Structure of the human palmitoyl-protein thioesterase-2 gene (PPT2) in the major histocompatibility complex on chromosome 6p21.3.
Structure of the human palmitoyl-protein thioesterase-2 gene (PPT2) in the major histocompatibility complex on chromosome 6p21.3.
复制标题
染色体 6p21.3 上主要组织相容性复合体中人棕榈酰蛋白硫酯酶 2 基因 (PPT2) 的结构。
DOI：
10.1006/geno.1998.5703
复制
发表时间：
1999
期刊：
影响因子：
--
通讯作者：
Hofmann,SL
中科院分区：
文献类型：
--
作者：
Soyombo,AA;Yi,W;Hofmann,SL
棕榈酰蛋白硫酯酶-2（PPT 2）是PPT 1的同源物，PPT 1是溶酶体贮积症婴儿神经元蜡样脂褐质沉积症（NCL）中缺乏的酶。作为确定编码PPT 2（PPT 2）的基因突变是否与任何分子上未表征的NCL形式相关的第一步，我们在这里报告了humanPPT 2的结构和染色体定位。PPT 2全长约10 kb，由9个外显子组成。一个主要（2.0kb）及两个次要该基因转录出7.0和2.8kb的mRNA，较大的转录产物为信使RNA，其中PPT 2外显子被剪接到编码人潜伏性转化生长因子β结合蛋白同源物的下游基因中（人LTBP）. PPT 2位于染色体6p21.3上的人主要组织相容性III类基因座，在任何确定的染色体位点上的NCL中排除PPT 2作为致病基因的位置。在对12例PPT活性正常的疑似诊断为婴儿NCL的受试者进行初步分析时，SSCP分析未检测到突变。然而，在无关的正常个体中发现了5个单核苷酸多态性。这些多态性（以及在PPT 2中发现的微卫星）将有助于进一步阐明PPT 2在病因不明的溶酶体贮积症中的可能作用。
Palmitoyl-protein thioesterase-2 (PPT2) is a homolog of PPT1, the enzyme that is deficient in the lysosomal storage disorder, infantile neuronal ceroid lipofuscinosis (NCL). As a first step toward determining whether mutations in the gene encoding PPT2 (PPT2) are associated with any of the molecularly uncharacterized forms of NCL, we report here the structure and chromosomal localization of humanPPT2. PPT2spans about 10 kb and is composed of nine exons. One major (2.0 kb) and two minor (7.0 and 2.8 kb) mRNAs are transcribed from the gene, and the larger transcripts appear to be messenger RNAs in whichPPT2exons are spliced into a downstream gene encoding a homolog of human latent transforming growth factor-β binding protein (human LTBP).PPT2is located in the human major histocompatibility class III locus on chromosome 6p21.3, a position that rules outPPT2as the causative gene in any of the NCLs at defined chromosomal loci. No mutations were detected by SSCP analysis in a preliminary analysis of 12 subjects referred with a suspected diagnosis of infantile NCL who had normal PPT activity. However, five single nucleotide polymorphisms were found in unrelated normal individuals. These polymorphisms (and a microsatellite discovered withinPPT2) will aid in the further delineation of the possible role ofPPT2in lysosomal storage disorders of unknown etiology.