Abstract
Cold-inducible RNA-binding protein (CIRP) is an intracellular stress-response protein that can respond to various stress conditions by changing its expression and regulating mRNA stability. As an RNA-binding protein, CIRP modulates gene expression at the post-transcriptional level, including those genes involved in DNA repair, cellular redox metabolism, circadian rhythms, telomere maintenance, and cell survival. CIRP is expressed in a large variety of tissues, including testis, brain, lung, kidney, liver, stomach, bone marrow, and heart. Recent studies have observed the important role of CIRP in cardiac physiology and diseases. CIRP regulates cardiac electrophysiological properties such as the repolarization of cardiomyocytes, the susceptibility of atrial fibrillation, and the function of the sinoatrial node in response to stress. CIRP has also been suggested to protect cardiomyocytes from apoptosis under various stress conditions, including heart failure, high glucose conditions, as well as during extended heart preservation under hypothermic conditions. This review summarizes the findings of CIRP investigations in cardiac physiology and diseases and the underlying molecular mechanism.
Highlights
Cold-inducible RNA binding protein (CIRP) was first discovered two decades ago
This study demonstrates the important role of Cold-inducible RNA-binding protein (CIRP) in atrial electrophysiology and in initiating atrial fibrillation (AF) onset by directly regulating the expression of the Kv1.5 and Kv4.2/4.3 channels posttranscriptionally, indicating that CIRP could be a promising potential target for interventions in AF
We found that CIRP protein levels were significantly reduced in heart samples from both patients with heart failure (HF) and mice with post-myocardial infarction, compared to that in the control samples, suggesting a possible involvement of CIRP in the HF development
Summary
Cold-inducible RNA binding protein (CIRP) was first discovered two decades ago. It came to the attention of researchers because its expression was induced after cells were exposed to a moderate cold shock. Later studies showed that the expression of CIRP could be regulated by hypoxia, UV radiation, glucose deprivation, heat stress, and H2O2, suggesting that CIRP is a general stressresponse protein (Zhong and Huang, 2017). As an RNA-binding protein, CIRP modulates mRNA stability at the post-transcriptional level through directly binding the 3′-UTR of its targets in the cytosol (Yang et al, 2010) (Yang et al, 2006; Zhong and Huang, 2017).
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