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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GlLT)
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Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GlLT)

机译：酶促溶酶体中二硫键的还原：γ-干扰素诱导的溶酶体硫醇还原酶（GlLT）的表征。

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摘要

Proteins internalized into the endocytic pathway are usually de- graded. Efficient proteolysis requires denaturation, induced by acidic conditions within lysosomes, and reduction of inter- and intrachain disulfide bonds. Cytosolic reduction is mediated enzy- matically by thioredoxin, but the mechanism of lysosomal reduc- tion is unknown. We describe here a lysosomal thiol reductase optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitrO. The active site, determined by mutagenesis, consists of a pair of cysteine residues separated by tWo amino acids, similar to other enzymes of the thioredoxin family. The enzyme is a soluble glycoprotein that is synthesized as a precursor. After delivery into the endosomal/lysosomal system by the mannose 6-phosphate receptor, N- and C-terminal prose- quences are removed. The enzyme is expressed constitutively in antigen-presenting cells and induced by IFN-y in other cell types, suggesting a potentially important role in antigen processing.
机译：内吞进入内吞途径的蛋白质通常会降解。高效的蛋白水解需要变性（由溶酶体内部的酸性条件诱导），以及还原链间和链内二硫键。硫氧还蛋白通过酶介导细胞溶质的还原，但溶酶体还原的机理尚不清楚。我们在这里描述了一种溶酶体硫醇还原酶，在低pH值下具有最佳活性，并且能够在体内和vitrO中催化二硫键的还原。通过诱变确定的活性位点由一对被两个氨基酸隔开的半胱氨酸残基组成，类似于硫氧还蛋白家族的其他酶。该酶是合成为前体的可溶性糖蛋白。由甘露糖6-磷酸受体递送到内体/溶酶体系统后，N和C末端的现象被去除。该酶在抗原呈递细胞中组成性表达，并在其他细胞类型中被IFN-γ诱导，表明在抗原加工中可能具有重要作用。

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