Adhesion of
calcium oxalate (CaOx) crystals to kidney cells is a key event in
kidney stones associated with marked
hyperoxaluria. As the propensity of stone recurrence and persistent side effects are not altered by surgical techniques available, phytotherapeutic agents could be useful as an adjuvant
therapy. The present study is aimed at examining the antilithiatic potency of the
protein biomolecules of Tribulus terrestris, a plant which is a common constituent of herbal marketed preparations to treat
urolithiasis. Various biochemical methods with mass spectrometry were used to purify and characterize the purified
protein. The protective potency of the
protein was tested on the
oxalate induced injury on renal epithelial cell lines (NRK 52E). An antilithiatic
protein having molecular weight of ~ 60kDa was purified. This purified
protein showed similarities with
Carotenoid cleavage
dioxygenase 7 (CCD7) of Arabidopsis thaliana after matching
peptide mass fingerprints in MASCOT search engine. An EF hand domain was identified in CCD7 by SCAN PROSITE. Presence of an EF hand domain, a characteristic feature of
calcium binding proteins and a role in the synthesis of
retinol which is transported by
retinol binding protein, a
protein found in
kidney stone matrix; of CCD7 support the role of
TTP as an antilithiatic
protein. The protective potency of
TTP on NRK 52E was quite comparable to the aqueous extract of
cystone. Our findings suggest that this purified
protein biomolecule from Tribulus terrestris could open new vista in medical management of
urolithiasis.