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Expression of Derlin-1 and its effect on expression of autophagy marker genes under endoplasmic reticulum stress in lung cancer cells.

Xu L, Wang ZH, Xu D, Lin G, Li DR, Wan T, Guo SL - Cancer Cell Int. (2014)

Bottom Line: Knockdown of Derlin-1 did not affect Beclin 1 and LC3II expression but disrupted the degradation of p62 under ER stress, which resulted in the blockage of autophagy flux.Furthermore, Derlin-1 and p62 were observed to interact under ER stress.Derlin-1 may function in tumour progression partially by interacting with p62.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Respiratory Medicine, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, P.R. China.

ABSTRACT

Background: Recent findings indicated that Derlin-1 has an important function in tumour progression. In this study, we aimed to determine whether Derlin-1 has an oncogene function as a cross-talk molecule with autophagy.

Methods: Cancer cells were treated with tunicamycin (TM) for 8 and 24 h. The expression of Derlin-1 and autophagy-related genes was determined by western blot. Autophagy was analysed by fluorescence microscopy after staining the cancer cells with monodansylcadaverine. The interaction between Derlin-1 and other proteins was identified using co-immunoprecipitation assay.

Results: Our study demonstrated high Derlin-1 expression levels in most non-small lung cancer cell lines. Derlin-1 expression was enhanced under endoplasmic reticulum (ER) stress. Previous studies revealed that TM triggers the initiation of autophagy by activating Beclin 1, converting LC3I to LC3II and degrading p62. Knockdown of Derlin-1 did not affect Beclin 1 and LC3II expression but disrupted the degradation of p62 under ER stress, which resulted in the blockage of autophagy flux. Furthermore, Derlin-1 and p62 were observed to interact under ER stress.

Conclusion: This study is the first report about the interaction between Derlin-1 and p62. Derlin-1 may function in tumour progression partially by interacting with p62.

No MeSH data available.


Related in: MedlinePlus

Interplay of Derlin-1 and p62 in A549 cells under ER stress as demonstrated by co-immunoprecipitation assay. Cells were treated with TM for 8 h. Derlin-1 antibody was used in immunoprecipitation. p62 and Derlin-1 antibody were used in western blot. The interaction between Derlin-1 and p62 was detected under ER stress.
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Figure 4: Interplay of Derlin-1 and p62 in A549 cells under ER stress as demonstrated by co-immunoprecipitation assay. Cells were treated with TM for 8 h. Derlin-1 antibody was used in immunoprecipitation. p62 and Derlin-1 antibody were used in western blot. The interaction between Derlin-1 and p62 was detected under ER stress.

Mentions: We investigated the interplay between Derlin-1 and p62 under ER stress using co-immunoprecipitation assay in A549 cells. As shown in Figure 4, the interaction between Derlin-1 and p62 was detected under ER stress (Figure 4), but no detectable band of Beclin 1 and LC3II was observed under normal or ER stress conditions (data not shown).


Expression of Derlin-1 and its effect on expression of autophagy marker genes under endoplasmic reticulum stress in lung cancer cells.

Xu L, Wang ZH, Xu D, Lin G, Li DR, Wan T, Guo SL - Cancer Cell Int. (2014)

Interplay of Derlin-1 and p62 in A549 cells under ER stress as demonstrated by co-immunoprecipitation assay. Cells were treated with TM for 8 h. Derlin-1 antibody was used in immunoprecipitation. p62 and Derlin-1 antibody were used in western blot. The interaction between Derlin-1 and p62 was detected under ER stress.
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4061450&req=5

Figure 4: Interplay of Derlin-1 and p62 in A549 cells under ER stress as demonstrated by co-immunoprecipitation assay. Cells were treated with TM for 8 h. Derlin-1 antibody was used in immunoprecipitation. p62 and Derlin-1 antibody were used in western blot. The interaction between Derlin-1 and p62 was detected under ER stress.
Mentions: We investigated the interplay between Derlin-1 and p62 under ER stress using co-immunoprecipitation assay in A549 cells. As shown in Figure 4, the interaction between Derlin-1 and p62 was detected under ER stress (Figure 4), but no detectable band of Beclin 1 and LC3II was observed under normal or ER stress conditions (data not shown).

Bottom Line: Knockdown of Derlin-1 did not affect Beclin 1 and LC3II expression but disrupted the degradation of p62 under ER stress, which resulted in the blockage of autophagy flux.Furthermore, Derlin-1 and p62 were observed to interact under ER stress.Derlin-1 may function in tumour progression partially by interacting with p62.

View Article: PubMed Central - HTML - PubMed

Affiliation: Department of Respiratory Medicine, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, P.R. China.

ABSTRACT

Background: Recent findings indicated that Derlin-1 has an important function in tumour progression. In this study, we aimed to determine whether Derlin-1 has an oncogene function as a cross-talk molecule with autophagy.

Methods: Cancer cells were treated with tunicamycin (TM) for 8 and 24 h. The expression of Derlin-1 and autophagy-related genes was determined by western blot. Autophagy was analysed by fluorescence microscopy after staining the cancer cells with monodansylcadaverine. The interaction between Derlin-1 and other proteins was identified using co-immunoprecipitation assay.

Results: Our study demonstrated high Derlin-1 expression levels in most non-small lung cancer cell lines. Derlin-1 expression was enhanced under endoplasmic reticulum (ER) stress. Previous studies revealed that TM triggers the initiation of autophagy by activating Beclin 1, converting LC3I to LC3II and degrading p62. Knockdown of Derlin-1 did not affect Beclin 1 and LC3II expression but disrupted the degradation of p62 under ER stress, which resulted in the blockage of autophagy flux. Furthermore, Derlin-1 and p62 were observed to interact under ER stress.

Conclusion: This study is the first report about the interaction between Derlin-1 and p62. Derlin-1 may function in tumour progression partially by interacting with p62.

No MeSH data available.


Related in: MedlinePlus