Regulation of endothelial monocyte-activating polypeptide II release by apoptosis

Knies, Ulrike E.; Behrensdorf, Heike A.; Mitchell, Christopher A.; Deutsch, Urban; Risau, Werner; Drexler, Hannes C.A.; Clauss, Matthias

doi:10.1073/pnas.95.21.12322

Cited by 148 publications

(162 citation statements)

References 33 publications

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“…Both require proteolytic processing to gain their chemotactic properties. 53 While EMAPII requires processing from the pro-EMAPII form, most likely through caspase 7 cleavage, 54 TyrRS cleavage is thought to occur by neutrophil-released elastase. 55 Of note, the C-terminal cleavage product of TyrRS shares homology (49%) with EMAPII.…”

Section: Steps Involved In Clearancementioning

confidence: 99%

“…57 EMAPII and TyrRS release likely occur relatively late in the apoptotic process, suggesting that they may be released during secondary necrosis of these cells. 53,54 Last, although authors were able to show that apoptotic cells secreted EMAPII and TyrRS and that these could in turn mediate chemotaxis, these studies lacked direct evidence proving that they are the chemotactic component in apoptotic cell supernatants.…”

Section: Steps Involved In Clearancementioning

confidence: 99%

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Do not let death do us part: ‘find-me’ signals in communication between dying cells and the phagocytes

2016

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The turnover and clearance of cells is an essential process that is part of many physiological and pathological processes. Improper or deficient clearance of apoptotic cells can lead to excessive inflammation and autoimmune disease. The steps involved in cell clearance include: migration of the phagocyte toward the proximity of the dying cells, specific recognition and internalization of the dying cell, and degradation of the corpse. The ability of phagocytes to recognize and react to dying cells to perform efficient and immunologically silent engulfment has been well-characterized in vitro and in vivo. However, how apoptotic cells themselves initiate the corpse removal and also influence the cells within the neighboring environment during clearance was less understood. Recent exciting observations suggest that apoptotic cells can attract phagocytes through the regulated release of 'find-me' signals. More recent studies also suggest that these find-me signals can have additional roles outside of phagocyte attraction to help orchestrate engulfment. This review will discuss our current understanding of the different find-me signals released by apoptotic cells, how they may be relevant in vivo, and their additional roles in facilitating engulfment.

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Section: Steps Involved In Clearancementioning

confidence: 99%

Section: Steps Involved In Clearancementioning

confidence: 99%

Do not let death do us part: ‘find-me’ signals in communication between dying cells and the phagocytes

2016

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“…17,18 Until now, only endothelial monocyte-activating polypeptide II (EMAP II) has been identified as an apoptotic cell-derived molecule with proinflammatory and chemotactic properties. 19 EMAP II is generated via cleavage by caspase-7 of the p43 subunit of the tRNA synthetase complex. 20 Here we report that caspases-3 and -7, involved in the execution of anti-Fas-induced apoptosis, are released in the cell culture supernatant during secondary necrosis.…”

Section: Introductionmentioning

confidence: 99%

Death receptor-induced apoptotic and necrotic cell death: differential role of caspases and mitochondria

et al. 2001

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In L929sAhFas cells, tumor necrosis factor (TNF) leads to necrotic cell death, whereas agonistic anti-Fas antibodies elicit apoptotic cell death. Apoptosis, but not necrosis, is correlated with a rapid externalization of phosphatidylserine and the appearance of a hypoploid population. During necrosis no cytosolic and organelle-associated active caspase-3 and -7 fragments are detectable. The necrotic process does not involve proteolytic generation of truncated Bid; moreover, no mitochondrial release of cytochrome c is observed. Bcl-2 overexpression slows down the onset of necrotic cell death. In the case of apoptosis, active caspases are released to the culture supernatant, coinciding with the release of lactate dehydrogenase. Following necrosis, mainly unprocessed forms of caspases are released. Both TNFinduced necrosis and necrosis induced by anti-Fas in the presence of the caspase inhibitor benzyloxycarbonyl-Val-AlaAsp(OMe)-fluoromethylketone are prevented by the serine protease inhibitor N-tosyl-L-phenylalanine chloromethylketone and the oxygen radical scavenger butylated hydroxyanisole, while Fas-induced apoptosis is not affected. Cell Death and Differentiation (2001) 8, 829 ± 840.

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“…The precursor of endothelial monocyte-activating polypeptide II is associated with the N-terminal noncatalytic extension of arginyl-tRNA synthetase and enhances aminoacylation activity (20). Like human tyrosyl-tRNA synthetase, the cytokine domain of this precursor is released upon apoptosis and exerts its proapoptotic function (21,22).…”

mentioning

confidence: 99%

Glutamine-dependent Antiapoptotic Interaction of Human Glutaminyl-tRNA Synthetase with Apoptosis Signal-regulating Kinase 1

Ko¹,

Kim²,

Kim³

et al. 2001

Journal of Biological Chemistry

182

123

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Glutamine has been known to be an apoptosis suppressor, since it blocks apoptosis induced by heat shock, irradiation, and c-Myc overexpression. Here, we demonstrated that HeLa cells were susceptible to Fas-mediated apoptosis under the condition of glutamine deprivation. Fas ligation activated apoptosis signalregulating kinase 1 (ASK1) and c-Jun N-terminal kinase (JNK; also known as stress-activated protein kinase (SAPK)) in Gln-deprived cells but not in normal cells, suggesting that Gln might be involved in the activity control of ASK1 and JNK/SAPK. As one of the possible mechanisms for the suppressive effect of Gln on ASK1, we investigated the molecular interaction between human glutaminyl-tRNA synthetase (QRS) and ASK1 and found the Gln-dependent association of the two molecules. While their association was enhanced by the elevation of Gln concentration, they were dissociated by Fas ligation within 5 min. The association involved the catalytic domains of the two enzymes. The ASK1 activity was inhibited by the interaction with QRS as determined by in vitro kinase and transcription assays. Finally, we have shown that QRS inhibited the cell death induced by ASK1, and this antiapoptotic function of QRS was weakened by the deprivation of Gln. Thus, the antiapoptotic interaction of QRS with ASK1 is controlled positively by the cellular concentration of Gln and negatively by Fas ligation. The results of this work provide one possible explanation for the working mechanism of the antiapoptotic activity of Gln and suggest a novel function of mammalian ARSs.

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Regulation of endothelial monocyte-activating polypeptide II release by apoptosis

Cited by 148 publications

References 33 publications

Do not let death do us part: ‘find-me’ signals in communication between dying cells and the phagocytes

Do not let death do us part: ‘find-me’ signals in communication between dying cells and the phagocytes

Death receptor-induced apoptotic and necrotic cell death: differential role of caspases and mitochondria

Glutamine-dependent Antiapoptotic Interaction of Human Glutaminyl-tRNA Synthetase with Apoptosis Signal-regulating Kinase 1

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