Regulation of lipoprotein lipase synthesis in 3T3-L1 adipocytes by cachectin. Further proof for identity with tumour necrosis factor.
Regulation of lipoprotein lipase synthesis in 3T3-L1 adipocytes by cachectin. Further proof for identity with tumour necrosis factor.
复制标题
恶病素调节 3T3-L1 脂肪细胞中脂蛋白脂肪酶的合成。
DOI：
10.1042/bj2400601
复制
发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Pekala,PH
中科院分区：
文献类型：
--
作者：
Price,SR;Olivecrona,T;Pekala,PH
我们研究了内毒素诱导的巨噬细胞分泌蛋白cachectin抑制3T3-L1脂肪细胞脂蛋白脂肪酶活性的机制。由于[35S]蛋氨酸与免疫可沉淀的脂蛋白脂肪酶结合减少，酶的合成受到影响，导致酶活性丧失。结果几乎相同，无论是粗条件培养基或高度纯化的制剂作为cachectin的来源。[35S]纯化的cachectin对蛋氨酸并入可酸沉淀蛋白的影响最小，这表明脂蛋白脂肪酶的抑制不是由于蛋白质合成的普遍抑制。这些结果，结合我们之前的工作，提供了额外的证据，证明cachectin和tumor necrosis factor在功能上是相同的。
We investigated the mechanism by which the endotoxin-induced macrophage secretory protein cachectin is able to suppress the activity of lipoprotein lipase in 3T3-L1 adipocytes. The loss in activity results from an effect on the synthesis of the enzyme, as determined by a decreased incorporation of [35S]methionine into immunoprecipitable lipoprotein lipase. The results were nearly identical whether crude conditioned medium or a highly purified preparation was utilized as a source of cachectin. [35S]Methionine incorporation into acid-precipitable protein was minimally affected by purified cachectin, suggesting that the suppression of the lipoprotein lipase was not due to a general suppression of protein synthesis. These results, taken together with our previous work, provide additional evidence that cachectin and tumour necrosis factor are functionally identical.