Novel TRPV6 mutations in the spectrum of transient neonatal hyperparathyroidism

The Journal of Physiological Sciences - Tập 70 - Trang 1-10 - 2020
Yoshiro Suzuki1,2,3, Hirotake Sawada4, Tomoko Tokumasu5, Shigeru Suzuki6,7, Shinsuke Ninomiya8, Masaru Shirai6, Tokuo Mukai6,9, Claire T. Saito2, Gen Nishimura10, Makoto Tominaga2,3
1Department of Physiology, Iwate Medical University, Iwate, Japan
2Division of Cell Signaling, National Institute for Physiological Sciences (Exploratory Research Center on Life and Living Systems), National Institutes of Natural Sciences, Okazaki, Japan
3Department of Physiological Sciences, SOKENDAI (The Graduate University for Advanced Studies), Okazaki, Japan
4Department of Fundamental Nursing, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan
5Department of Pediatrics, Kurashiki Central Hospital, Kurashiki, Japan
6Department of Pediatrics, Asahikawa-Kosei General Hospital, Asahikawa, Japan
7Department of Pediatrics, Asahikawa Medical University, Asahikawa, Japan
8Department of Clinical Genetics, Kurashiki Central Hospital, Kurashiki, Japan
9Department of Pediatrics, Japanese Red Cross Asahikawa Hospital, Asahikawa, Japan
10Center for Intractable Disease, Saitama Medical University Hospital, Saitama, Japan

Tóm tắt

Maternal–fetal calcium (Ca2+) transport in the placenta plays a critical role in maintaining fetal bone mineralization. Mutations in the gene encoding the transient receptor potential cation channel, subfamily V, member 6 (TRPV6) have been identified as causative mutations of transient neonatal hyperparathyroidism due to insufficient maternal–fetal Ca2+ transport in the placenta. In this study, we found two novel mutations in subjects that have transient neonatal hyperparathyroidism. TRPV6 carrying the mutation p.Arg390His that localizes to the outer edge of the first transmembrane domain (S1) showed impaired trafficking to the plasma membrane, whereas TRPV6 having the mutation p.Gly291Ser in the sixth ankyrin repeat (AR) domain had channel properties that were comparable those of WT channels, although the increases in steady-state intracellular Ca2+ concentration could have led to Ca2+ overload and subsequent death of cells expressing this mutant channel. These results indicate that the AR6 domain contributes to TRPV6-mediated maintenance of intracellular Ca2+ concentrations, and that this region could play a novel role in regulating the activity of TRPV6 Ca2+-selective channels.

Tài liệu tham khảo

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