Human extravillous trophoblasts express laeverin, a novel protein that belongs to membrane-bound gluzincin metallopeptidases
Human extravillous trophoblasts express laeverin, a novel protein that belongs to membrane-bound gluzincin metallopeptidases
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DOI：
10.1016/j.bbrc.2003.12.024
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发表时间：
2004-01-23
影响因子：
3.1
通讯作者：
Fujii, S
中科院分区：
文献类型：
--
作者：
Fujiwara, H;Higuchi, T;Fujii, S
人类绒毛外滋养层细胞(EVT)侵入母体蜕膜。为了确定与EVT侵袭有关的分子，我们提出了一种与人EVT反应的鼠单抗(CHL2)。从胎盘组织中纯化的CHL2抗原的相对分子质量为160 kDa。虽然N端部分氨基酸序列和1个内部序列尚未报道，但其他3个内部序列与从估计序列标签的编码区推导出的序列(1672bp，AK075131)相匹配。根据这一信息，用5‘RACE方法确定了CHL2抗原编码的全长(2970bp)，这是在其他地方未见报道的。这种新的蛋白质命名为laeverin，具有一个包含锌结合活性部位的多肽酶M1基序。在N端附近也有一个跨膜结构域。它的氨基酸序列与氨基肽酶N同源，这些数据表明人EVTS表达Leeverin，这是一种属于谷氨酸锌金属肽酶的新蛋白。(C)2003 Elsevier Inc.保留所有权利。
Human extravillous trophoblasts (EVTs) invade the maternal decidua. To identify the molecules involved in EVT invasion, we raised a murine monoclonal antibody (CHL2) that reacts with human EVTs. The molecular mass of CHL2 antigen purified from placental tissues was 160 kDa. Although the N-terminal partial amino acid sequence and one internal sequence are still unreported, the other three internal sequences matched those deduced from the coding region of the estimated sequence tag (1672 bp, AK075131). Based on this information, the full-length of the coding cDNA sequence of CHL2 antigen (2970 bp), which has not been reported elsewhere, was determined by 5' RACE. This novel protein, named laeverin, has a peptidase M1 motif containing a zinc-binding active site. It also has a transmembrane domain near the N-terminus. Its amino acid sequence is homologous with aminopeptidase N. These data indicate that human EVTs express laeverin, a novel protein belonging to gluzincin metallopepticlases. (C) 2003 Elsevier Inc. All rights reserved.