A Missense Variation in Human Casein Kinase I Epsilon Gene that Induces Functional Alteration and Shows an Inverse Association with ... View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2004-10

AUTHORS

Atsuko Takano, Makoto Uchiyama, Naofumi Kajimura, Kazuo Mishima, Yuichi Inoue, Yuichi Kamei, Tsuyoshi Kitajima, Kayo Shibui, Masaaki Katoh, Tsuyoshi Watanabe, Yuki Hashimotodani, Toru Nakajima, Yuji Ozeki, Toru Hori, Naoto Yamada, Ryoichi Toyoshima, Norio Ozaki, Masako Okawa, Katsuya Nagai, Kiyohisa Takahashi, Yasushi Isojima, Toshio Yamauchi, Takashi Ebisawa

ABSTRACT

Recent studies have shown that functional variations in clock genes, which generate circadian rhythms through interactive positive/negative feedback loops, contribute to the development of circadian rhythm sleep disorders in humans. Another potential candidate for rhythm disorder susceptibility is casein kinase I epsilon (CKIepsilon), which phosphorylates clock proteins and plays a pivotal role in the circadian clock. To determine whether variations in CKIepsilon induce vulnerability to human circadian rhythm sleep disorders, such as delayed sleep phase syndrome (DSPS) and non-24-h sleep-wake syndrome (N-24), we analyzed all of the coding exons of the human CKIepsilon gene. One of the variants identified encoded an amino-acid substitution S408N, eliminating one of the putative autophosphorylation sites in the carboxyl-terminal extension of CKIepsilon. The N408 allele was less common in both DSPS (p = 0.028) and N-24 patients (p = 0.035) compared to controls. When DSPS and N-24 subjects were combined, based on an a priori prediction of a common mechanism underlying both DSPS and N-24, the inverse association between the N408 allele and rhythm disorders was highly significant (p = 0.0067, odds ratio = 0.42, 95% confidence interval: 0.22-0.79). In vitro kinase assay revealed that CKIepsilon with the S408N variation was approximately 1.8-fold more active than wild-type CKIepsilon. These results indicate that the N408 allele in CKIepsilon plays a protective role in the development of DSPS and N-24 through alteration of the enzyme activity. More... »

PAGES

1300503

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/sj.npp.1300503

DOI

http://dx.doi.org/10.1038/sj.npp.1300503

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1040136593

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15187983


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