Solea senegalensis genes responding to lipopolysaccharide and copper sulphate challenges: Large-scale identification by suppression subtractive hybridization and absolute quantification of transcriptional profiles by real-time RT-PCR

Prieto‐Álamo, María‐José; Abril, Nieves; Osuna-Jiménez, Inmaculada; Pueyo, Carmen

doi:10.1016/j.aquatox.2008.11.001

Cited by 40 publications

(15 citation statements)

References 53 publications

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“…In a recent study by Prieto-Alamo et al [49], it was found that in the fish Solea senegalensis, M ferritin expression was upregulated by CuSO 4 in both liver and kidney. Similarly, in our study, we found that significant induction of SoFer1 expression occurred following copper exposure.…”

Section: Discussionmentioning

confidence: 97%

Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus)

Zheng

Sun

2010

Fish & Shellfish Immunology

107

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Section: Discussionmentioning

confidence: 97%

Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus)

Zheng

Sun

2010

Fish & Shellfish Immunology

107

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“…LPS is a classical endotoxin and can induce drastic immune responses by promoting the secretion of a number of pro-inflammatory cytokines [51], some of which, such as tumor necrosis factor and interleukin 1, are documented as stimulators of ferritin production [52e54]. For aquaculture animals, it is known that LPS upregulates the expression of H ferritins in echinoderm (Asterias forbesi) coelomocytes [55] and horseshoe crab (Carcinoscorpius rotundicauda) [56] but down-regulates the expression of M ferritin in Solea senegalensis [57]. In the context of these previous observations, our results suggest that LPS elevates the expression of at least H ferritin, which may account for the strong inducing effect observed with L. anguillarum and E. tarda infections but not with S. iniae infection.…”

Section: Discussionmentioning

confidence: 99%

Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus)

Zheng

Xiao

et al. 2010

Fish & Shellfish Immunology

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“…These temperature‐dependent CIRP expression studies have been conducted mostly in neurons, fibroblasts, and male germ cells . CIRP can also be induced by a wide range of stimuli such as endotoxemia, hypoxia, radiation, toxins, and drugs in a temperature‐independent manner . The temperature‐independent CIRP's expression studies such as in hypoxia and endotoxemia were performed mainly on macrophages .…”

Section: Facts and Findings: Temperature‐dependent And ‐Independent Ementioning

confidence: 99%

Extracellular CIRP (eCIRP) and inflammation

Aziz

Brenner

Wang

2019

Journal of Leukocyte Biology

135

170

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Cold-inducible RNA-binding protein (CIRP) was discovered 2 decades ago while studying the mechanism of cold stress adaptation in mammals. Since then, the role of intracellular CIRP (iCIRP) as a stress-response protein has been extensively studied. Recently, extracellular CIRP (eCIRP) was discovered to also have an important role, acting as a damage-associated molecular pattern, raising critical implications for the pathobiology of inflammatory diseases. During hemorrhagic shock and sepsis, inflammation triggers the translocation of CIRP from the nucleus to the cytosol and its release to the extracellular space. eCIRP then induces inflammatory responses in macrophages, neutrophils, lymphocytes, and dendritic cells. eCIRP also induces endoplasmic reticulum stress and pyroptosis in endothelial cells by activating the NF-B and inflammasome pathways, and necroptosis in macrophages via mitochondrial DNA damage. eCIRP works through the TLR4-MD2 receptors. Studies with CIRP −/− mice reveal protection against inflammation, implicating eCIRP to be a novel drug target. Anti-CIRP Ab or CIRP-derived small peptide may have effective therapeutic potentials in sepsis, acute lung injury, and organ ischemia/reperfusion injuries. The current review focuses on the pathobiology of eCIRP by emphasizing on signal transduction machineries, leading to discovering novel therapeutic interventions targeting eCIRP in various inflammatory diseases. K E Y W O R D S ALI, CIRP, DAMP, eCIRP, hemorrhage, inflammation, ischemia/reperfusion, macrophage, neutrophils, sepsis PMN, polymorphonuclear neutrophils; RA, rheumatoid arthritis; RM, reverse migrated; rTEM, reverse transendothelial migration; STAT3, signal transducer and activator of transcription 3; TRPV, transient receptor potential vanilloid; UC, ulcerative colitis telomerase maintenance, 7 stress adaptation, 8 and tumor formation and progression. 9,10 These iCIRP activities, which allow cells to cope with various cellular stress conditions, have been reviewed in detail. 8 In contrast to iCIRP, extracellular CIRP (eCIRP) was recently discovered to act as a damage-associated molecular pattern (DAMP) promoting inflammation and injury. 11 The identification of eCIRP as a new DAMP has originated a new era of investigation in inflammation pathobiology. Serum levels of eCIRP not only were found to be elevated in individuals admitted to the intensive care unit (ICU)with hemorrhagic shock (HS), but also correlated with organ injury. 11 Furthermore, it was demonstrated that eCIRP was able to promote inflammation independently. 11 In cells subjected to hypoxia, CIRP translocates from its usual location in the nucleus to the cytosol 1,12 and is then released to the extracellular space. 11 eCIRP then acts as a DAMP increasing macrophage production of proinflammatory cytokines. 11 Since its original discovery as a DAMP, eCIRP's emerging proinflammatory role has been progressively extended to include additional target cells, such as neutrophils, lymphocytes, epithelial cells, and endothelial cells. 13-2...

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Solea senegalensis genes responding to lipopolysaccharide and copper sulphate challenges: Large-scale identification by suppression subtractive hybridization and absolute quantification of transcriptional profiles by real-time RT-PCR

Cited by 40 publications

References 53 publications

Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus)

Identification and molecular analysis of a ferritin subunit from red drum (Sciaenops ocellatus)

Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus)

Extracellular CIRP (eCIRP) and inflammation

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