Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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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 -