Decreased inhibitory activity of prothrombin to calcium oxalate crystallization by specific chemical modification of its gamma-carboxyglutamic acid residues

Urology. 2006 Jan;67(1):201-3. doi: 10.1016/j.urology.2005.07.058.

Abstract

Objectives: To investigate the inhibitory role of gamma (gamma)-carboxyglutamic acid (Gla) in the Gla domain of urinary prothrombin in the formation of calcium oxalate crystals.

Methods: Morpholine and formaldehyde at different concentrations were added to the solution of prothrombin to cause the conversion of Gla to gamma-methyleneglutamic acid (MGlu). The extent of the modification was controlled by the relative amount of modification reagents to prothrombin. The 100-fold molar excess of modification reagents to prothrombin produced the prothrombin molecule containing 2gamma-MGlu residues, and the 10,000-fold molar excess produced the molecule containing 8gamma-MGlu residues. The inhibitory activities of prothrombin and modified prothrombin to calcium oxalate crystallization were evaluated by the seeded crystallization technique.

Results: The inhibitory index of Gla prothrombin to calcium oxalate crystallization was 14.2%, that of 2gamma-MGlu prothrombin was 12.8%, decreased by about 10%, and that of 8gamma-MGlu prothrombin was 5.0%, decreased by about 65%.

Conclusions: The Gla in the Gla domain of urinary prothrombin may play an important role in inhibiting the formation of renal calcium oxalate calculus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-Carboxyglutamic Acid / chemistry*
  • 1-Carboxyglutamic Acid / drug effects*
  • Calcium Oxalate / chemistry*
  • Crystallization
  • Prothrombin / pharmacology*

Substances

  • Calcium Oxalate
  • 1-Carboxyglutamic Acid
  • Prothrombin