PANCREATIC BILE-SALT-DEPENDENT LIPASE ACTIVITY IN SERUM OF DIABETIC-PATIENTS - IS THERE A RELATIONSHIP WITH GLYCATION

1. Pancreatic bile-salt-dependent lipase has been detected in human pl asma where it has the capability to modify normal low-and high-density lipoprotein composition and structure and to reduce the atherogenicit y of oxidized low-density lipoprotein (Shamir R, Johnson WJ, Morlock-F itzpatrick K, Zolfaghari R, Li L, Mas E, Lombardo D, Morel DW, Fisher EA, Pancreatic carboxyl ester lipase: a circulating enzyme that modifi es normal and oxidized lipoproteins in vitro. J Clin Invest 1996; 97: 1696-704). 2. In the present study, we investigated the effect of glyc ation and particularly that of human serum albumin on the activity of bile-salt-dependent lipase, lit vitro, bile-salt-dependent lipase acti vity decreased in the presence of human serum albumin; however this wa s less pronounced in the presence of glycated human serum albumin. In vivo, bile-salt-dependent lipase specific activity was about 2-fold hi gher in the sera of diabetic patients than in the sera of normal subje cts. 3. A significant increase in the specific activity of bile-salt-d ependent lipase related to the serum level of glycation was observed. The increase in bile-salt-dependent lipase specific activity was not r elated to the glucose concentration in serum suggesting that glycation of bile-salt-dependent lipase could not be involved in the observed e ffects. Although the stability of serum bile-salt-dependent lipase was important enough to allow a systemic action of the enzyme on lipoprot eins, it could not explain the higher activity of the enzyme in diabet ic serum. 4. We concluded that bile-salt-dependent lipase could be hel pful against the premature development of atherosclerosis in diabetes.