A novel secretory tumor necrosis factor-inducible protein (TSG-6) is a member of the family of hyaluronate binding proteins, closely related to the adhesion receptor CD44.
A novel secretory tumor necrosis factor-inducible protein (TSG-6) is a member of the family of hyaluronate binding proteins, closely related to the adhesion receptor CD44.
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一种新型的分泌性肿瘤坏死因子诱导蛋白（TSG-6）是透明质酸元素结合蛋白家族的成员，与粘附受体CD44密切相关。
DOI：
10.1083/jcb.116.2.545
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发表时间：
1992-01
影响因子：
7.8
通讯作者：
Vilcek, J
中科院分区：
文献类型：
--
作者：
Lee, T H;Wisniewski, H G;Vilcek, J
TSG-6 cDNA通过从肿瘤坏死因子（TNF）处理的人二倍体FS-4成纤维细胞制备的λ cDNA文库的差异筛选来分离。我们发现，TSG-6 mRNA在未经处理的细胞中检测不到，但在正常人成纤维细胞系和外周血单核细胞中很容易被TNF诱导。与此相反，TSG-6 mRNA在对照或TNF处理的人血管内皮细胞和各种肿瘤衍生或病毒转化的细胞系中检测不到。TSG-6全长cDNA序列显示一个主要的开放阅读框架，预测277个氨基酸的多肽，包括一个典型的可切割的信号肽。预测的TSG-6蛋白序列的NH 2-末端一半显示出与透明质酸结合相关的区域的显著同源性，该区域存在于软骨连接蛋白、蛋白聚糖核心蛋白和粘附受体CD 44中。预测的TSG-6蛋白和CD 44之间存在最广泛的序列同源性。Western印迹分析与TSG-6融合蛋白的抗血清检测到39 kD的糖蛋白在TNF-处理的FS-4细胞和转染TSG-6 cDNA的细胞的上清液中。通过共沉淀证明TSG-6蛋白与透明质酸盐的结合。我们的数据表明，炎症细胞因子（TNF或IL-1）诱导的分泌TSG-6蛋白是透明质酸结合蛋白家族的新成员，可能参与炎症和肿瘤发生过程中的细胞-细胞和细胞-基质相互作用。
TSG-6 cDNA was isolated by differential screening of a lambda cDNA library prepared from tumor necrosis factor (TNF)-treated human diploid FS-4 fibroblasts. We show that TSG-6 mRNA was not detectable in untreated cells, but became readily induced by TNF in normal human fibroblast lines and in peripheral blood mononuclear cells. In contrast, TSG-6 mRNA was undetectable in either control or TNF-treated human vascular endothelial cells and a variety of tumor-derived or virus-transformed cell lines. The sequence of full-length TSG-6 cDNA revealed one major open reading frame predicting a polypeptide of 277 amino acids, including a typical cleavable signal peptide. The NH2- terminal half of the predicted TSG-6 protein sequence shows a significant homology with a region implicated in hyaluronate binding, present in cartilage link protein, proteoglycan core proteins, and the adhesion receptor CD44. The most extensive sequence homology exists between the predicted TSG-6 protein and CD44. Western blot analysis with an antiserum raised against a TSG-6 fusion protein detected a 39- kD glycoprotein in the supernatants of TNF-treated FS-4 cells and of cells transfected with TSG-6 cDNA. Binding of the TSG-6 protein to hyaluronate was demonstrated by coprecipitation. Our data indicate that the inflammatory cytokine (TNF or IL-1)-inducible, secretory TSG-6 protein is a novel member of the family of hyaluronate binding proteins, possibly involved in cell-cell and cell-matrix interactions during inflammation and tumorigenesis.