Histopathologic and immunochemical features of lattice corneal dystrophy type III

Am J Ophthalmol. 1987 Sep 15;104(3):249-54. doi: 10.1016/0002-9394(87)90412-0.


We examined seven corneas from five patients with a new form of lattice corneal dystrophy (designated lattice corneal dystrophy type III) by light and electron microscopy. Numerous amyloid deposits were scattered throughout the corneal stroma, some of which were much larger than those usually observed in either lattice corneal dystrophy type I or II; these were located predominantly midway between the epithelium and the endothelium. Image analysis disclosed that the cross-sectional size of the large stromal amyloid deposits was significantly greater than those in age-matched patients with lattice corneal dystrophy type I. All patients had a discontinuous band of amyloid (15 to 25 micron wide) in the superficial stroma beneath Bowman's layer, which usually had only one or two small disruptions. Descemet's membrane and the endothelium were normal. The stromal deposits, which were composed of 10-nm diameter fibrils typical of amyloid, stained positively with Congo red after the histologic sections were pretreated with dilute potassium permanganate. Immunohistochemical studies on formalin-fixed, paraffin-embedded tissue indicated that only some deposits reacted weakly with antibodies to amyloid protein AA. The deposits stained positively with antibodies to protein AP and negatively with antibodies to kappa and lambda immunoglobulin light chains.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amyloid / metabolism
  • Cornea / pathology
  • Cornea / ultrastructure
  • Corneal Dystrophies, Hereditary / classification*
  • Corneal Dystrophies, Hereditary / genetics
  • Corneal Dystrophies, Hereditary / metabolism
  • Corneal Dystrophies, Hereditary / pathology
  • Epithelium / pathology
  • Epithelium / ultrastructure
  • Histocytochemistry
  • Humans
  • Immunochemistry
  • Microscopy, Electron


  • Amyloid