Degradation of Enamel Matrix Proteins in Porcine Secretory Enamel
Degradation of Enamel Matrix Proteins in Porcine Secretory Enamel
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DOI：
10.3109/03008209809023918
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发表时间：
1998-01-01
影响因子：
2.9
通讯作者：
Tanabe, T.
中科院分区：
文献类型：
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作者：
Fukae, M.;Tanabe, T.
为了阐明在釉质表面附近的狭窄空间中发生的25 kDa釉原蛋白的逐渐消失，从新形成的猪釉质中提取含有80%总蛋白的碱溶性部分。当这种牵引孵育与钙离子在体外系统中，共存的釉原蛋白和釉蛋白的降解发生在孵育期间没有激活。虽然该组分主要含有两种金属蛋白酶，56 kDa和61 kDa的明胶分解活性，和41 kDa和46 kDa的酪蛋白分解活性，它被证明在釉原蛋白酶谱，酪蛋白分解的一个与25 kDa的釉原蛋白转化为20 kDa的釉原蛋白。新形成釉质的蛋白质分布表明，金属蛋白酶对共存的釉蛋白和釉原蛋白的降解不完全。尽管如此，在下一个发展阶段，他们展示了他们的全部活动。据推测，这些活动是由钙离子，这可能是增加了级联系统的调节。
To elucidate the progressive disappearance of 25 kDa amelogenin occurring in a narrow space near the surface of enamel, the alkaline soluble fraction which contained 80% of the total proteins was extracted from a newly formed porcine enamel. When this traction was incubated with the addition of Ca ions in an in vitro system, the degradation of the coexisting amelogenin and enamelin occurred without activation during the incubation period. Although the fraction contained mainly two kinds of metalloproteinases, 56 kDa and 61 kDa gelatinolytic, and 41 kDa and 46 kDa caseinolytic activities, it was demonstrated on amelogenin enzymography that the caseinolytic one was concerned with the conversion of the 25 kDa amelogenin into the 20 kDa amelogenin. The protein distribution of the newly formed enamel indicated that the metalloproteinases degraded the coexisting enamelin and amelogenin imperfectly. Nevertheless, during the next developing stage they demonstrated their full activities. It is suspected that these activities are regulated by Ca ions, which may be increased by a cascade system.