C-reactive protein in human lattice corneal dystrophy

Abstract

Lattice corneal dystrophy (LCD), an autosomal dominantly inherited disease, is characterized by a branching network of subepithelial and stromal amyloid deposits (1). Due to their small size and close association with stromal components and epithelial cells, their chemical composition is as yet undetermined. Amyloid deposits in other types of diseases have been found to contain amyloid P protein (AP). Serum amyloid P component (SAP) and C-reactive protein (CRP) resemble each other in molecular structure and amino acid sequence, but appear to be antigenically distinct (2-6). A humoral mediator most likely stimulates CRP release by hepatocytes and could be related to Interleukin-I synthesis from macrophages (4-6). Rabbit corneal epithelial cells also produced an Interleukin-I-like activity and contain a thymocyte activating cytokine (7). In this study, corneas from normal controls, primary LCD and recurrent LCD were fixed in formalin with lmM CaCl2 and tested with antibodies to CRP, AP and AA (non-immunoamyloid), using the immunoperoxidase technique. The stroma of LCD and normal corneas did not stain with antibodies to AP, AA or CRP. However, we now report that antibodies to CRP show immunospecific binding to the corneal epithelium in primary and recurrent LCD.