Delmotte P, Degroote S, Merten M D, Van Seuningen I, Bernigaud A, Figarella C, Roussel P, Périni J M
Unité INSERM n degrees 377, place de Verdun, F-59045 Lille, France.
Glycoconj J. 2001 Jun;18(6):487-97. doi: 10.1023/a:1016038219183.
In order to investigate the influence of inflammation on the peripheral glycosylation of airway mucins, a human respiratory glandular cell line (MM-39) was treated by TNFalpha. The expression and the activity of sialyl- and fucosyl-transferases, involved in the biosynthesis of peripheral carbohydrate determinants like sialyl-Lewis x, were investigated by RT-PCR and by HPAEC respectively. The mRNA steady-state level of sialyl- (ST3Gal III) and of fucosyl- (FUT3) transferases was moderately up-regulated by TNFalpha; a 52% increase of alpha2,3-sialyltransferase activity was also observed in TNFalpha-stimulated MM-39 cells. After metabolic radio-labelling with [(3)H]glucosamine and [(3)H]fucose, the mucins released in the culture supernatant were purified by Sepharose CL-4B, density-gradient centrifugation and treatment with glycosaminoglycans-degrading enzymes. The mucins, released in the culture supernatant from control MM-39 cells, were constituted by two populations of molecules having the same 1.39-1.44 mg/ml density but carrying either high or low amounts of sialic acid residues at their periphery. TNFalpha was able to increase the sialylation of the weakly sialylated mucins. This effect and the enhancement of the alpha2,3-sialyltransferase activity by TNFalpha argue in favour of a regulation of the mucin sialylation by this pro-inflammatory cytokine. Despite the moderate overexpression of FUT3, no fucosylation of mucins produced by MM-39 cells was induced by TNFalpha. In conclusion, the influence of TNFalpha on the sialylation of mucins could explain why the mucins from infected patients suffering either from cystic fibrosis or from chronic bronchitis are more sialylated.
为了研究炎症对气道粘蛋白外周糖基化的影响,用人呼吸道腺癌细胞系(MM - 39)进行肿瘤坏死因子α(TNFα)处理。分别通过逆转录聚合酶链反应(RT - PCR)和高效阴离子交换色谱(HPAEC)研究参与外周碳水化合物决定簇(如唾液酸化路易斯x)生物合成的唾液酸转移酶和岩藻糖基转移酶的表达及活性。TNFα使唾液酸转移酶(ST3Gal III)和岩藻糖基转移酶(FUT3)的mRNA稳态水平适度上调;在TNFα刺激的MM - 39细胞中还观察到α2,3 - 唾液酸转移酶活性增加52%。用[³H]葡萄糖胺和[³H]岩藻糖进行代谢放射性标记后,通过琼脂糖凝胶CL - 4B、密度梯度离心和用糖胺聚糖降解酶处理,纯化培养上清液中释放的粘蛋白。对照MM - 39细胞培养上清液中释放的粘蛋白由两个分子群体组成,它们具有相同的1.39 - 1.44 mg/ml密度,但外周携带的唾液酸残基量不同,分别为高或低。TNFα能够增加弱唾液酸化粘蛋白的唾液酸化程度。这种作用以及TNFα对α2,3 - 唾液酸转移酶活性的增强表明这种促炎细胞因子对粘蛋白唾液酸化有调节作用。尽管FUT3有适度的过表达,但TNFα并未诱导MM - 39细胞产生的粘蛋白发生岩藻糖基化。总之,TNFα对粘蛋白唾液酸化的影响可以解释为什么患有囊性纤维化或慢性支气管炎的感染患者的粘蛋白唾液酸化程度更高。