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Title
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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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Authors
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T.H.Lee,
H.G.Wisniewski,
J.Vilcek.
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Ref.
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J Cell Biol, 1992,
116,
545-557.
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PubMed id
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Abstract
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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.
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