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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?

Is the 32-kDa fragment the functional enamelin unit in all species?

作者信息

Brookes Steven J, Kingswell Nicola J, Barron Martin J, Dixon Michael J, Kirkham Jennifer

机构信息

Department of Oral Biology, Leeds Dental Institute, University of Leeds, Leeds, UK.

出版信息

Eur J Oral Sci. 2011 Dec;119 Suppl 1(S1):345-50. doi: 10.1111/j.1600-0722.2011.00869.x.

DOI:10.1111/j.1600-0722.2011.00869.x
PMID:22243266
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3427898/
Abstract

Enamelin is an extracellular enamel matrix protein essential for normal amelogenesis. After secretion, porcine enamelin is processed to generate several enamelin-degradation products. The cumulative 32-kDa enamelin is the most abundant enamelin present, and various roles for this molecule have been suggested. However, the proteolytic cleavage sites in porcine enamelin that generate the 32-kDa enamelin are not conserved across species, and the 32-kDa enamelin analogue may not be present in all species. To explore this we studied rat enamelin biochemistry using western blotting with anti-peptide IgGs to porcine 32-kDa enamelin and to the putative rat 32-kDa enamelin analogue. The dominant enamelins in secretory-stage rat enamel migrated at around 60-70 kDa. In contrast, the dominant enamelins in secretory-stage porcine enamel migrated at around 32 kDa. In contrast, secretory-stage porcine-enamel enamelins were dominated by the 32-kDa enamelin. Rat enamelin was completely removed from maturation-stage enamel without any accumulation of 32-kDa enamelin. We suggest that a discrete 32-kDa enamelin is not essential for normal amelogenesis in all species, and in pig it may be a processing product of a larger functional enamelin molecule. The pig may be an atypical model in terms of enamelin biochemistry and function, and caution should be exercised when assigning functional roles to the 32-kDa enamelin as a discrete enamel matrix entity.

摘要

釉蛋白是正常釉质形成所必需的一种细胞外釉质基质蛋白。分泌后,猪釉蛋白会被加工产生几种釉蛋白降解产物。累积的32 kDa釉蛋白是含量最丰富的釉蛋白,人们已提出该分子具有多种作用。然而,猪釉蛋白中产生32 kDa釉蛋白的蛋白水解切割位点在不同物种间并不保守,而且并非所有物种都存在32 kDa釉蛋白类似物。为了探究这一点,我们使用针对猪32 kDa釉蛋白和假定的大鼠32 kDa釉蛋白类似物的抗肽IgG进行蛋白质印迹法,研究了大鼠釉蛋白的生物化学性质。分泌期大鼠釉质中的主要釉蛋白迁移至约60 - 70 kDa处。相比之下,分泌期猪釉质中的主要釉蛋白迁移至约32 kDa处。相反,分泌期猪釉质中的釉蛋白以32 kDa釉蛋白为主。大鼠釉蛋白在成熟阶段的釉质中完全消失,没有32 kDa釉蛋白的任何积累。我们认为,一个离散的32 kDa釉蛋白并非所有物种正常釉质形成所必需的,在猪中它可能是一个更大的功能性釉蛋白分子的加工产物。就釉蛋白的生物化学性质和功能而言,猪可能是一个非典型模型,在将32 kDa釉蛋白作为一个离散的釉质基质实体赋予功能作用时应谨慎行事。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0d1/3427898/5054793041a9/eos0119-0345-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0d1/3427898/a064d0cba5de/eos0119-0345-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0d1/3427898/121d7daac888/eos0119-0345-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0d1/3427898/5054793041a9/eos0119-0345-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0d1/3427898/a064d0cba5de/eos0119-0345-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0d1/3427898/121d7daac888/eos0119-0345-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0d1/3427898/5054793041a9/eos0119-0345-f3.jpg

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