GELSOLIN IMMUNOREACTIVITY IN CORNEAL AMYLOID, WOUND-HEALING, AND MACULAR AND GRANULAR DYSTROPHIES

Immunohistologic studies of tissue sections obtained from patients wit h type 1 or type 2 lattice corneal dystrophy, polymorphic amyloid dege neration, or gelatinous amyloid degeneration were performed by using a monoclonal antibody raised to a chymotryptic fragment inclusive of th e carboxy-terminal half of plasma gelsolin, and also with a series of polyclonal antibodies specific for synthetic peptides corresponding to immunogenic epitopes of gelsolin. These epitopes are parts of sequenc es at the amino- and carboxy-terminal ends of gelsolin, as well as adj acent to and inclusive of the codon 187 mutant 7-11 kD fragment that h as been shown to be the subunit protein of amyloid fibrils occurring s ystemically in patients affected by Finnish type familial amyloidosis. These antibodies were also tested on tissue sections obtained from pa tients with granular and macular corneal dystrophy, corneal wounds, an d normal control corneas. Specificity of staining was established by a bsorption with gelsolin purified from plasma, or the appropriate synth etic peptide. Gelsolin immunoreactivity was detected in the conjunctiv al and skin amyloid in familial amyloidosis by using familial amyloid (Finnish type) antibody. In other types of corneal amyloid, including lattice dystrophy type 1, immunoreactivity with gelsolin and synthetic peptides was observed adjacent to the deposits, but rarely within the m. In macular dystrophy, variable staining of the deposits could resul t from the association of subunit protein with glycosaminoglycans.