KDEL proteins are found on the surface of NG108-15 cells

Gao, Xiao; Chung, Tzu-Feng; Pyun, Hae Yung; Fine, Richard E.; Johnson, Robin J.

doi:10.1016/s0169-328x(99)00188-6

Cited by 106 publications

(90 citation statements)

References 40 publications

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“…A direct link is plausible because accumulation of damaged or unfolded proteins has been known to overwhelm the retention system for chaperones like CALR thereby causing its 'escape' towards the surface. [36][37][38]43 Moreover, this correlation is further supported by the observations that while blocking caspase signaling delays the execution of apoptosis 23 without altering ecto-CALR induction 9 following Hyp-PDT-based phox-ER stress 22 yet, interference with autophagy (via ATG5-silencing) increases accumulation of oxidized proteins, 33 ecto-CALR and cell death, 33 likely by an amplification of ROSmediated ER stress (A. D. Garg and P. Agostinis, unpublished results). Last but not least, we recently found that Hyp-PDT induced an initial reticulophagy in the ER-photodamaged cells, which we revealed by the increase in the colocalization of CALR with the LC3-decorated autophagosomes.…”

Section: Discussionmentioning

confidence: 74%

“…9,37,38,[43][44][45] On the other hand, autophagy is a catabolic process that tends to remove damaged proteins like oxidized proteins and/or damaged organelles and reduce the effects of stress on a cell. 33,41,46 Since carbonylation of amino acid chains is a good indicator of the level of irreversible oxidative damage of proteins and since such proteins are marked for degradation/removal; 33,47 we next investigated the pattern of early accumulation of carbonylated or oxidatively damaged proteins in cells responding to Hyp-PDT.…”

Section: Ecto-calr Induced By Hyp-pdt Correlates With the Accumulatiomentioning

confidence: 99%

“…33,34 This is interesting, considering that the surface mobilization of CALR, which is a ROS-dependent process, 9,35 has been linked to the accumulation of damaged proteins. [35][36][37][38] Since autophagy activated by Hyp-PDT counteracts the accumulation of oxidatively damaged proteins, 33 this raises the interesting possibility that autophagy may affect Hyp-PDT-induced ecto-CALR. Moreover, it has been proposed recently that autophagy might be crucial for Hyp-PDT-elicited ATP secretion as well, 16 an avenue that needs further attention.…”

Section: Introductionmentioning

confidence: 99%

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ROS-induced autophagy in cancer cells assists in evasion from determinants of immunogenic cell death

et al. 2013

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Calreticulin surface exposure (ecto-CALR), ATP secretion, maturation of dendritic cells (DCs) and stimulation of T cells are prerequisites for anticancer therapy-induced immunogenic cell death (ICD). Recent evidence suggests that chemotherapy-induced autophagy may positively regulate ICD by favoring ATP secretion. We have recently shown that reactive oxygen species (ROS)-based endoplasmic reticulum (ER) stress triggered by hypericin-mediated photodynamic therapy (Hyp-PDT) induces bona fide ICD. However, whether Hyp-PDT-induced autophagy regulates ICD was not explored. Here we showed that, in contrast to expectations, reducing autophagy (by ATG5 knockdown) in cancer cells did not alter ATP secretion after Hyp-PDT. Autophagy-attenuated cancer cells displayed enhanced ecto-CALR induction following Hyp-PDT, which strongly correlated with their inability to clear oxidatively damaged proteins. Furthermore, autophagy-attenuation in Hyp-PDT-treated cancer cells increased their ability to induce DC maturation, IL6 production and proliferation of CD4(+) or CD8(+) T cells, which was accompanied by IFNG production. Thus, our study unravels a role for ROS-induced autophagy in weakening functional interaction between dying cancer cells and the immune system thereby helping in evasion from ICD prerequisites or determinants

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Section: Discussionmentioning

confidence: 74%

Section: Ecto-calr Induced By Hyp-pdt Correlates With the Accumulatiomentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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ROS-induced autophagy in cancer cells assists in evasion from determinants of immunogenic cell death

et al. 2013

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“…Biotinylation of Cell Surface Proteins-Cell surface biotinylation was performed as described previously (60,61). Briefly, cell monolayers were washed once with ice-cold FBS-free M199 medium and three times with ice-cold 1ϫ PBS to remove residual FBS and other proteins from the culture medium.…”

Section: Methodsmentioning

confidence: 99%

Overexpression of the 78-kDa Glucose-regulated Protein/Immunoglobulin-binding Protein (GRP78/BiP) Inhibits Tissue Factor Procoagulant Activity

Watson

Chan

Berry

et al. 2003

Journal of Biological Chemistry

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Previous studies have demonstrated that overexpression of GRP78/BiP, an endoplasmic reticulum (ER)-resident molecular chaperone, in mammalian cells inhibits the secretion of specific coagulation factors. However, the effects of GRP78/BiP on activation of the coagulation cascade leading to thrombin generation are not known. In this study, we examined whether GRP78/BiP overexpression mediates cell surface thrombin generation in a human bladder cancer cell line T24/83 having prothrombotic characteristics. We report here that cells overexpressing GRP78/BiP exhibited significant decreases in cell surface-mediated thrombin generation, prothrombin consumption and the formation of thrombin-inhibitor complexes, compared with wild-type or vector-transfected cells. This effect was attributed to the ability of GRP78/BiP to inhibit cell surface tissue factor (TF) procoagulant activity (PCA) because conversion of factor X to Xa and factor VII to VIIa were significantly lower on the surface of GRP78/BiP-overexpressing cells. The additional findings that (i) cell surface factor Xa generation was inhibited in the absence of factor VIIa and (ii) TF PCA was inhibited by a neutralizing antibody to human TF suggests that thrombin generation is mediated exclusively by TF. GRP78/BiP overexpression did not decrease cell surface levels of TF, suggesting that the inhibition in TF PCA does not result from retention of TF in the ER by GRP78/BiP. The additional observations that both adenovirus-mediated and stable GRP78/BiP overexpression attenuated TF PCA stimulated by ionomycin or hydrogen peroxide suggest that GRP78/BiP indirectly alters TF PCA through a mechanism involving cellular Ca 2؉ and/or oxidative stress. Similar results were also observed in human aortic smooth muscle cells transfected with the GRP78/BiP adenovirus. Taken together, these findings demonstrate that overexpression of GRP78/BiP decreases thrombin generation by inhibiting cell surface TF PCA, thereby suppressing the prothrombotic potential of cells.

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“…22 Lectin-like proteins have been identified on the surface of a neuroblastoma cell line, associated with many proteins in high molecular weight complexes, and one of them, calreticulin, was found to be essential for adhesion and neurite formation. 23 Other cellular receptors for extracellular matrix components have been shown to trigger signaling pathways for migration, proliferation, survival, and differentiation by modulating ion channel properties. Some types of integrins have been shown to specifically activate a member of a potassium channel family, resulting in the control of neurite extension in neuroblastoma cells.…”

Section: Acs Chemical Neurosciencementioning

confidence: 99%

Neoglucosylated Collagen Matrices Drive Neuronal Cells to Differentiate

Russo

Sgambato

Lecchi

et al. 2014

ACS Chem. Neurosci.

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Despite the relevance of carbohydrates as cues in eliciting specific biological responses, glycans have been rarely exploited in the study of neuronal physiology. We report thereby the study of the effect of neoglucosylated collagen matrices on neuroblastoma F11 cell line behavior. Morphological and functional analysis clearly showed that neoglucosylated collagen matrices were able to drive cells to differentiate. These data show for the first time that F11 cells can be driven from proliferation to differentiation without the use of chemical differentiating agents. Our work may offer to cell biologists new opportunities to study neuronal cell differentiation mechanisms in a cell environment closer to physiological conditions.

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KDEL proteins are found on the surface of NG108-15 cells

Cited by 106 publications

References 40 publications

ROS-induced autophagy in cancer cells assists in evasion from determinants of immunogenic cell death

ROS-induced autophagy in cancer cells assists in evasion from determinants of immunogenic cell death

Overexpression of the 78-kDa Glucose-regulated Protein/Immunoglobulin-binding Protein (GRP78/BiP) Inhibits Tissue Factor Procoagulant Activity

Neoglucosylated Collagen Matrices Drive Neuronal Cells to Differentiate

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