TY - JOUR

T1 - SCHEIES-SYNDROME

T2 - THE ARCHITECTURE OF CORNEAL COLLAGEN AND DISTRIBUTION OF CORNEAL PROTEOGLYCANS

AU - QUANTOCK, A J

AU - MEEK, K M

AU - FULLWOOD, N J

AU - ZABEL, R W

PY - 1993/10

Y1 - 1993/10

N2 - Processes that modulate the regular architecture and, hence, transparency of the cornea are poorly understood, although proteoglycans are thought to be involved. Scheie's syndrome displays corneal opacification and systemic accumulation of glycosaminoglycans. The manifestations of these two occurrences were examined in relation to the corneal stroma. Collagen architecture was investigated by transmission electron microscopy and synchrotron x-ray diffraction. Cuprolinic blue staining located sulfated glycosaminoglycan deposits that disrupted the extracellular matrix. Unlike normal cornea, which contained collagen fibrils of remarkably uniform diameter (26.0 +/- 2.4 nm), there was a large range of fibril sizes in the Scheie's syndrome stroma (19.9 to 52.0 nm). Moreover, the distribution of fibril diameters appeared bimodal. X-ray diffraction confirmed the discovery of abnormally large stromal collagen. The results suggest a link in Scheie's syndrome between proteoglycan content/distribution and stromal disruption, and between stromal disruption and corneal opacification.

AB - Processes that modulate the regular architecture and, hence, transparency of the cornea are poorly understood, although proteoglycans are thought to be involved. Scheie's syndrome displays corneal opacification and systemic accumulation of glycosaminoglycans. The manifestations of these two occurrences were examined in relation to the corneal stroma. Collagen architecture was investigated by transmission electron microscopy and synchrotron x-ray diffraction. Cuprolinic blue staining located sulfated glycosaminoglycan deposits that disrupted the extracellular matrix. Unlike normal cornea, which contained collagen fibrils of remarkably uniform diameter (26.0 +/- 2.4 nm), there was a large range of fibril sizes in the Scheie's syndrome stroma (19.9 to 52.0 nm). Moreover, the distribution of fibril diameters appeared bimodal. X-ray diffraction confirmed the discovery of abnormally large stromal collagen. The results suggest a link in Scheie's syndrome between proteoglycan content/distribution and stromal disruption, and between stromal disruption and corneal opacification.

KW - CORNEA

KW - STROMA

KW - PROTEOGLYCANS

KW - SCHEIE SYNDROME

KW - SYNCHROTRON

KW - X-RAY-DIFFRACTION

KW - ELECTRON-MICROSCOPY

KW - V COLLAGEN

KW - DYSTROPHY

KW - SULFATE

KW - INVITRO

KW - FIBRILS

KW - FIBRILLOGENESIS

KW - ORGANIZATION

M3 - Journal article

VL - 28

SP - 266

EP - 272

JO - Canadian Journal of Ophthalmology

JF - Canadian Journal of Ophthalmology

SN - 0008-4182

IS - 6

ER -