Cold Shock Proteins Are Expressed in the Retina Following Exposure to Low Temperatures

Larráyoz, Ignacio M.; Rey-Funes, Manuel; Contartese, Daniela S; Rolón, Federico; Sarotto, Aníbal; Dorfman, Verónica Berta; Loidl, César Fabián; Martı́nez, Alfredo

doi:10.1371/journal.pone.0161458

Cited by 25 publications

(32 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Bullfrog CIRP is 72.7% similar to mammalian CIRPs and 78.54% to Xenopus laevis ’ CIRP [ 4 ]. The amino acid sequence of CIRP in different species is shown in Figure 1 B. CIRP is ubiquitously expressed in a large variety of tissues and cells from both human and murine origins, including the brain, lungs, heart, kidneys, retinas, testis, liver, ovaries, nervous system, lymphocytes and endometrium [ 5 ]. CIRP is mainly localized in the nucleus, but can translocate to the cytoplasm under stress conditions.…”

mentioning

confidence: 99%

Recent progress in the research of cold-inducible RNA-binding protein

2017

View full text Add to dashboard Cite

Cold-inducible RNA-binding protein (CIRP) is a cold-shock protein which can be induced after exposure to a moderate cold-shock in different species ranging from amphibians to humans. Expression of CIRP can also be regulated by hypoxia, UV radiation, glucose deprivation, heat stress and H2O2, suggesting that CIRP is a general stress-response protein. In response to stress, CIRP can migrate from the nucleus to the cytoplasm and regulate mRNA stability through its binding site on the 3′-UTR of its targeted mRNAs. Through the regulation of its targets, CIRP has been implicated in multiple cellular process such as cell proliferation, cell survival, circadian modulation, telomere maintenance and tumor formation and progression. In addition, CIRP can also exert its functions by directly interacting with intracellular signaling proteins. Moreover, CIRP can be secreted out of cells. Extracellular CIRP functions as a damage-associated molecular pattern to promote inflammatory responses and plays an important role in both acute and chronic inflammatory diseases. Here, we summarize novel findings of CIRP investigation and hope to provide insights into the role of CIRP in cell biology and diseases.

show abstract

mentioning

confidence: 99%

Recent progress in the research of cold-inducible RNA-binding protein

2017

View full text Add to dashboard Cite

show abstract

“…After a period of 45 min of recovery at room temperature (24 °C), some of the rats were subjected to hypothermia in a cold room (8 °C for 3 h) while the rest remained at 24 °C (normothermia). In previous studies we have shown that 3h at 8 °C produces a temperature drop in the rat of approximately 3 °C 35 . To calculate changes in retro-ocular temperature, some animals kept at normothermia (n = 5) and some animals that had just received the hypothermic treatment (n = 5) were deeply anesthetized and a thermocouple (type K, model TPK-01, Tecpel, Taiwan), connected to a digital thermometer (TES-1300, Tecpel), was placed in the orbital fossa and the temperature was rapidly recorded.…”

Section: Methodsmentioning

confidence: 85%

“…A subset of rats (n = 6 per experimental group) were sacrificed 3 h after hypothermic or normothermic treatment. The posterior chambers of the eyes were homogenized with TRIzol (Invitrogen, Madrid, Spain) and RNA was isolated and reverse transcribed as previously reported 35 . Resulting cDNA was mixed with SYBR Green PCR Master Mix (Applied Biosystems, Carlsbad, CA) for quantitative real time polymerase chain reaction (qRT-PCR) using 0.3 µM forward and reverse oligonucleotide primers (Table 1 ).…”

Section: Methodsmentioning

confidence: 99%

“…These proteins, which belong to the heterogeneous nuclear ribonucleoprotein family, bind to cellular RNAs and regulate their half-life and thus their expression potential and their final functions 30 – 34 . The expression of these proteins in the rat retina has been recently characterized 35 and they may be part of the mechanism by which hypothermia prevents tissue damage.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Hypothermia Prevents Retinal Damage Generated by Optic Nerve Trauma in the Rat

Rey-Funes

Larráyoz

Contartese

et al. 2017

Sci Rep

Self Cite

View full text Add to dashboard Cite

Ocular and periocular traumatisms may result in loss of vision. Hypothermia provides a beneficial intervention for brain and heart conditions and, here, we study whether hypothermia can prevent retinal damage caused by traumatic neuropathy. Intraorbital optic nerve crush (IONC) or sham manipulation was applied to male rats. Some animals were subjected to hypothermia (8 °C) for 3 h following surgery. Thirty days later, animals were subjected to electroretinography and behavioral tests. IONC treatment resulted in amplitude reduction of the b-wave and oscillatory potentials of the electroretinogram, whereas the hypothermic treatment significantly (p < 0.05) reversed this process. Using a descending method of limits in a two-choice visual task apparatus, we demonstrated that hypothermia significantly (p < 0.001) preserved visual acuity. Furthermore, IONC-treated rats had a lower (p < 0.0001) number of retinal ganglion cells and a higher (p < 0.0001) number of TUNEL-positive cells than sham-operated controls. These numbers were significantly (p < 0.0001) corrected by hypothermic treatment. There was a significant (p < 0.001) increase of RNA-binding motif protein 3 (RBM3) and of BCL2 (p < 0.01) mRNA expression in the eyes exposed to hypothermia. In conclusion, hypothermia constitutes an efficacious treatment for traumatic vision-impairing conditions, and the cold-shock protein pathway may be involved in mediating the beneficial effects shown in the retina.

show abstract

“…In addition to homologues and orthologues, CIRP has at least two paralogues: RNA‐binding motif protein 3 (RBM3)—an RNA‐binding protein up‐regulated in response to low temperature and aggrecan promoter‐binding protein‐1 (APBP‐1)—a 19‐kDa DNA/RNA‐binding protein . CIRP is constitutively and ubiquitously expressed at low levels, with studies showing its presence in the brain, lungs, heart, liver, kidneys, and endometrium, as well as in macrophages and neutrophils . Recently, both CIRP expression and release have been shown to be induced in cellular stress and inflammatory conditions .…”

Section: Cirpmentioning

confidence: 99%

Extracellular CIRP (eCIRP) and inflammation

Aziz

Brenner

Wang

2019

Journal of Leukocyte Biology

148

188

View full text Add to dashboard Cite

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...

show abstract

Cold Shock Proteins Are Expressed in the Retina Following Exposure to Low Temperatures

Cited by 25 publications

References 40 publications

Recent progress in the research of cold-inducible RNA-binding protein

Recent progress in the research of cold-inducible RNA-binding protein

Hypothermia Prevents Retinal Damage Generated by Optic Nerve Trauma in the Rat

Extracellular CIRP (eCIRP) and inflammation

Contact Info

Product

Resources

About