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首页> 外文期刊>Biochemistry >Effects of glycosylation on the structure and function of the extracellular chaperone clusterin.
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Effects of glycosylation on the structure and function of the extracellular chaperone clusterin.

机译：糖基化对细胞外分子伴侣簇蛋白的结构和功能的影响。

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摘要

Clusterin is the first well characterized, constitutively secreted extracellular chaperone that binds to exposed regions of hydrophobicity on non-native proteins. It may help control the folding state of extracellular proteins by targeting them for receptor-mediated endocytosis and intracellular lysosomal degradation. A notable feature of secreted clusterin is its heavy glycosylation. Although carbohydrate comprises approximately 20-25% of the total mass of the mature molecule, its function is unknown. Results from the current study demonstrate that deglycosylation of human serum clusterin had little effect on its overall secondary structure content but produced a small increase in solvent-exposed hydrophobicity and enhanced the propensity of the molecule to aggregate in solution. These changes were associated with increased binding to a variety of ligands but did not substantially impact the ability of clusterin to inhibit heat-induced precipitation of citrate synthase. Evidence suggesting that the normally conjugated sugars are important in the interaction of secreted clusterin with a lectin-type receptor on liver cells is also presented. Bulk expression of fully processed, glycosylated clusterin in mammalian cells is difficult, often producing inappropriately disulfide-bonded high molecular weight aggregates; this has hampered previous studies aimed at identifying those regions of the molecule important in its chaperone action. The current results suggest that it may be possible in the future to study the structure and chaperone function of clusterin using recombinant protein (lacking sugars) conveniently bulk-expressed in bacteria.
机译：簇蛋白是第一个特征明确的，组成型分泌的细胞外伴侣，它与非天然蛋白上的疏水性暴露区域结合。通过靶向受体介导的内吞作用和细胞内溶酶体降解，可以帮助控制细胞外蛋白的折叠状态。分泌的簇蛋白的显着特征是其重糖基化。尽管碳水化合物约占成熟分子总质量的20-25％，但其功能尚不清楚。当前研究的结果表明，人血清簇蛋白的去糖基化对其整体二级结构含量影响不大，但溶剂暴露的疏水性增加很小，并增强了分子在溶液中聚集的倾向。这些变化与与各种配体的结合增加有关，但基本上不影响簇蛋白抑制热诱导的柠檬酸合酶沉淀的能力。有证据表明，正常结合的糖在分泌的簇蛋白与肝细胞上的凝集素型受体的相互作用中很重要。很难在哺乳动物细胞中大量表达完全加工的糖基化簇蛋白，通常会产生不适当的二硫键结合的高分子量聚集体。这阻碍了先前旨在鉴定对分子伴侣起重要作用的分子区域的研究。目前的结果表明，将来有可能使用方便地在细菌中大量表达的重组蛋白（缺乏糖）来研究簇蛋白的结构和分子伴侣功能。

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