A ROLE FOR A 70-KILODATON HEAT-SHOCK PROTEIN IN LYSOSOMAL DEGRADATION OF INTRACELLULAR PROTEINS
A ROLE FOR A 70-KILODATON HEAT-SHOCK PROTEIN IN LYSOSOMAL DEGRADATION OF INTRACELLULAR PROTEINS
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DOI：
10.1126/science.2799391
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发表时间：
1989-10-20
期刊：
影响因子：
56.9
通讯作者：
DICE, JF
中科院分区：
文献类型：
--
作者：
CHIANG, HL;TERLECKY, SR;DICE, JF
发现一种73千道尔顿（kD）的细胞内蛋白质结合到靶向细胞内蛋白质的肽区域，以响应血清戒断而进行溶酶体降解。该蛋白质与针对70-kD热休克蛋白（hsp 70）家族成员的单克隆抗体交叉反应，并且73-kD蛋白质的两个内部肽的序列证实它是该家族的成员。在血清撤出，细胞内浓度的73-kD蛋白增加了几倍。在腺苷5“-三磷酸（TP）和MgCl 2的存在下，73 kD蛋白在两种不同的溶酶体蛋白水解无细胞测定中增强蛋白质降解。
A 73-kilodalton (kD) intracellular protein was found to bind to peptide regions that target intracellular proteins for lysosomal degradation in response to serum withdrawal. This protein cross-reacted with a monoclonal antibody raised to a member of the 70-kD heat shock protein (hsp70) family, and sequences of two internal peptides of the 73-kD protein confirm that it is a member of this family. In response to serum withdrawal, the intracellular concentration of the 73-kD protein increased severalfold. In the presence of adenosine 5''-triphosphate (TP) and MgCl2, the 73-kD protein enhanced protein degradation in two different cell-free assays for lysosomal proteolysis.