December 2002
Volume 43, Issue 13
Free
ARVO Annual Meeting Abstract  |   December 2002
>Analysis of the Basal Laminar Deposit Associated with Sorsby's Fundus Dystrophy
Author Affiliations & Notes
  • V Chong
    Dept of Pathology Institute of Ophthalmology and Moorfields Eye Hosptial London United Kingdom
  • C Knupp
    Biological Structure and Function Section Imperial College Faculty of Medicine London United Kingdom
  • PM G Munro
    Dept of Pathology Institute of Ophthalmology and Moorfields Eye Hosptial London United Kingdom
  • PJ Luthert
    Dept of Pathology Institute of Ophthalmology and Moorfields Eye Hosptial London United Kingdom
  • JM Squire
    Biological Structure and Function Section Imperial College Faculty of Medicine London United Kingdom
  • Footnotes
    Commercial Relationships   V. Chong, None; C. Knupp, None; P.M.G. Munro, None; P.J. Luthert, None; J.M. Squire, None.
Investigative Ophthalmology & Visual Science December 2002, Vol.43, 2792. doi:
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      V Chong, C Knupp, PM G Munro, PJ Luthert, JM Squire; >Analysis of the Basal Laminar Deposit Associated with Sorsby's Fundus Dystrophy . Invest. Ophthalmol. Vis. Sci. 2002;43(13):2792.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Abstract: : Purpose: To analyse the basal laminar deposit associated with Sorsby's fundus dystrophy (SFD). Methods: The Bruch's membrane of a SFD donor with confirmed TIMP-3 mutation was examined with electron microscopy. The periodicity and the banding pattern of these deposits were measured and analysed. Results:The deposits found in the Bruch's membrane of SFD can be classified into two types, one characterised structurally by single broad transverse bands occurring periodically every 100 nm, and the other with pairs of transverse bands (30 nm apart) occurring every 100 nm. Collagen VI is considered to be the most likely protein in these deposits. Furthermore, the deposits associated with SFD can both be explained in terms of collagen VI tetramers, one in which the tetramers bind to the mutant TIMP-3 and the other in which little or no binding occurs. Conclusion:TIMP-3 bound to collagen VI may be more resistant to degradation and create imbalance between the normal amount of TIMP-3 and MMP's in the Bruch's membrane. This may, in turn, cause disruption of the normal metabolic processes. As similar deposits are also found in age-related macular degeneration (AMD), understanding the structure of these collagen VI / TIMP assemblies in the Bruch's membrane may prove to be important for shedding light upon the pathophysiological mechanisms of SFD as well as AMD.

Keywords: 308 age-related macular degeneration • 507 pathology: human • 562 retinal degenerations: hereditary 
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