ER Stress and Angiogenesis

Binet, François; Sapieha, Przemysław

doi:10.1016/j.cmet.2015.07.010

Cited by 145 publications

(150 citation statements)

References 164 publications

Supporting

Mentioning

142

Contrasting

Unclassified

Order By: Relevance

“…1). However, chronic or overwhelming ER-stress elicits apoptotic signals such as CHOP expression followed by an activation of intrinsic mitochondrial apoptotic pathway (18,37). In this study, we observed that NSC produced a dose-and timedependent elevation of GRP78, XBP1s and CHOP mRNAs (Fig.…”

Section: Discussionsupporting

confidence: 49%

“…When PERK is activated, it phosphorylates eukaryotic translation-initiation factor 2α (eIF2α), reducing mRNA translation and biosynthetic protein-folding load in the ER. Once IRE1α is activated, it functions as an endoribonuclease to remove a 26-nucleotide region from unspliced X-box binding protein 1 (XBP1u) mRNA, generating a spliced XBP1 (XBP1s) mRNA that yields an active transcription factor (XBP1s) to regulate the expression of various subsets of genes involved in protein folding (18,38). On the other hand, the activated IRE1α causes a degradation of selective mRNAs, resulting in an overall decrease in protein biosynthesis.…”

Section: Discussionmentioning

confidence: 99%

“…ER associated degradation (ERAD) (Fig. 7), a process which directs unfolded or misfolded proteins for destruction by the cytoplasmic proteasome pathways, is enhanced when cells are subjected to ER-stress (18,37,49). ERAD involves the chaperone of unfolded or misfolded proteins by GRP78 to the cytosol and then degradation of these proteins through either ubiquitin-proteasome or autophagy-lysosome pathway.…”

Section: Discussionmentioning

confidence: 99%

“…Endoplasmic reticulum (ER) plays an essential role in cell function and survival. Accumulation of unfolded or misfolded proteins in the lumen of the ER activates the unfold protein response (UPR), resulting in ER-stress (16)(17)(18). The complex cellular response of ER-stress is mediated through three ER transmembrane systems: pancreatic ER kinase-like ER kinase (PERK), activating transcription factor 6 (ATF6) and inositolrequiring enzyme 1 (IRE1).…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Dissociation of NSC606985 induces atypical ER-stress and cell death in prostate cancer cells

Wang

Zhao

et al. 2016

International Journal of Oncology

View full text Add to dashboard Cite

Abstract. Castration-resistant prostate cancer (CRPC) is a major cause of prostate cancer (Pca) death. Chemotherapy is able to improve the survival of CRPC patients. We previously found that NSC606985 (NSC), a highly water-soluble camptothecin analog, induced cell death in Pca cells via interaction with topoisomerase 1 and activation of the mitochondrial apoptotic pathway. To further elucidate the role of NSC, we studied the effect of NSC on ER-stress and its association with NSC-induced cell death in Pca cells. NSC produced a timeand dose-dependent induction of GRP78, CHOP and XBP1s mRNA, and CHOP protein expression in Pca cells including DU145, indicating an activation of ER-stress. However, unlike conventional ER-stress in which GRP78 protein is increased, NSC produced a time-and dose-dependent U-shape change in GRP78 protein in DU145 cells. The NSC-induced decrease in GRP78 protein was blocked by protease inhibitors, N-acetyl-L-leucyl-L-leucylnorleucinal (ALLN), a lysosomal protease inhibitor, and epoxomicin (EPO), a ubiquitin-protease inhibitor. ALLN, but not EPO, also partially inhibited NSC-induced cell death. However, both 4-PBA and TUDCA, two chemical chaperons that effectively reduced tunicamycin-induced ER-stress, failed to attenuate NSC-induced GRP78, CHOP and XBP1s mRNA expression and cell death. Moreover, knockdown of NSC induction of CHOP expression using a specific siRNA had no effect on NSC-induced cytochrome c release and NSC-induced cell death. These results suggest that NSC produced an atypical ER-stress that is dissociated from NSC-induced activation of the mitochondrial apoptotic pathway and NSC-induced cell death in DU145 prostate cancer cells.

show abstract

Section: Discussionsupporting

confidence: 49%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Dissociation of NSC606985 induces atypical ER-stress and cell death in prostate cancer cells

Wang

Zhao

et al. 2016

International Journal of Oncology

View full text Add to dashboard Cite

show abstract

“…Hence, CHOP has the propensity to drive apoptosis [51] and thus cells might be led to apoptosis. Our linear regression analysis showed that the expression level of p-eIF2α was positively associated with the number of bone-forming osteoblasts, and negatively associated with that of bone-resorbing osteoclasts.…”

Section: Discussionmentioning

confidence: 99%

Role of endoplasmic reticulum stress in disuse osteoporosis

Yang

et al. 2017

Bone

View full text Add to dashboard Cite

Transmembrane protein 215 promotes angiogenesis by maintaining endothelial cell survival

Liu

Zheng

et al. 2018

Journal Cellular Physiology

View full text Add to dashboard Cite

Sprouting angiogenesis is a major form of neovascularization of tissues suffering from hypoxia and other related stress. Endothelial cells (ECs) undergo proliferation, differentiation, programmed death, and migration during angiogenic sprouting, but the underlying molecular mechanisms regulating ECs in angiogenesis have been incompletely elucidated. Here we report that the transmembrane protein 215 (TMEM215) is involved in angiogenesis by regulating EC survival. The murine TMEM215 gene, which possesses two transcriptional starting sites as determined by 5′‐rapid amplification of complementary DNA (cDNA) ends (RACE), encodes a two‐pass TMEM. The TMEM215 transcripts were detected in ECs in addition to other tissues by quantitative reverse transcription‐polymerase chain reaction. Immunofluorescence showed that TMEM215 was expressed in the vasculature in retina, liver, and tumor, and colocalized with EC markers. We show that knockdown of TMEM215 in ECs induced strong cell death of ECs in vitro without affecting cell proliferation and migration, suggesting that TMEM215 was required for EC survival. Downregulation of TMEM215 expression compromised lumen formation and sprouting capacities of ECs in vitro. Moreover, intravitreous injection of TMEM215 small interfering RNA resulted in delayed and abnormal development of retinal vasculature with poor perfusion. These results identified TMEM215 as a novel molecule involved in angiogenesis by regulating the survival of ECs.

show abstract

ER Stress and Angiogenesis

Cited by 145 publications

References 164 publications

Dissociation of NSC606985 induces atypical ER-stress and cell death in prostate cancer cells

Dissociation of NSC606985 induces atypical ER-stress and cell death in prostate cancer cells

Role of endoplasmic reticulum stress in disuse osteoporosis

Transmembrane protein 215 promotes angiogenesis by maintaining endothelial cell survival

Contact Info

Product

Resources

About