Two patients with clinical and pathologic features of eosinophilic fasciitis manifested serologic and systemic abnormalities that raised the question of the fundamental nature and relationship of eosinophilic fasciitis to scleroderma. In addition to the characteristic features of eosinophilic fasciitis, both patients exhibited arthritis, a predominantly mononuclear cell infiltration of muscles with normal serum muscle enzyme levels, weakly positive serum antinuclear factor, IgA deficiency, and abnormalities of pulmonary function. In addition, one patient had wide-mouthed colonic diverticulae and synovial deposits consistent with amyloid; the second patient had bone marrow hypoplasia. Although corticosteroid therapy was of benefit, hydroxychloroquine and potassium para-aminobenzoate were of further help in controlling the disorder. Biopsies from the two patients revealed inflammatory lesions to be heaviest deep in the skeletal muscle; fascia was only minimally inflamed with mild fibrosis. The findings suggest that striking fibroinflammatory lesions noted in the fascia in some patients with eosinophilic fasciitis may derive largely from spillover of lesions in neighboring skeletal muscle. Shulman recently described a scleroderma-like disease characterized clinically by thickening of the skin and pain and swelling of the distal extremities, often with rapid development of contractures (1,2). Unlike scleroderma, however, the onset was relatively rapid and followed episodes of unusual physical exertion. Furthermore, there was striking peripheral blood eosinophilia. Raynaud's phenomenon, telangiectasia, myositis, and extracutaneous manifestations were absent, as were various serologic markers including antinuclear antibodies and antibodies to the extractable nuclear antigen. Most importantly, the disease usually responded well to steroid therapy. Pathologically, the syndrome apparently differed from scleroderma in that the fibroinflammatory lesions showed a predilection for fascia, as opposed to subcutis and dermis. Patients with similar features were soon thereafter reported by others, and it was suggested that this was a clinicopathologically distinct connective tissue disease for which the name "Eosinophilic fasciitis" was proposed (3).As clinical and pathologic experience with this syndrome accumulated, the distinction between scleroderma and eosinophilic fasciitis became somewhat blurred. Much discussion has ensued as to the exact features which define this entity and differentiate it from scleroderma (43). We have recently seen two patients whose clinical and pathologic features warrant classification of their disease process as eosinophilic fasciitis. Clinical scrutiny and correlative pathologic examination, including ultrastructural study, provide some insights into the relationship of eosinophilic fasciitis and scleroderma. This report addresses the clinical, immunologic, and histologic aspects. The immunohistochemical and ultrastructural findings and the pathogenesis are discussed in detail in a separate rep...

Summary. Less observed trypsin inhibitor activity, at times significant in amount, was noted using benzoyl-DL-arginine-p-nitroanilide (BAPA) as a trypsin substrate than with a similar method using casein, with or without calcium in the system. When increasing amounts of serum were added to a constant amount of trypsin, the observed trypsin inhibitor activity was more nearly linear with the casein method. At high serum concentrations the amount of trypsin inhibitor activity remained relatively constant using casein substrate, while with BAPA the amount of inhibitor activity showed a fall with large excesses of serum. Trypsin inhibitor analysis of serum fractions obtained by Sephadex G-100 chromatography revealed that not only was trypsin inhibitor activity less with BAPA than with casein, but, in certain fractions, more enzymatic activity was present than could be ascribed to the initial trypsin used. It is suggested that the differences observed using BAPA and casein substrates may be the result of several possible factors including: (1) formation of a trypsin-α(2)-macroglobulin complex having differential hydrolytic activity for BAPA and casein, (2) trypsin activation of esterases or proteases from precursors and (3) differential results dependent on the interplay of various substrates with enzyme after alteration of the latter by inhibitor. It would appear that more accurate results can be obtained using casein substrate than BAPA substrate in studies of serum trypsin inhibitor activity.

No abstract