Accumulation and pepsin solubility of collagens in the bowel of patients with Crohn's disease.
The collagen content of resected strictured intestine, with and without fistulas, from patients with Crohn's disease has been compared with that in macroscopically normal intestine removed from the same patients and from others without inflammatory bowel disease. Collagen content per unit wet or dry weight of tissue was significantly increased in all grossly diseased tissue whether fistulated or not. Although there was a significant increase in collagen types I, III, and V in diseased tissue, the relative proportions of major collagen types extracted by limited pepsin digestion were similar for both Crohn's and non-Crohn's intestine (type I, 65 to 70 percent; type III, 25 to 30 percent; type IV, 2 to 3 percent; and type V, 2.5 to 3 percent). CNBr digestion of pepsin insoluble material showed a similar relative abundance of types I and III, indicating no major change in collagen type distribution between older (insoluble) and more newly synthesized collagen. There was no evidence of the presence of type I trimer collagen. Type VI collagen, although not quantitated, was observed in 70 percent of intestinal specimens. The proportion of total collagen solubilized by pepsin treatment was significantly greater in both grossly diseased and macroscopically normal Crohn's bowel compared with non-inflammatory bowel disease bowel. These findings suggest that there are disturbances of collagen metabolism in Crohn's intestine, which account for the stricturing process and which may predate gross pathologic changes.
Alexander
A C
AC
University of Manchester, Department of Surgery, Hope Hospital, Salford, United Kingdom.
Irving
M H
MH
D003094:Collagen / Q000378:metabolism*; D003424:Crohn Disease / Q000150:complications / Q000378:metabolism*; D006801:Humans; D007412:Intestinal Fistula / Q000209:etiology / Q000378:metabolism; D007420:Intestine, Large / Q000378:metabolism*; D010434:Pepsin A; D012995:Solubility
D003094:Collagen; D010434:Pepsin A