Mammalian hyaluronan synthases: investigation of functional relationships in vivo.
Mammalian hyaluronan synthases: investigation of functional relationships in vivo.
复制标题
哺乳动物透明质酸合酶：体内功能关系的研究。
DOI：
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发表时间：
1999
影响因子：
3.9
通讯作者：
T. Nguyen
中科院分区：
文献类型：
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作者：
A. Spicer;T. Nguyen
前言透明质酸(HA)的生物合成发生在质膜的内面[1，2]，而其他糖胺聚糖的生物合成是在高尔基体网络中合成的。已在脊椎动物中鉴定出三个HA合成酶(ID1S)基因[3-81。每个基因编码一个预测的具有多个跨膜区的质膜糖基转移酶。哺乳动物的蛋白质有55%到71%的氨基酸同源性，由位于不同常染色体上的不同基因编码[9]。任何一个IFAs基因的表达都足以驱动哺乳动物细胞中HA的生物合成([S]；N.Itano，M.Yosida，P.Lenas，Y.Yamada，A.P.Spicer，J.A.McDonald和K.Kimata，未发表的工作)。我们之前已经证明了ID1S基因在胚胎发育期间和成人组织中的差异表达[S]。因此，自从这个小基因家族通过基因复制产生以来，负责调节各自EUROUS基因转录的启动子和增强子序列已经有了很大的分歧。然而，目前还不清楚这三种HAS蛋白的酶功能是否也发生了分化。最近通过细胞培养研究获得的数据表明，尽管任何一个人拥有足够的蛋白质来合成HA，
Introduction Hyaluronan (HA) biosynthesis occurs at the inner face of the plasma membrane [1,2], in contrast to the biosynthesis of other glycosaminoglycans, which are synthesized within the Golgi network. Three HA synthase (ID1S) genes have been identified in vertebrates [3-81. Each gene encodes a predicted plasma membrane glycosyltransferase with multiple transmembrane domains. The mammalian HAS proteins share between 55 and 71% amino acid identity, and are encoded by distinct genes located on separate autosomes [9]. Expression of any one IfAS gene is sufficient to drive the biosynthesis of HA in mammalian cells ([S]; N. Itano, M. Yosida, P. Lenas, Y. Yamada, A. P. Spicer, J. A. McDonald and K. Kimata, unpublished work). We have previously demonstrated the differential expression of ID1S genes during embryonic development and in adult tissues [S]. Thus, promoter and enhancer sequences responsible for regulating the transcription of the respective €US genes have diverged substantially since this small gene family arose through gene duplication. However, it remains unclear as to whether or not the enzymic functions of the three HAS proteins have also diverged. Recent data obtained through cell culture studies suggest that although any one HAS protein is sufficient for HA biosynthesis,