Molecular and cellular basis of hypophosphatasia.


Journal

Journal of oral biosciences
ISSN: 1880-3865
Titre abrégé: J Oral Biosci
Pays: Netherlands
ID NLM: 101226721

Informations de publication

Date de publication:
09 2019
Historique:
received: 15 05 2019
revised: 10 07 2019
accepted: 11 07 2019
pubmed: 11 8 2019
medline: 28 3 2020
entrez: 11 8 2019
Statut: ppublish

Résumé

Hypophosphatasia (HPP) is an inherited disorder characterized by defective mineralization of the bone and teeth that is also associated with a deficiency of serum alkaline phosphatase (ALP). Patients with HPP exhibit a broad range of symptoms including stillbirth with an unmineralized skeleton, premature exfoliation and dental caries in childhood, and pseudo-fractures in adulthood. The broad clinical spectrum of HPP is attributed to various mutations in the ALPL gene, which encodes tissue-nonspecific alkaline phosphatase (TNSALP). Nevertheless, the molecular mechanisms underlying the genotypic and phenotypic relationship of HPP remain unclear. The expression of HPP-related TNSALP mutants in mammalian cells allows us to determine for the effects of mutations on the properties of TNSALP, which could contribute to a better understanding of the relationship between structure and function of TNSALP. Molecular characterization of TNSALP mutants helps establish the etiology and onset of HPP.

Sections du résumé

BACKGROUND
Hypophosphatasia (HPP) is an inherited disorder characterized by defective mineralization of the bone and teeth that is also associated with a deficiency of serum alkaline phosphatase (ALP). Patients with HPP exhibit a broad range of symptoms including stillbirth with an unmineralized skeleton, premature exfoliation and dental caries in childhood, and pseudo-fractures in adulthood. The broad clinical spectrum of HPP is attributed to various mutations in the ALPL gene, which encodes tissue-nonspecific alkaline phosphatase (TNSALP). Nevertheless, the molecular mechanisms underlying the genotypic and phenotypic relationship of HPP remain unclear.
HIGHLIGHT
The expression of HPP-related TNSALP mutants in mammalian cells allows us to determine for the effects of mutations on the properties of TNSALP, which could contribute to a better understanding of the relationship between structure and function of TNSALP.
CONCLUSION
Molecular characterization of TNSALP mutants helps establish the etiology and onset of HPP.

Identifiants

pubmed: 31400546
pii: S1349-0079(19)30075-1
doi: 10.1016/j.job.2019.07.003
pii:
doi:

Substances chimiques

Alkaline Phosphatase EC 3.1.3.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

141-148

Informations de copyright

Copyright © 2019 Japanese Association for Oral Biology. Published by Elsevier B.V. All rights reserved.

Auteurs

Keiichi Komaru (K)

Kitasato Junior College of Health and Hygienic Science, 500 Kurotsuchi-Shinden, Minami-Uonoma, Niigata 949-7241, Japan. Electronic address: komaru.k@kitasato-u.ac.jp.

Yoko Ishida-Okumura (Y)

Niigata University Graduate School of Medical and Dental Sciences 2-5274, Gakkocho-dori, Chuo-ku, Niigata 951-8514, Japan. Electronic address: yishida@dent.niigata-u.ac.jp.

Natsuko Numa-Kinjoh (N)

Kinjoh Children's Dental Clinic, 5-17-45, Ikarashinakajima, Nishi-ku, Niigata 950-2162, Japan. Electronic address: kirin.shika@sj9.so-net.ne.jp.

Tomoka Hasegawa (T)

Department of Developmental Biology of Hard Tissue, Graduate School of Dental Medicine, Hokkaido University, Kita 13, Nishi 7, Kita-ku, Sapporo, 060-8586 Japan. Electronic address: hasegawa@den.hokudai.ac.jp.

Kimimitsu Oda (K)

Showa Hospital, 911-1 Tokunaga Omachi, Nishi-ku, Fukuoka 819-0375, Japan. Electronic address: hypooda@yahoo.co.jp.

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Classifications MeSH