Assembly of 100 nm periodic fibrils (type VI collagen) in human infant corneal stroma.
An experimental model for the age-related changes in the extracellular matrix of the human cornea was developed. Human infant corneal stroma in which no long-spacing collagen occurred naturally was treated with 20 mM adenosine triphosphate (ATP). The ATP-treated cornea was observed and compared with nontreated control specimens by electron microscopy. Numerous 100 nm periodic fibrils which resembled long-spacing collagen were formed by the treatment. These experimentally formed fibrils appeared to attract and aggregate the collagen fibrils with D-periodicity, which indicated a connection between type VI and type I collagen. By ruthenium red staining, the cross-bands of the 100 nm periodic fibrils were positively stained, indicating that glycosaminoglycans or proteoglycans were involved in the formation of these fibrils.
Nakamura
M
M
Department of Ophthalmology, Nagoya University School of Medicine, Japan.
Kobayashi
M
M
Hirano
K
K
Kobayashi
K
K
Hoshino
T
T
Awaya
S
S
D000255:Adenosine Triphosphate; D003094:Collagen / Q000378:metabolism / Q000648:ultrastructure*; D003319:Corneal Stroma / Q000648:ultrastructure*; D005109:Extracellular Matrix / Q000378:metabolism; D006801:Humans; D007223:Infant; D008297:Male; D008954:Models, Biological; D012430:Ruthenium Red
D012430:Ruthenium Red; D000255:Adenosine Triphosphate; D003094:Collagen