A synchrotron x-ray diffraction study of developing chick corneas.

To study some ultrastructural aspects of developing chick corneas we performed a synchrotron x-ray diffraction analysis of 22 specimens obtained daily from developmental day 10 through day 19. Before day 12 of development in chicks we were unable to detect a meridional x-ray diffraction pattern from cornea. Neither were we able to record a first-order equatorial x-ray reflection at this time. Normally, these reflections are present in corneal x-ray patterns, arising from, respectively, the periodic axial electron density of fibrillar collagen and the lattice-like arrangement of the fibrils. By day 12 of development we could detect the third- and fifth-order meridional reflections (indicating increased amounts of collagen) and a first-order equatorial reflection (implying that more collagen was regularly arranged). The third- and fifth-order meridional reflections became more intense as the tissue matured, suggestive of a continued deposition of fibrillar collagen, and the scattering angle of the interfibrillar maximum increased, suggesting that regularly arranged collagen was becoming more closely packed with maturation. In embryonic chick corneas, the establishment of an orderly, fairly compacted matrix of collagen fibrils may be one of the main events underlying the acquisition of corneal transparency

Proteoglycans contain a 4.6 A repeat in muscular dystrophy corneas: x-ray diffraction evidence.

Synchrotron x-ray diffraction patterns from macular corneal dystrophy (MCD) corneas contain an unusual reflection that arises because of an undefined ultrastructure with a periodic repeat in the region of 4.6 A. In this study, we compared with wide-angle x-ray diffraction patterns obtained from four normal human corneas and four MCD corneas. Moreover, portions of two of the MCD corneas were pretreated with a specific glycosidase to shed light on the origin of the 4.6 A reflection. None of the normal corneas produced an x-ray reflection in the region of 4.6 A, whereas all four of the MCD corneas did (MCD type I at 4.65 A and 4.63 A, MCD type II at 4.63 A and 4.67 A). This reflection was diminished after incubation of the MCD tissues with either chondroitinase ABC or N-glycanase. The findings indicate that glycosaminoglycans or proteoglycans contribute to the unusual MCD x-ray reflection and hence most likely contain a periodic 4.6 A ultrastructure. Furthermore, the results imply that periodic 4.6 A MCD ultrastructures reside in either intact, unsulfated lumican molecules and regions of the CS/DS-containing molecules or in a region of a hybrid macromolecular aggregate formed by the interaction of the two molecules