ArticleAnnals of translational medicine2021
Cold-inducible RNA-binding protein migrates from the nucleus to the cytoplasm under cold stress in normal human bronchial epithelial cells via TRPM8-mediated mechanism.
Article in Annals of translational medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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9 authors at 3 institutions in 1 country.
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Abstract
backgroundCold-inducible RNA-binding protein (CIRP or hnRNP A18) is a multifunctional stress-responsive protein. Our previous study demonstrated that cold stress increased CIRP expression and migrated from the nucleus to the cytoplasm in airway epithelial cells. However, the mechanism through which CIRP migrates from the nucleus to the cytoplasm upon cold stress remains unknown.
methodsThe expression of CIRP in the bronchial epithelium was examined using immunofluorescence, real-time polymerase chain reaction (RT-PCR), and Western blotting. The expression of inflammatory factors interleukin-1β (IL-1β), interleukin-6 (IL-6), interleukin-8 (IL-8), and tumor necrosis factor-α (TNF-α) were detected by ELISA and RT-PCR. Transient receptor potential melastatin 8 (TRPM8) receptor function was characterized by Ca
resultsCold stress upregulated the expression of CIRP, inflammatory factors and promoted the translocation of CIRP from the nucleus to the cytoplasm in normal human bronchial epithelial (NHBE) cells. Cold stress activated the TRPM8/(Ca
conclusionsThese results indicate that cold stress leads to the migration of CIRP from the nucleus to the cytoplasm with alteration of expression, which are involved in the expression of inflammatory factors (IL-1β, IL-6, IL-8 and TNF-α) induced by cold air, through TRPM8/Ca
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