Molecular cloning and expression of the pituitary glycoprotein hormone <i>N</i>-acetylgalactosamine-4-<i>O</i>-sulfotransferase

作     者：Xia, GQ Evers, MR Kang, HG Schachner, M Baenziger, JU 

作者机构：Washington Univ Sch Med Dept Pathol St Louis MO 63110 USA Univ Hamburg Zentrum Mol Neurobiol D-20246 Hamburg Germany 

出 版 物：《JOURNAL OF BIOLOGICAL CHEMISTRY》 (生物化学杂志)

年 卷 期：2000年第275卷第49期

页      面：38402-38409页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学] 

基　　金：NIDDK NIH HHS [R01DK41738] Funding Source: Medline 

主　　题：氨基酸序列 碱基序列 CHO细胞 碳水化合物序列 染色体图 染色体 人 19对 克隆 分子 仓鼠亚科 促黄体激素/代谢 分子序列数据 寡糖类/化学 垂体激素类 前叶/化学 垂体激素类 前叶/代谢 前阿片黑素细胞皮质激素/代谢 重组蛋白质类/代谢 序列比对 序列同源性 氨基酸 磺基转移酶类/遗传学 磺基转移酶类/代谢 促甲状腺素/代谢 转染 动物 人类 大鼠 

摘      要：N-Linked oligosaccharides terminating with the sequence SO4-4-GalNAc beta1,4GlcNAc beta1,2Man alpha are present on the pituitary hormones lutropin (LH), thyrotropin, and pro-opiomelanocortin. The sulfated structures on LII are essential for expression of its biologic function in vivo. We have cloned the N-acetglgalactosamine-4-sulfo-transferase (GalNac-4-ST1, GenBank(TM) accession number AF300612), which mediates sulfate addition to the N-linked oligosaccharides on LH and other pituitary glycoproteins with terminal (beta1,4-linked GalNAc based on its homology to HNK-1 sulfotransferase (HNK-1 ST). GalNAc-4-ST1 displays 23% identity to HNK-1 ST and 28% to chondroitin 4-sulfotransferase I (C4ST-1) and 26% to chondroitin 4-sulfotransferase 2 (C4ST-2), The cDNA predicts a type II transmembrane protein of 424 amino acids with four potential N-linked glycosylation sites and a single membrane-spanning domain. GalNAc-4-ST1 has putative 5 -phosphosulfonate and S -phosphate binding sites, Three more carboxyl-terminal regions of unknown function also show a high degree of identity with HNK-1 ST, C4ST-1, and C4ST-2. The membrane-bound form of GalNAc-4-ST1 transfers sulfate to GalNAc beta1,4GlcNAc beta -R but not to chondroitin, whereas truncated forms of GalNAc-4-ST1 that are released into the medium transfer sulfate to both GalNAc beta1, 4GlcNAc beta -R and chondroitin, The first 118 amino acids of GalNAc-4-ST1 appear to contribute to both its activity and specificity for terminal beta1,4-linked GalNAc. GalNAc-4-ST1 also efficiently transfers sulfate to N-linked oligosaccharides on native LH and other glycoproteins terminating with beta1,4-linked GalNAc. A single transcript of 2.4 kilobases is most highly expressed in the pituitary and other regions of the central nervous system. The GalNAc-4-ST1 gene is located on human chromosome 19q13.1.