The influence of lipase on serum lipase and lipids; a pilot study.

The purpose of this study was to determine the effect of lipase given by mouth on serum lipids, serum lipase and urinary lipase in patients with psoriasis Pancreatic secretion is under hormonal control. Secretin, elaborated by the duodenal mucosa, in response to acid chyme, is transported by the blood stream to the pancreas, activating secretion of pancreatic juice. Still another substance originating in the intestinal mucosa which affects pancreatic function is pancreozymin. This hormone is apparently restricted in its activity to stimulation of pancreatic enzymes and does not influence the actual volume of pancreatic juice. Other pancreatic hormones include lipocaic and insulin, products of the alpha and beta cells respectively. It is possible that lipocaic is functionally similar to pyridoxine hydrochloride. The enzymes identified in pancreatic juice include trypsin, chymotrypsin, carboxypeptidase, amylopsin (amylase), steapsin (lipase) and cholesterol esterase. Some of these are secreted in the form of precursors (zymogens) such as trypsinogen and chyrnotrypsinogen, which on contact with the intestinal mucosa are activated by some as yet undetermined means. In view of many reports of improvement of patients with psoriasis following the administration of various pancreatic enzymatic fractions, (1) including whole defatted pancreas itself, (2) it was thought that more definitive information might be obtained by administration of these pancreatic fractions alone. The first study was confined to the lipolytic enzyme. Since pancreatic lipase (steapsin) requires an alkaline medium for activity, a search was made for a lipase active in an acid medium, as it was considered desirable that lipolysis begin in the stomach; and also in order to avoid any destruction of the enzyme by hydrochloric acid. A lipase consisting of a purified enzyme preparation of microbial origin was selected which hydrolysed fats and fatty acid esters according to the following scheme. Lipid + (lipase) — monoand di-glycerides + fatty acids Fatty acid esters + (lipase) alcohol + fatty acids Maximum activity is obtained between pH 5 and 7 and is checked by inactivation of the enzyme by a shift of the pH to below 1.5 or to above 10. This lipase does not require emulsification of lipids prior to lipolysis but is capable of hydrolysing from 20 to 25 times its weight of emulsified fat in two and a half hours. It has almost no proteolytic activity at pH 7.