Tumor Necrosis Factor Alpha Induced Protein 6 (TNFaIP6)

TSG6; TNF-Stimulated Gene 6; Hyaluronate-binding protein; Tumor necrosis factor alpha-induced protein 6

SPN	L992
HGNC	11898
MGI	1195266
PubMed	12972412
UniProt	P98066
Wiki	TNFAIP6

TSG-6 is a 30 kDa secreted protein that contains a hyaluronan-binding LINK domain a and thus is a member of the hyaluronan-binding protein family, also called hyaladherins. The hyaluronan-binding domain is known to be involved in extracellular matrix stability and cell migration. This protein has been shown to form a stable, covalent complex with inter-alpha-inhibitor (IαI), and thus enhance the serine protease inhibitory activity of IαI, which is important in the protease network associated with inflammation. The expression of this gene can be induced by a number of signalling molecules, principally tumor necrosis factor α (TNF-α) and interleukin-1 (IL-1). The expression can also be induced by mechanical stimuli in vascular smooth muscle cells, and is found to be correlated with proteoglycan synthesis and aggregation.

Reference

"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."
J. Cell Biol. 116:545-557(1992) [PubMed] [Europe PMC] [Abstract]

"A novel allelic variant of the human TSG-6 gene encoding an amino acid difference in the CUB module. Chromosomal localization, frequency analysis, modeling, and expression."
J. Biol. Chem. 277:15354-15362(2002) [PubMed] [Europe PMC] [Abstract]

"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"TSG-6, an arthritis-associated hyaluronan binding protein, forms a stable complex with the serum protein inter-alpha-inhibitor."
Biochemistry 33:7423-7429(1994) [PubMed] [Europe PMC] [Abstract]

"Solution structure of the link module: a hyaluronan-binding domain involved in extracellular matrix stability and cell migration."
Cell 86:767-775(1996) [PubMed] [Europe PMC] [Abstract]