Differential expression and enzymatic properties of GalNAc-4-sulfotransferase-1 and GalNAc-4-sulfotransferase-2.

Differential expression and enzymatic properties of GalNAc-4-sulfotransferase-1 and GalNAc-4-sulfotransferase-2.
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GalNAc-4-sulfotransferase-1 和 GalNAc-4-sulfotransferase-2 的差异表达和酶特性。

DOI:
10.1093/glycob/cwj024
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发表时间:
2005
期刊:
影响因子:
4.3
通讯作者:
Baenziger,JacquesU
Baenziger,JacquesU
中科院分区:
生物学3区
文献类型:
--
作者:
Boregowda,RajeevK;Mi,YiLing;Bu,Hongyin;Baenziger,JacquesU

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我们克隆了两种 GalNAc-4-磺基转移酶 GalNAc-4-ST1 和 GalNAc-4-ST2,它们将硫酸盐转移到末端 β1,4 连接的 GalNAc。结合蛋白质特异性 β1,4GalNAc 转移酶的作用,GalNAc-4-ST1 和 GalNAc-4-ST2 解释了糖蛋白(如促黄体素、促甲状腺素 (TSH)、阿片黑皮素原 (POMC)、碳酸酐酶-VI (CA-VI) 和腱生蛋白-R)上末端 β1,4 连接的 GalNAc-4-SO4 的存在。 GalNAc-4-ST1 和 GalNAc-4-ST2 可以通过它们对寡糖受体的不同特异性和温度不稳定性来区分。性质的差异已用于表明 GalNAc-4-ST1 和 GalNAc-4-ST2 活性的水平与其各自转录物的水平成比例。此外,我们发现GalNAc-4-ST1和GalNAc-4-ST2的转录物和活性水平在不同组织中差异很大,表明它们的表达调控存在差异。特异性和表达调节的差异可能是体内存在两种 GalNAc-4-磺基转移酶的原因。 GalNAc-4-ST1 和 GalNAc-4-ST2 转录物的最高水平存在于具有多种细胞类型的小鼠垂体中,这些细胞类型产生以 GalNAc-4-SO4 结尾的糖蛋白。 GalNAc-4-ST1 和 GalNAc-4-ST2 的基因消融可能是改变组织(如垂体)中硫酸盐添加到末端 β1,4GalNAc 的模式和/或程度所必需的。
We have cloned two GalNAc-4-sulfotransferases, GalNAc-4-ST1 and GalNAc-4-ST2, that transfer sulfate to terminal β1,4-linked GalNAc. In conjunction with the action of protein-specific β1,4GalNAc-transferases, GalNAc-4-ST1 and GalNAc-4-ST2 account for the presence of terminal β1,4-linked GalNAc-4-SO4on glycoproteins such as lutropin, thyrotropin (TSH), proopiomelanocortin (POMC), carbonic anhydratase-VI (CA-VI), and tenascin-R. GalNAc-4-ST1 and GalNAc-4-ST2 can be distinguished by their differing specificity for oligosaccharide acceptors and temperature lability. The differences in properties have been used to show that the levels of GalNAc-4-ST1 and GalNAc-4-ST2 activity are proportionate to the levels of their respective transcripts. Furthermore, we have found that both transcript and activity levels of GalNAc-4-ST1 and GalNAc-4-ST2 vary widely among different tissues indicating that the regulation of their expression differs. Differences in specificity and the regulation of expression may account for existence of two GalNAc-4-sulfotransferasesin vivo. The highest levels of both GalNAc-4-ST1 and GalNAc-4-ST2 transcripts are present in the pituitary of the mouse with multiple cell types that produce glycoproteins terminating with GalNAc-4-SO4. Genetic ablation of both GalNAc-4-ST1 and GalNAc-4-ST2 may be necessary to alter the pattern and/or extent of sulfate addition to terminal β1,4GalNAc in tissues such as pituitary.
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