1H-NMR and raman studies on perforating trauma-induced cataract formation in a mouse lens.

In order to provide new insight into the molecular mechanism of perforating trauma-induced cataract formation in an 8-week-old ddY mouse lens, we performed an in situ investigation into changes in the water-protein and/or protein-protein interactions by using 500 MHz (1)H-NMR spectroscopy, and into structural alterations in lens proteins by using Raman spectroscopy. Cross-relaxation times of water protons in the perforated opaque lens were considerably shorter than those in the intact transparent lens, whereas there was no significant difference in water content, suggesting a drastic change in water-protein and protein-protein interactions in the perforated lens. In addition, there was no significant difference in the intensity ratios of several key Raman bands between intact and perforated lenses, indicating that no significant local and overall conformational changes in lens protein itself occur in the perforated lens. The present (1)H-NMR and Raman results lead us to the conclusion that changes leading to lens opacification in the perforating trauma-induced cataract appear to involve the rapid formation of immobile large lens protein aggregates without formation of intra- and intermolecular disulfide linkages, and rapid increase in a fraction of bound water associated with large protein aggregates.