SEL1L expression in non–small cell lung cancer

Ferrero, Stefano; Falleni, Monica; Cattaneo, Monica; Malferrari, Giulia; Canton, Cristina; Biagiotti, Laura; Maggioni, Marco; Nosotti, Mario; Coggi, Guido; Bòsari, Silvano; Biunno, Ida

doi:10.1016/j.humpath.2005.12.012

Cited by 12 publications

(12 citation statements)

References 15 publications

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“…Interestingly, the SEL1L subcellular localization (nucleus or cytoplasm) may result from SEL1L variant activation in response to genotoxic insults, which is a previously described phenomenon (26,27).…”

Section: Discussionmentioning

confidence: 88%

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Down-modulation of SEL1L, an Unfolded Protein Response and Endoplasmic Reticulum-associated Degradation Protein, Sensitizes Glioma Stem Cells to the Cytotoxic Effect of Valproic Acid

Cattaneo

Baronchelli

Schiffer³

et al. 2014

Journal of Biological Chemistry

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Background: Valproic acid is considered as a promising anti-cancer therapeutic agent acting on unfolded protein response. SEL1L is an UPR-responsive gene. Results: SEL1L interference synergy enhances VPA cytotoxic effects on glioma stem cells. Conclusion: VPA treatment combined with SEL1L depletion may influence GSC pharmacological response. Significance: Targeting SEL1L in association with valproic acid treatment may improve glioma treatment.

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Section: Discussionmentioning

confidence: 88%

“…Generally, it is up-regulated during the initial phases of neoplastic transformation, underlying a potential biomarker function in tumor progression (24 -27). Moreover, the protein subcellular localization is able to distinguish lung cancer subtypes (27).…”

mentioning

confidence: 99%

Down-modulation of SEL1L, an Unfolded Protein Response and Endoplasmic Reticulum-associated Degradation Protein, Sensitizes Glioma Stem Cells to the Cytotoxic Effect of Valproic Acid

Cattaneo

Baronchelli

Schiffer³

et al. 2014

Journal of Biological Chemistry

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“…The intensity of AnxA3 immunoreactivity was scored as: 1 ϭ weak, 2 ϭ moderate, 3 ϭ intense. By multiplying the score with the intensity 19 we obtained the final score of normal and tumor tissue for each case (range, 1 to 9).…”

Section: Tissue Microarraysmentioning

confidence: 99%

Primary Cell Cultures from Human Renal Cortex and Renal-Cell Carcinoma Evidence a Differential Expression of Two Spliced Isoforms of Annexin A3

Bianchi

Bombelli

Raimondo

et al. 2010

The American Journal of Pathology

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“…In addition to HRD1, SEL1L interacts with several components of the dislocation machinery such as the erlectins OS-9 and XTP3-b, both implicated in substrate recognition; derlin-1, previously reported to protect human breast cancer cells from ER stress induced apoptosis [9]. Previous results indicate that SEL1L expression down-modulates breast and pancreatic carcinoma cell aggressiveness both in vivo and in vitro [10, 11], associates with the transition to severe dysplasia in esophageal carcinogenesis, being lost in aggressive esophageal cancers [12], and becomes consistently expressed in the initial stages of prostate and lung cancers [13, 14]. However, no data has yet been reported on the role of SEL1L protein nor of ERAD/UPR in colorectal cancer (CRC), a key model of human epithelial carcinogenesis.…”

Section: Introductionmentioning

confidence: 99%

SEL1L, an UPR Response Protein, a Potential Marker of Colonic Cell Transformation

Ashktorab

Green

Finzi³

et al. 2012

Dig Dis Sci

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Background SEL1L gene product is implicated in the endoplasmic reticulum (ER)-associated protein degradation and Unfolded Protein Response pathways. This gene and associated miRNAs have been indicated as predictive and prognostic markers of pancreatic cancer. Aim Explore the role of SEL1L in colorectal cancer (CRC) progression. Methods SEL1L expression was analysed immunohistochemically in 153 adenomas and 71 CRCs from African American and North Italian patients. The distribution of stained cells was determined by computing median and inter quartile range. The receiver operating characteristics plot was used as discriminate power of SEL1L expression, CRC diagnosis and the effects on patient survival. Results SEL1L was low in normal mucosa and confined to few scattered cells at the base crypt of the villi and in the foveolar glandular compartment. The highest levels were in Paneth cells within the lysosomes. The enterocytic progenitor cells and mature enterocytes showed less cytoplasmic staining. In CRCs, SEL1L expression significantly correlated with the progression from adenoma to carcinoma (P = 0.0001) being stronger in well-to-moderately differentiated cancers. No correlation was found with other clinicopathological characteristics or ethnicity. Conclusions SEL1L expression is a potential CRC tissue biomarker since its expression is significantly higher in adenoma cells with respect to normal mucosa. The levels of expression decrease sensibly in undifferentiated CRC cancers. Interestingly, Paneth cells contain high levels of SEL1L protein that could indicate pre-neoplastic mucosa undergoing neoplastic transformation. Since SEL1L’s major function lies within ER stress and active ERAD response, it may identify CRCs with differentiated secretory phenotype and acute cellular stress.

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SEL1L expression in non–small cell lung cancer

Cited by 12 publications

References 15 publications

Down-modulation of SEL1L, an Unfolded Protein Response and Endoplasmic Reticulum-associated Degradation Protein, Sensitizes Glioma Stem Cells to the Cytotoxic Effect of Valproic Acid

Down-modulation of SEL1L, an Unfolded Protein Response and Endoplasmic Reticulum-associated Degradation Protein, Sensitizes Glioma Stem Cells to the Cytotoxic Effect of Valproic Acid

Primary Cell Cultures from Human Renal Cortex and Renal-Cell Carcinoma Evidence a Differential Expression of Two Spliced Isoforms of Annexin A3

SEL1L, an UPR Response Protein, a Potential Marker of Colonic Cell Transformation

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