Identity of human extra parotid glycoprotein (EP-GP) with secretory actin binding protein (SABP) and its biological properties.

In this paper the identity of the salivary protein EP-GP (extra-parotid glycoprotein) is reported, also apparent in other human secretions. Immunochemical and biochemical analysis demonstrated that EP-GP is similar to the secretory actin-binding protein (SABP), also known as gross cystic disease fluid protein-15 (GCDFP-15) and prolactin-inducible protein (PIP). The molecular mass and charge microheterogeneity of EP-GP, also observed for SABP, was shown to be predominantly caused by the carbohydrate moiety. In addition, evidence was given that EP-GP is not related to the lipocalin Von Ebner's gland protein (human; VEGh). The biological significance of EP-GP and its homologues is not clear. EP-GP bound to actin and fibrinogen as described for SABP and GCDFP-15. However, the affinity for these proteins does not appear to have any direct physiological role in the mucosal secretions. On the other hand, EP-GP binds to several bacteria. By electron microscopy the ultrastructural localization is demonstrated of EP-GP to the cell wall of both Streptococcus salivarius HB and its cell appendage-lacking mutant Streptococcus salivarius HB-C12. Concerning this finding we hypothesize on the possible functional aspects of this enigmatic protein EP-GP.