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发育中的猪牙釉质中釉原蛋白的区室化

Enamelin compartmentalization in developing porcine enamel.

作者信息

Brookes S J, Lyngstadaas S P, Robinson C, Shore R C, Wood S R, Kirkham J

机构信息

Division of Oral Biology, Leeds Dental Institute, Leeds LS2 9LU, UK.

出版信息

Connect Tissue Res. 2002;43(2-3):477-81. doi: 10.1080/03008200290000862.

DOI:10.1080/03008200290000862
PMID:12489201
Abstract

The tissue compartmentalization of enamelin-processing products has been investigated in developing pig enamel using a sequential extraction procedure. Only trace amounts of enamelin-processing products were detected in simulated enamel fluid extracts, suggesting that enamelins are not solubilized in the matrix to any great extent. Subsequent phosphate buffer extraction desorbed and extracted several enamelin-processing products that were presumably bound to the mineral phase. A 35-kD processing product dominated the phosphate extract, suggesting that enamelin processing leads to an accumulation of this mineral-bound molecule. Dissociative extraction with urea subsequently extracted the remainder of the enamelin-processing products present. This material was presumably present in the tissue in an aggregated insoluble state. Several enamelin-processing products were only extracted by specific extraction procedures, suggesting that different enamelin-processing products are differentially compartmentalized. This may indicate that specific enamelin-processing products have different functions. In contrast to amelogenins, which are processed in the deeper tissue to generate products having a low affinity for the mineral, enamelin processing appears to produce products (those enamelins desorbed by phosphate buffer) that have a high affinity for the mineral. These products, appearing in the deeper enamel layers, may serve to influence crystal growth kinetics in the absence of any mineral-binding amelogenins.

摘要

利用连续提取程序,对发育中的猪牙釉质中釉原蛋白加工产物的组织区室化进行了研究。在模拟釉质液提取物中仅检测到痕量的釉原蛋白加工产物,这表明釉原蛋白在很大程度上不会溶解在基质中。随后用磷酸盐缓冲液提取,解吸并提取了几种可能与矿相结合的釉原蛋白加工产物。一种35kD的加工产物在磷酸盐提取物中占主导地位,这表明釉原蛋白加工导致了这种与矿质结合的分子的积累。随后用尿素进行解离提取,提取出了剩余的釉原蛋白加工产物。这些物质可能以聚集的不溶性状态存在于组织中。几种釉原蛋白加工产物仅通过特定的提取程序才能提取出来,这表明不同的釉原蛋白加工产物在组织中是分区存在的。这可能表明特定的釉原蛋白加工产物具有不同的功能。与在较深层组织中加工以产生对矿物质亲和力较低的产物的釉原蛋白不同,釉原蛋白加工似乎产生了对矿物质具有高亲和力的产物(那些被磷酸盐缓冲液解吸的釉原蛋白)。这些出现在较深釉质层中的产物,可能在没有任何与矿物质结合的釉原蛋白的情况下,影响晶体生长动力学。

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Enamelin compartmentalization in developing porcine enamel.发育中的猪牙釉质中釉原蛋白的区室化
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Physiol Rev. 2017 Jul 1;97(3):939-993. doi: 10.1152/physrev.00030.2016.
2
Amelogenesis imperfecta caused by N-terminal enamelin point mutations in mice and men is driven by endoplasmic reticulum stress.在小鼠和人类中,由釉原蛋白N端点突变引起的牙釉质发育不全是由内质网应激驱动的。
Hum Mol Genet. 2017 May 15;26(10):1863-1876. doi: 10.1093/hmg/ddx090.
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Enamel defects reflect perinatal exposure to bisphenol A.牙釉质缺陷反映了围产期双酚 A 的暴露。
Am J Pathol. 2013 Jul;183(1):108-18. doi: 10.1016/j.ajpath.2013.04.004. Epub 2013 Jun 10.
4
Is the 32-kDa fragment the functional enamelin unit in all species?32千道尔顿片段在所有物种中都是功能性釉原蛋白单位吗?
Eur J Oral Sci. 2011 Dec;119 Suppl 1(S1):345-50. doi: 10.1111/j.1600-0722.2011.00869.x.
5
A mutation in the mouse Amelx tri-tyrosyl domain results in impaired secretion of amelogenin and phenocopies human X-linked amelogenesis imperfecta.鼠 amelx 三酪氨酰结构域中的突变导致釉原蛋白分泌受损,并模拟了人类 X 连锁型釉质不全。
Hum Mol Genet. 2010 Apr 1;19(7):1230-47. doi: 10.1093/hmg/ddq001. Epub 2010 Jan 12.
6
Evolutionary analysis of mammalian enamelin, the largest enamel protein, supports a crucial role for the 32-kDa peptide and reveals selective adaptation in rodents and primates.哺乳动物釉原蛋白(最大的釉质蛋白)的进化分析支持 32kDa 肽的关键作用,并揭示了啮齿动物和灵长类动物的选择性适应。
J Mol Evol. 2009 Dec;69(6):635-56. doi: 10.1007/s00239-009-9302-x.