Description of two classes of proteinases from enamel extracellular matrix cleaving a recombinant amelogenin.
Description of two classes of proteinases from enamel extracellular matrix cleaving a recombinant amelogenin.
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DOI：
10.3109/03008209609029196
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发表时间：
1996
影响因子：
2.9
通讯作者：
Janet Moradian-oldak;P. Sarte;A. Fincham
中科院分区：
文献类型：
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作者：
Janet Moradian-oldak;P. Sarte;A. Fincham
本文以重组小鼠釉原蛋白M179为底物，对其体外蛋白降解的研究进展进行了简要的综述。本研究的具体目的是鉴定、分离和鉴定釉质细胞外基质中的蛋白水解酶。我们鉴定了两类釉质蛋白：1)高分子量蛋白酶(60-68 kDa)裂解M179的c-末端，是一种钙依赖的金属蛋白酶，最适pH为8.2)；低分子量蛋白酶(约30 kDa)去除TRAP(富酪氨酸蛋白釉原多肽)序列，导致M179进一步降解。后者是一种丝氨酸蛋白酶，在pH值为6时活性最高。这些数据支持釉原蛋白是通过特定的和高度受控的机制切割的，它们可能在釉质成熟过程中发挥直接作用。
This paper is a short review of our recent studies on amelogenin proteolysis in vitro using a recombinant mouse amelogenin M179 as a substrate. The specific aims of this study were to identify, isolate and characterize the proteinases in the enamel extracellular matrix. We identified two classes of enamel proteinases; 1) the high molecular weight proteinase (60-68 kDa) cleaves the c-terminal segment of M179 and is a calcium dependent metalloproteinase with an optimum pH of 8.2) The low molecular weight proteinase (approximately 30 kDa) removes the TRAP (Tyrosine Rich Amelogenin Polypeptide) sequence and causes further degradation of M179. The latter was identified to be a serine proteinase with an optimal activity at pH 6. These data support the notion that enamel proteinases cleave amelogenin through specific and highly controlled mechanisms and that they may fulfill direct roles during enamel maturation.