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doi: 10.1242/10.1242/jcs.00407

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TSG-6: a multifunctional protein associated with inflammation

Caroline M. Milner and Anthony J. Day*

MRC Immunochemistry Unit, Department of Biochemistry, South Parks Road, Oxford OX1 3QU, UK



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  		Fig. 1. TSG-6 expression. TSG-6 is expressed in the context of inflammatory diseases and inflammation-like processes and has also been detected during development (see references in text and Table 1).

 


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  		Fig. 2. TSG-6 properties and functions. TSG-6 binds specifically to GAGs, including HA, C4S and heparin and to the proteoglycan aggrecan. It also interacts, both covalently and non-covalently, with I{alpha}I: covalent complexes may be involved in crosslinking HA chains, whereas non-covalent interactions potentiate the anti-plasmin activity of I{alpha}I. TSG-6 has been implicated in cell proliferation, the inhibition of neutrophil migration and the regulation of CD44. The mechanisms of these activities remain to be elucidated.

 


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  		Fig. 3. Structure of human TSG-6. A representation of the modular structure of the mature TSG-6 protein is shown with amino acid positions indicated on the basis of the preprotein sequence (Lee et al., 1992Go): contiguous Link and CUB (Complement subcomponents C1r/C1s, Uegf, BMP-1) modules are flanked by a 19 amino-acid N-terminal sequence and a 27 amino-acid C-terminal sequence. The refined solution structure of the Link module (C. D. Blundell, I. D. Campbell and A.J.D., unpublished; PDB accession code 1o7b) and a model of the Gln144 allotype of the CUB domain (Nentwich et al., 2002Go) are depicted below. The five amino acids identified as being involved in HA binding (Mahoney et al., 2001Go) are highlighted in purple on the Link module and the polymorphic residue (position 144) (Nentwich et al., 2002Go) is marked on the CUB module. The point of connection between the Link and CUB modules is indicated by a dashed line (their relative orientations remain to be determined) and the locations of the N- and C-terminal sequences, which are of unknown structure, are indicated.

 

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© The Company of Biologists Ltd 2003