followed by Western blot analysis with anti-α1(I) antibody.