The microscopic protein structure of the lens with a theory for cataract formation as determined by Raman spectroscopy of intact bovine lenses.
Intact bovine lenses have been studied using the polarized Raman spectroscopic technique. A brief theoretical and experimental review of Raman spectroscopy is presented. From the dependence of the Raman depolarization ratio on the propagation direction of the incident radiation we have determined that the uniaxial qualities of the lens result from microscopic anisotropy and have established the quantitative positional correlation of specific chemical bonds with respect to the lens optic axis. In particular, the hydrogen bonded linear CONH groups of the antiparallel beta-pleated sheet are preferentially oriented in directions orthogonal to the lens optic axis. The Raman spectra of intact lenses do not exhibit bands at positions characteristic of either the alpha-helix or the random coil protein structure. The antiparallel beta-pleated sheet protein microstructure and the lens fiber cross-sectional macrostructure exhibit a remarkable similarity. This similarity may be causal and is consistent with the protein concentration of the lens, the birefringent properties observed by both Lenhard and Brewster, the CONH bond angle distribution with respect to the optic axis, and the lens anatomy. It is suggested that cortical cataracts are caused by fluctuations in protein orientational order.
D000818:Animals; D001128:Argon; D001718:Birefringence; D002386:Cataract / Q000209:etiology*; D002417:Cattle; D003459:Crystallins; D066298:In Vitro Techniques; D007834:Lasers; D007908:Lens, Crystalline / Q000648:ultrastructure*; D008163:Luminescent Measurements; D010455:Peptides; D012542:Scattering, Radiation; D013057:Spectrum Analysis / Q000379:methods
D003459:Crystallins; D010455:Peptides; D001128:Argon