Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ
Molecular cloning and mRNA tissue distribution of a novel matrix metalloproteinase isolated from porcine enamel organ
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DOI：
10.1016/s0378-1119(96)00525-2
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发表时间：
1996-12-12
期刊：
影响因子：
3.5
通讯作者：
Moreno, EC
中科院分区：
文献类型：
--
作者：
Bartlett, JD;Simmer, JP;Moreno, EC
从猪牙釉质器官特异的cDNA文库中克隆了一个新的基质金属蛋白酶(MMPs)编码基因。多个组织的Northern印迹分析表明，存在两个只在成釉器官中表达的mRNA转录本。转录本全长1968个或3420个碱基，并利用了不同的多聚腺苷酸化位点。该基因的开放阅读框编码483个氨基酸组成的蛋白质。基质金属蛋白酶的预测分子质量为54.1 kDa，与基质蛋白或胶原酶相似，尽管它不是这两类基质金属蛋白酶的成员。基序分析表明，克隆的基质金属蛋白酶不包含一致的类血凝蛋白结构域，因为它在适当的位置缺少关键的色氨酸和脯氨酸残基。由于克隆的基质金属蛋白酶是基质金属蛋白酶基因家族的新成员，其表达似乎仅限于成釉器官，因此我们将其命名为釉质溶素。
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.