July 1992
Volume 33, Issue 8
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Articles  |   July 1992
Extracellular matrix in aged human ciliary body: an immunoelectron microscope study.
Author Affiliations
  • G E Marshall
    Department of Ophthalmology, University of Glasgow, Scotland.
  • A G Konstas
    Department of Ophthalmology, University of Glasgow, Scotland.
  • S Abraham
    Department of Ophthalmology, University of Glasgow, Scotland.
  • W R Lee
    Department of Ophthalmology, University of Glasgow, Scotland.
Investigative Ophthalmology & Visual Science July 1992, Vol.33, 2546-2560. doi:
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      G E Marshall, A G Konstas, S Abraham, W R Lee; Extracellular matrix in aged human ciliary body: an immunoelectron microscope study.. Invest. Ophthalmol. Vis. Sci. 1992;33(8):2546-2560.

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Abstract

Tissue from nine human eyes (ages 52-78 yr) was used to investigate the fine structural distribution of collagens I-VI and laminin in the ciliary body using the immunogold antibody labeling technique. The anterior segments of the specimens were normal, and the eyes were removed in treatment of choroidal melanoma. The basement membranes of the ciliary epithelium contained collagens I, III, and IV. Laminin was in greater concentration in the outer part of the nonpigmented epithelial basement membrane, and the distribution suggested a washout effect. The zonular apparatus labeled intensely with laminin. In contrast, laminin was not present in the basement membrane of the myocytes in the ciliary body. These cells were sheathed in a basement membrane that contained types I, III, and IV collagen. Plaque-like structures of slightly different morphology (a, filamentous; b, granular; c, amorphous) were found in the tendinous insertions, and subtypes a and b were strongly labeled with laminin. The basement membranes of the vessels contained types I and IV collagen, but laminin labeling was inconclusive. The major finding was that the lamina densa in the basement membranes of various sites labeled for collagens I, III, and IV. Striated collagen fibrils in the stroma were labeled for types I and III. Collagen subtypes V and VI were not identified in significant quantity in any of the regions examined.

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