TUMOR-CELL AUTOCRINE MOTILITY FACTOR
TUMOR-CELL AUTOCRINE MOTILITY FACTOR
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DOI：
10.1073/pnas.83.10.3302
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发表时间：
1986-05-01
影响因子：
11.1
通讯作者：
SCHIFFMANN, E
中科院分区：
文献类型：
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作者：
LIOTTA, LA;MANDLER, R;SCHIFFMANN, E
从人A2058黑色素瘤细胞的无血清条件培养基中分离、纯化并部分表征了细胞运动刺激因子。我们称这种活性为“自分泌运动因子”（AMF）。AMF具有蛋白质的性质，估计大小为55 kDa。在10 nM或更低的浓度下，AMF刺激生产细胞的随机或定向运动。然而，AMF不是中性粒细胞的引诱剂。氨基酸分析表明，纯化的AMF蛋白的丝氨酸，甘氨酸，谷氨酸和天冬氨酸残基的含量高。AMF的活性不被已知的生长因子如表皮生长因子或β型替代或阻断。转化生长因子机制研究表明，AMF刺激的[3 H]甲基掺入细胞膜磷脂孵育后，与[甲基-3H]蛋氨酸与持续增加的磷脂酰乙醇胺的甲基化磷脂酰胆碱。相反，AMF不影响[1，2- 14 C]胆碱掺入磷脂酰胆碱。AMF大量产生的ras癌基因转染的转移性NIH 3 T3细胞的三个不同的克隆，但不是由非转化的亲本细胞。AMF可能在肿瘤细胞的局部侵袭行为中起主要作用，也可能促进肿瘤细胞群的协同侵袭。
A cell motility-stimulating factor has been isolated, purified, and partially characterized from the serum-free conditioned medium of human A2058 melanoma cells. We term this activity "autocrine motility factor" (AMF). AMF has the properties of a protein with an estimated size of 55 kDa. At concentrations of 10 nM or less, AMF stimulated the random or directed motility of the producer cells. However, AMF is not an attractant for neutrophils. Amino acid analysis of the purified AMF protein revealed a high content of serine, glycine, glutamic acid, and aspartic acid residues. The activity of AMF was not replaced or blocked by known growth factors such as epidermal growth factor or type .beta. transforming growth factor. Mechanistic studies showed that AMF stimulated the incorporation of [3H]methyl into cell membrane phospholipids after incubation with [methyl-3H]methionine with a sustained increase in the methylation of phosphatidylethanolamine to phosphatidylcholine. In contrast, AMF did not affect the incorporation of [1, 2-14C]choline into phosphatidylcholine. AMF was produced in large amounts by three different clones of ras-oncogene-transfected metastatic NIH 3T3 cells but not by the nontransformed parental cells. AMF may play a major role in the local invasive behavior of tumor cells and may also facilitate the concerted invasion by groups of tumor cells.