Abstract：
:Procollagen I is a trimer consisting of two proalpha1(I) chains and one proalpha 2(I) chain. In certain cases of mild osteogenesis imperfecta, abnormal proalpha1(I) chains are degraded very soon after synthesis. As a consequence, the cells produce excess proalpha2(I) chains, which cannot form trimers and are not secreted. The objective of this work was to determine the intracellular fate of unassociated proalpha2(I) chains. Mov13 mouse fibroblasts, which do not synthesize proalpha1(I) mRNA, but do produce proalpha2(I) mRNA, were incubated with radioactive amino acids using pulse-chase protocols, and proteins were analyzed by gel electrophoresis, autoradiography, and Western blotting. Mov13 cells produced proalpha2(I) chains that were degraded intracellularly within 30 min. Degradation was inhibited when cells were treated with brefeldin-A, which blocks transit from endoplasmic reticulum to Golgi. Fixed cells exposed to various immunofluorescence markers and imaged by confocal laser scanning microscopy showed that proalpha2(I) chains colocalized with Golgi and lysosome markers. Degradation was inhibited and chains were secreted when cells were treated with wortmannin, which blocks trafficking to lysosomes. These results demonstrate that unassociated proalpha2(I) chains leave the endoplasmic reticulum, transit the Golgi, and enter lysosomes where they are degraded.
journal_name
Exp Cell Resjournal_title
Experimental cell researchauthors
Gotkin MG,Ripley CR,Lamande SR,Bateman JF,Bienkowski RSdoi
10.1016/j.yexcr.2004.01.029keywords:
subject
Has Abstractpub_date
2004-06-10 00:00:00pages
307-16issue
2eissn
0014-4827issn
1090-2422pii
S0014482704000655journal_volume
296pub_type
杂志文章abstract：:Poly(ADP-ribosyl)ation (PARylation) is a post-translational modification of proteins catalysed by Poly(ADP-ribose) polymerases (PARP). A wealth of recent advances in the biochemical and functional characterization of the DNA-dependent PARP family members have highlighted their key contribution in the DNA damage respon...
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