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首页> 外文期刊>Journal of Leukocyte Biology: An Official Publication of the Reticuloendothelial Society >The significance of carbohydrates on G-CSF: differential sensitivity of G-CSFs to human neutrophil elastase degradation.
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The significance of carbohydrates on G-CSF: differential sensitivity of G-CSFs to human neutrophil elastase degradation.

机译：碳水化合物对G-CSF的重要性：G-CSF对人嗜中性粒细胞弹性蛋白酶降解的敏感性不同。

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摘要

It has been reported recently that granulocyte-colony stimulating factor (G-CSF) is degraded upon exposure to human neutrophil elastase (HNE), and this has a negative effect on the ability of the cytokine to promote the in vitro proliferation and maturation of CD34+ cells. This has important implications on the possible in vivo role of elastase in providing negative feedback to granulopoiesis by the direct antagonism of G-CSF. The cytokine used in that study was expressed in Escherichia coli [and was nonglycosylated (NG)], unlike the naturally occurring cytokine, which is an O-linked glycoprotein. As a Chinese hamster ovary-derived (glycosylated) cytokine is available, we compared the susceptibility of NG and glycosylated G-CSF to elastase degradation by incubating the cytokines with HNE and assessing its impact by sodium dodecyl sulfate gel electrophoresis and bioassay. We confirmed the ability of elastase to degrade NG G-CSF in a time- and concentration-dependent manner and found this was associated with a reduction in biological activity of the cytokine. Glycosylated G-CSF, however, was more resistant to elastase degradation, although prolonged exposure did lead to degradation and decreased biological activity. The significance of sugar residues on glycosylated G-CSF in providing protection against the effects of elastase was investigated using enzymatically deglycosylated G-CSF and a mutated form of the G-CSF molecule that was expressed in yeast but was NG. The possible role of HNE in serum-induced inactivation of NG G-CSF was also considered.
机译：最近有报道说，粒细胞集落刺激因子（G-CSF）暴露于人中性粒细胞弹性蛋白酶（HNE）后会降解，这对细胞因子促进体外CD34 +增殖和成熟的能力产生负面影响。细胞。这对弹性蛋白酶可能在体内通过G-CSF的直接拮抗作用向粒细胞生成提供负反馈具有重要的意义。在这项研究中使用的细胞因子在大肠杆菌中表达[并且是非糖基化的（NG）]，这与天然存在的细胞因子是O型连接的糖蛋白不同。由于有中国仓鼠卵巢衍生的（糖基化的）细胞因子，我们通过将细胞因子与HNE孵育并通过十二烷基硫酸钠硫酸钠凝胶电泳和生物分析评估其对NG和糖基化G-CSF对弹性蛋白酶降解的敏感性。我们证实了弹性蛋白酶以时间和浓度依赖性方式降解NG G-CSF的能力，发现这与细胞因子的生物学活性降低有关。糖基化的G-CSF对弹性蛋白酶降解的抵抗力更大，尽管长时间接触确实会导致降解和生物活性降低。使用酶促去糖基化的G-CSF和在酵母中表达但为NG的G-CSF分子的突变形式，研究了糖基化G-CSF上糖残基在提供针对弹性蛋白酶作用的保护中的重要性。还考虑了HNE在血清诱导的NG G-CSF失活中的可能作用。

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