成釉蛋白丝氨酸残基磷酸化在釉质形成过程中的意义

The importance of serine phosphorylation of ameloblastin on enamel formation
2016-12-30 18:29发表评论
作者:Ma, P., Yan, W., Tian, Y., He, J., Brookes, S.J., Wang, X.
机构: 首都医科大学,北京口腔医院口腔种植科
期刊: J DENT RES2016年11月12期95卷

FAM20C is a newly identified kinase on the secretory pathway responsible for the phosphorylation of serine residues in the Ser-x-Glu/pSer motifs in several enamel matrix proteins. Fam20C-knockout mice showed severe enamel defects very similar to those in the ameloblastin (Ambn)-knockout mice, implying that phosphoserines may have a critical role in AMBN function. To test this hypothesis, we generated amelogenin (Amel) promoter-driven Ambn-transgenic mice, in which Ser48, Ser226, and Ser227 were replaced by aspartic acid (designated as D-Tg) or alanines (designated as A-Tg). The negative charge of aspartic acid is believed to be able to mimic the phosphorylation state of serine, while alanine is a commonly used residue to substitute serine due to their similar structure. Using Western immunoblotting and quantitative polymerase chain reaction, the authors identified transgenic lines expressing transgenes somewhat higher (Tg+) or much higher (Tg++) than endogenous Ambn. The lower incisors collected from 7-d-old and 7-wk-old mice were analyzed by histology, scanning electron microscopy, immunohistochemistry, and Western immunoblotting to examine the morphology and microstructure changes in enamel, as well as the expression pattern of enamel matrix proteins. The A-Tg+ and A-Tg++ mice displayed severe enamel defects in spite of the expression level of transgenes, while the D-Tg+ and D-Tg++ mice showed minor to mild enamel defects, indicating that the D-Tg transgenes disturbed enamel formation less than the A-Tg transgenes did. Our results suggest that the phosphorylation state of serines is likely an essential component for the integrity of AMBN function. © International & American Associations for Dental Research.

通讯机构:Department of Oral Implantology, Beijing Stomatological Hospital, Capital Medical University, Beijing, China
学科代码:口腔医学   关键词:成釉蛋白丝氨酸残基磷酸化 ,中国作者重要发表 爱思唯尔医学网, Elseviermed
来源: Scopus
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