EXTRACELLULAR-MATRIX PROTEINS IN BILE AND SERUM OF PATIENTS WITH GALLSTONE DISEASE

The relationship of basement membrane to interstitial collagen-related protein metabolism was investigated in a sample of 100 consecutive pa tients undergoing surgery for gallstone disease. The measurements were performed on both sem and bile specimens using specific radioimmunoas says for type IV collagen, laminin, endogenous intact human type III c ollagen aminopropeptide and its degradation product, Col. 1. While bas ement membrane related proteins, type IV collagen and laminin were dom inant in the bile, type III collagen related proteins were lower than in the corresponding serum samples. Both the intact type III procollag en peptide and its Col. 1 fragment were, however, found in the bile. T he highest bile laminin concentrations were observed in patients with gallbladder fibrosis, whereas type III aminopropeptides were elevated not only in fibrosis and cancer but, most markedly, in acute inflammat ion of the gallbladder. Bile type IV collagen concentration was also f ound to vary according to the cholesterol content of gallstones. The r esults point to differences in the metabolism of various extracellular matrix proteins during the development of gallstone disease. The asso ciation between such proteins, the histological alterations in the gal lbladder wall and the cholesterol content of gallstones may have impli cations for the pathogenesis of gallstone disease.