Post-translational regulation of interleukin 1β secretion

Rubartelli, Anna; Bajetto, Adriana; Allavena, G; Cozzolino, Federico; Sitia, Roberto

doi:10.1016/1043-4666(93)90050-f

Cited by 79 publications

(80 citation statements)

References 34 publications

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“…3B). Another thioredoxin, Trx1, is secreted via an endoplasmic reticulum-Golgi-independent pathway (38). However, although we could confirm the secretion of Trx1 into the growth medium, Txnl1, like the proteasome, was exclusively present in the interior of HeLa cells (Fig.…”

Section: Txnl1 Is a Novel Proteasome Componentcontrasting

confidence: 38%

Thioredoxin Txnl1/TRP32 Is a Redox-active Cofactor of the 26 S Proteasome

Andersen

Madsen

Prag

et al. 2009

Journal of Biological Chemistry

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The 26 S proteasome is a large proteolytic machine, which degrades most intracellular proteins. We found that thioredoxin, Txnl1/TRP32, binds to Rpn11, a subunit of the regulatory complex of the human 26 S proteasome. Txnl1 is abundant, metabolically stable, and widely expressed and is present in the cytoplasm and nucleus. Txnl1 has thioredoxin activity with a redox potential of about ؊250 mV. Mutant Txnl1 with one active site cysteine replaced by serine formed disulfide bonds to eEF1A1, a substrate-recruiting factor of the 26 S proteasome. eEF1A1 is therefore a likely physiological substrate. In response to knockdown of Txnl1, ubiquitin-protein conjugates were moderately stabilized. Hence, Txnl1 is the first example of a direct connection between protein reduction and proteolysis, two major intracellular protein quality control mechanisms.

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Section: Txnl1 Is a Novel Proteasome Componentcontrasting

confidence: 38%

Thioredoxin Txnl1/TRP32 Is a Redox-active Cofactor of the 26 S Proteasome

Andersen

Madsen

Prag

et al. 2009

Journal of Biological Chemistry

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“…Despite the fact that the SPTRX-3 expression pattern is coincidental with other Golgi-specific proteins, it lacks a clear signal sequence to follow the ER/Golgi pathway. A leaderless pathway independent of ER/Golgi has been proposed for the secretion of some other proteins, including TRX-1 (52,53). Regardless of the clear sequence conservation, SPTRX-3 is not expected to follow the ER/Golgi pathway because it localizes exclusively within the Golgi apparatus, and there is no evidence for ER localization or secretion of SPTRX-3.…”

Section: Sptrx-3 a Novel Golgi Apparatus-associated Thioredoxinmentioning

confidence: 99%

Spermatocyte/Spermatid-specific Thioredoxin-3, a Novel Golgi Apparatus-associated Thioredoxin, Is a Specific Marker of Aberrant Spermatogenesis

Jiménez

Wei

Rawe

et al. 2004

Journal of Biological Chemistry

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Mammalian germ cells are endowed with a complete set of thioredoxins (Trx), a class of redox proteins located in specific structures of the spermatid and sperm tail. We report here the characterization, under normal and pathological conditions, of a novel thioredoxin with a germ line-restricted expression pattern, named spermatocyte/spermatid-specific thioredoxin-3 (SPTRX-3). The human SPTRX-3 gene maps at 9q32, only 50 kb downstream from the TRX-1 gene from which it probably originated as genomic duplication. Therefore, human SPTRX-3 protein comprises a unique thioredoxin domain displaying high homology with the ubiquitously expressed TRX-1. Among the tissues investigated, Sptrx-3 mRNA is found exclusively in the male germ cells at pachytene spermatocyte and round spermatid stages. Light and electron microscopy show SPTRX-3 protein to be predominately located in the Golgi apparatus of pachytene spermatocytes and round and elongated spermatids, with a transient localization in the developing acrosome of round spermatids. In addition, increased levels of SPTRX-3, possibly caused by overexpression, are observed in morphologically abnormal human spermatozoa from infertile men. In addition, SPTRX-3 is identified as a novel postobstruction autoantigen. In this report, we propose that SPTRX-3 can be used as a specific marker for diverse sperm and testis pathologies. SPTRX-3 is the first thioredoxin specific to the Golgi apparatus, and its function within this organelle might be related to the post-translational modification of proteins required for germ cell-specific functions, such as acrosomal biogenesis.

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“…Previous studies have demonstrated that the secretion of IL-1β is as an active, mature cytokine through activation of different receptors [4]. The synthesis of IL-1β precursor (pro-IL-1β) is induced by stimulation of TLR4, and the release of mature IL-1β cleaved by a cysteine protease called caspase-1 is induced by stimulation of P2X purinoreceptors by ATP [5,6]. However, the mechanisms of morphine-induced IL-1β release in microglia are still unclear.…”

Section: Introductionmentioning

confidence: 99%

Morphine enhances IL-1β release through toll-like receptor 4-mediated endocytic pathway in microglia

Liang

Jiang

et al. 2016

Purinergic Signalling

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Morphine creates a neuroinflammatory response and enhances release of the proinflammatory cytokines like interleukin-1β (IL-1β), which compromises morphine analgesia as well as induces morphine tolerance. In this study, we attempted to investigate the mechanisms of morphine induced IL-1β synthesis and release. Microglial cells were treated with morphine (100 μM) once daily for 3 days. Control groups underwent the same procedure but received sterile saline injection instead of morphine. Toll-like receptor 4 (TLR4) and P2X4 receptor (P2X4R) signaling were analyzed using Western blot; immunofluorescence was used to detect the signaling of CD68; real-time RT-PCR and ELISA kit was used to measure the messenger RNA and protein synthesis and release level of IL-1β. Morphine enhanced IL-1β synthesis and P2X4R protein expression. TLR4 were responsible for morphine-induced IL-1β synthesis, while morphineinduced IL-1β release was via P2X4R. Morphineinduced IL-1β release is mediated by endocytosis of TLR4. These results indicated that TLR4 and P2X4R pathways mediated IL-1β synthesis and release in microglia followed chronic morphine. TLR4 internalization is the main mechanism of morphine-induced microglia activation and IL-1β release.

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Post-translational regulation of interleukin 1β secretion

Cited by 79 publications

References 34 publications

Thioredoxin Txnl1/TRP32 Is a Redox-active Cofactor of the 26 S Proteasome

Thioredoxin Txnl1/TRP32 Is a Redox-active Cofactor of the 26 S Proteasome

Spermatocyte/Spermatid-specific Thioredoxin-3, a Novel Golgi Apparatus-associated Thioredoxin, Is a Specific Marker of Aberrant Spermatogenesis

Morphine enhances IL-1β release through toll-like receptor 4-mediated endocytic pathway in microglia

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