Scientists identify novel kidney stone inhibitors

  • Vanita Srivastava, Hindustan Times, New Delhi
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  • Updated: Feb 03, 2013 23:19 IST

Indian researchers have identified three novel proteins in human kidney stones that could inhibit the formation of these very stones in kidneys and urinary tract. These proteins are also capable of protecting kidney epithelial cells from stone-induced injury.

The research highlight in Nature India, an online publication by the Nature Publishing Group, may yield new therapies to alleviate urolithiasis, the formation of stones in the urinary tract. Such stone-induced diseases affect people globally, including residents from the north-western states of India. Proteins in the stones inhibit or promote stone formation, and studies have thrown light on the roles of negatively charged proteins in such stones. However, no studies have investigated the functions of positively charged proteins in stone formation.

Sophisticated spectroscopic analyses identified positively charged proteins that inhibit stone formation. The researchers detected three new proteins - histone-lysine N-methyltransferase, inward rectifier K channel and protein Wnt-2, the research highlight said.

The authors of this work are from department of biotechnology and bioinformatics, Jaypee University of Information Technology, Waknaghat, Solan, Himachal Pradesh and Department of Urology, Post Graduate Institute of Medical Education & Research, Chandigarh.

"We identified histone-lysine N-methyltransferase, inward rectifier K channel and protein Wnt-2 as novel antilithiatic proteins which play a vital role in the kidney function and have been associated with various kidney diseases," the researchers said.

These proteins were purified and their effects on calcium oxalate stone formation and stone-induced injury to dog kidney epithelial cells were studied. Purified proteins showed significant inhibition of calcium oxalate crystal nucleation and growth and showed protective effects toward the cell injury caused by oxalate.


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