免费精品视频一区二区三区学生,被3个黑人老外玩的4p,人妻精品无码中文无码一区无,添女人荫蒂全部过

首頁> 外文期刊>Biochimica et biophysica acta. Molecular basis of disease: BBA >Abnormal glycosylation with hypersialylated O-glycans in patients with Sialuria
【24h】

Abnormal glycosylation with hypersialylated O-glycans in patients with Sialuria

機譯：唾液尿癥患者高唾液酸化O-聚糖糖基化異常

獲取原文
獲取原文并翻譯 | 示例
  • 摘要
  • 著錄項
  • 相似文獻
  • 相關主題

摘要

Sialuria is an inborn error of metabolism characterized by coarse face, hepatomegaly and recurrent respiratory tract infections. The genetic defect in this disorder results in a loss of feedback control of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine-kinase by CMP-N-acetylneuraminic acid (CMP-NeuAc) resulting in a substantial overproduction of cytoplasmic free sialic acid. This study addresses fibroblast CMP-NeuAc levels and N- and O-glycan sialylation of serum proteins from Sialuria patients. CMP-NeuAc levels were measured with HPLC in fibroblasts. Isoelectric focusing (IEF) of serum transferrin and of apolipoprotein C-III (apoC-III) was performed on serum of three Sialuria patients. Isoforms of these proteins can be used as specific markers for the biosynthesis of N- and core 1 O-glycans. Furthermore, total N- and O-linked glycans from serum proteins were analyzed by HPLC. HPLC showed a clear overproduction of CMP-NeuAc in fibroblasts of a Sialuria patient. Minor changes were found for serum N-glycans and hypersialylation was found for core 1 O-glycans on serum apo C-III and on total serum O-glycans in Sialuria patients. HPLC showed an increased ratio of disialylated over monosialylated core 1 O-glycans. The hypersialylation of core 1 O-glycans is due to the increase of NeuAc alpha 2,6-containing structures (mainly NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc). This may relate to Km differences between GalNAc-alpha 2,6-sialyltransferase and alpha 2,3-sialyltransferases. This is the first study demonstrating that the genetic defect in Sialuria results in a CMP-NeuAc overproduction. Subsequently, increased amounts of alpha 2,6-linked NeuAc were found on serum core I O-glycans from Sialuria patients. N-glycosylation of serum proteins seems largely unaffected. Sialuria is the first metabolic disorder presenting with hypersialylated O-glycans. (c) 2006 Elsevier B.V. All rights reserved.
機譯：唾液尿癥是先天性代謝錯誤，特征是面部粗糙，肝腫大和反復出現呼吸道感染。該疾病的遺傳缺陷導致CMP-N-乙酰神經氨酸（CMP-NeuAc）對UDP-N-乙酰氨基葡萄糖2-表異構酶/ N-乙酰甘露糖胺激酶的反饋控制喪失，導致細胞質游離唾液酸大量過量生產。這項研究解決了唾液尿癥患者的成纖維細胞CMP-NeuAc水平以及血清蛋白的N-和O-聚糖唾液酸化作用。用HPLC測量成纖維細胞中的CMP-NeuAc水平。對三名唾液尿癥患者的血清進行了血清轉鐵蛋白和載脂蛋白C-III（apoC-III）的等電聚焦（IEF）。這些蛋白質的同工型可用作N和核心1 O-聚糖生物合成的特異性標記。此外，通過HPLC分析了來自血清蛋白的總的N-和O-連接的聚糖。 HPLC顯示，唾液尿癥患者的成纖維細胞中CMP-NeuAc明顯過量生產。在唾液尿癥患者中，血清N-聚糖的變化很小，而血清apo C-III和總血清O-聚糖的核心1 O-聚糖的唾液酸化過度。 HPLC顯示二唾液酸化的比單唾液酸化的核心1 O-聚糖的比率增加。核心1 O-聚糖的過度唾液酸化是由于含有NeuAc alpha 2,6-的結構（主要是NeuAc alpha 2-3Gal beta 1-3 [NeuAc alpha 2-6] GalNAc）增加所致。這可能與GalNAc-α2，6-唾液酸轉移酶和α2，3-唾液酸轉移酶之間的Km差異有關。這是第一項證明唾液酸的遺傳缺陷導致CMP-NeuAc過量生產的研究。隨后，在來自唾液尿癥患者的血清核心I O-聚糖上發現了數量增加的α2,6-連接的NeuAc。血清蛋白的N-糖基化作用似乎基本不受影響。唾液尿癥是首個出現高唾液酸化O聚糖的代謝性疾病。 （c）2006 Elsevier B.V.保留所有權利。

著錄項

相似文獻

  • 外文文獻
  • 中文文獻
  • 專利
獲取原文

客服郵箱：kefu@zhangqiaokeyan.com

京公網安備：11010802029741號 ICP備案號：京ICP備15016152號-6 六維聯合信息科技 (北京) 有限公司?版權所有

  • 客服微信

  • 服務號

主站蜘蛛池模板： 武平县| 漾濞| 诸城市| 惠州市| 铜梁县| 千阳县| 汉寿县| 元朗区| 宣汉县| 扎鲁特旗| 宣化县| 瑞金市| 锡林郭勒盟| 太白县| 白银市| 淄博市| 荔浦县| 开鲁县| 松江区| 衡阳市| 宁乡县| 贵定县| 刚察县| 正蓝旗| 广平县| 晋城| 明水县| 饶河县| 微博| 云林县| 两当县| 东城区| 盐边县| 客服| 枣阳市| 巩义市| 临江市| 交城县| 鲜城| 乐都县| 海安县|