Adipogenic function of mouse tetranectin and identification of its functional domain.

Tetranectin (TN), a plasminogen (Plg) binding protein, enhances the Plg activator (PA)-catalyzed activation of Plg to plasmin (Pln). Previously, TN was identified as an adipogenic serum protein, which promotes adipocyte differentiation. In the present study, we investigated the adipogenic function of mouse TN using recombinant proteins (rmTNs) in full-length and domain-truncated forms. Adipocyte differentiation in TN-depleted-FBS-media was significantly enhanced by rmTNs supplementation. The adipogenic effect of rmTNs was found to be dependent on the presence of a Plg binding domain, indicating the domain is essential for the adipogenic function of mTN. In addition, these results suggested the involvement of Plg activation, however Plg, PA and Pln appeared to have no direct effect on adipocyte differentiation. This study demonstrates the adipogenic function of mTN, which is dependent on the Plg binding domain as its functional domain.