Abstract

Cold-inducible RNA-binding protein (CIRP) is an 18-kDa nuclear protein belonging to the family of cold-shock proteins. It is widely expressed in various tissues and upregulated in response to various cellular stresses. Originally, CIRP was found to stabilize specific mRNAs to facilitate their translation, which results in a survival advantage for cells under stress. Hypothermia-induced CIRP has been shown to protect the neuronal system. Recently, CIRP was found to be a multifunctional protein. In addition to acting as a damage-associated molecular pattern molecule to promote inflammation, it was also found to affect tumorigenesis. CIRP was also found to regulate telomerase activity and cardiac repolarization. Therefore, biological activities of CIRP in novel systems should receive more attention. This review will provide a brief introduction to the recent studies of CIRP with the aim of inspiring future research of novel CIRP functions.

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