Bartlett J D, Simmer J P, Xue J, Margolis H C, Moreno E C
Department of Biomineralization, Forsyth Dental Center, Boston, MA 02115, USA.
Gene. 1996 Dec 12;183(1-2):123-8. doi: 10.1016/s0378-1119(96)00525-2.
A cDNA encoding a novel matrix metalloproteinase (MMP) was isolated from a porcine enamel organ-specific cDNA library. Multiple tissue northern blot analysis revealed the presence of two mRNA transcripts which were expressed only in the enamel organ. The transcripts were 1968 bp or 3420 bp in length and resulted from the utilization of alternative polyadenylation sites. The open reading frame of the cloned mRNA encodes a protein composed of 483 amino acids. The MMP has a predicted molecular mass of 54.1 kDa, which is similar to that of the stromelysins or collagenases, although it is not a member of either of these two classes of MMPs. A motif analysis revealed that the cloned MMP does not contain a consensus hemopexin-like domain because it lacks a critical tryptophan and proline residue at the appropriate positions. Since the cloned MMP is a new member of the MMP gene family and its expression appears limited to the enamel organ, we have named it enamelysin.
从猪牙釉质器官特异性cDNA文库中分离出一种编码新型基质金属蛋白酶（MMP）的cDNA。多组织Northern印迹分析显示存在两种仅在牙釉质器官中表达的mRNA转录本。这些转录本长度分别为1968 bp或3420 bp，是由于使用了可变聚腺苷酸化位点所致。克隆的mRNA的开放阅读框编码一种由483个氨基酸组成的蛋白质。该MMP预测分子量为54.1 kDa，与基质溶素或胶原酶相似，尽管它不属于这两类MMP中的任何一类。基序分析表明，克隆的MMP不包含共有血色素结合蛋白样结构域，因为它在适当位置缺少关键的色氨酸和脯氨酸残基。由于克隆的MMP是MMP基因家族的新成员，且其表达似乎仅限于牙釉质器官，我们将其命名为釉质溶解素。
