1. Pancreatic
bile-salt-dependent lipase has been detected in human plasma where it has the capability to modify normal low- and
high-density lipoprotein composition and structure and to reduce the atherogenicity of
oxidized low-density lipoprotein (Shamir R, Johnson WJ, Morlock-Fitzpatrick K, Zolfaghari R, Li L, Mas E, Lombardo D, Morel DW, Fisher EA. Pancreatic carboxyl
ester lipase: a circulating
enzyme that modifies normal and oxidized
lipoproteins in vitro. J Clin Invest 1996; 97: 1696-704). 2. In the present study, we investigated the effect of glycation and particularly that of
human serum albumin on the activity of
bile-salt-dependent lipase. In vitro,
bile-salt-dependent lipase activity decreased in the presence of
human serum albumin; however, this was less pronounced in the presence of glycated
human serum albumin. In vivo,
bile-salt-dependent lipase specific activity was about 2-fold higher in the sera of diabetic patients than in the sera of normal subjects. 3. A significant increase in the specific activity of
bile-salt-dependent lipase related to the serum level of glycation was observed. The increase in
bile-salt-dependent lipase specific activity was not related to the
glucose concentration in serum suggesting that glycation of
bile-salt-dependent lipase could not be involved in the observed effects. Although the stability of serum
bile-salt-dependent lipase was important enough to allow a systemic action of the
enzyme on
lipoproteins, it could not explain the higher activity of the
enzyme in diabetic serum. 4. We concluded that
bile-salt-dependent lipase could be helpful against the premature development of
atherosclerosis in diabetes.