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Kv channel interacting protein 1 gene (KCNIP1), a member of KCNIP family, plays crucial roles in modulating insulin secretion of pancreatic β cells at a Ca2+-dependent manner by binding to a specific downstream regulatory element site. It has been demonstrated that KCNIP1 is expressed in the mammalian atrium, especially highly expressed in pancreatic cells. It has been reported that KCNIP1 knockdown antagonized β-cell repolarization and facilitated insulin secretion in a glucose-dependent pattern. In addition, genome-wide copy number variations (CNVs) screening in human genome has identified KCNIP1 encompassing a CNV region, which was also found in the database of genomic variants.
Atrial fibrillation (AF) is the most common sustained cardiac arrhythmia. Previous genome-wide association studies have identified single nucleotide polymorphisms associated with AF in several genomic regions, CNVs are known to contribute to diseases susceptibility. It is reported that KCNIP1 is physically associated with potassium Kv channels and modulates atrial transient outward current in cardiac myocytes. In the mammalian atrium, KCHIP1 formed a protein complex with Kv4.2/4.3 and modulated the atrial transient outward current, thus modulating atrial repolarization properties. The intracellular calcium level plays a pivotal role in the mechanism of AF. At high atrial rates, the intracellular calcium level is accumulated and elevated due to the short time available for beat-to-beat diastolic calcium reuptake into the sarcoplasmic reticulum, thereby triggering atrial electrical remodelling (for example, APD shortening) and facilitating the maintenance of AF. In the zebrafish model, it has been shown that genetic over-expression of KCNIP1 resulted in facilitation of APD to shorten at high rates and promotes AF.
In Xenopus embryos, KCNIP1 is expressed throughout embryonic development and is the only KCNIP family member that is expressed during gastrulation. It has been demonstrated that Kcnip1 possesses a Ca2+-dependent DRE-binding activity. According to the cellular models, KCNIP proteins have been shown to positively or negatively affect cell proliferation by controlling cell-cycle regulators. One report shows that the loss-of-function of kcnip1 positively controls proliferation by increasing foxm1 and reducing the cyclin-dependent kinase inhibitor p27xic1.