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Am J Physiol Gastrointest Liver Physiol 280: G1187-G1196, 2001;
0193-1857/01 $5.00
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Vol. 280, Issue 6, G1187-G1196, June 2001

The intestine expresses pancreatic triacylglycerol lipase: regulation by dietary lipid

James T. Mahan, Ghanshyam D. Heda, R. Hanumantha Rao, and Charles M. Mansbach II

Department of Medicine, Division of Gastroenterology, The University of Tennessee, Memphis, Memphis 38163; and The Veterans Affairs Medical Center, Memphis, Tennessee 38104

We identified the enzyme responsible for alkaline lipolysis in mucosa of rat small intestine. RT-PCR was used to amplify a transcript that, by cloning and sequencing, is identical to pancreatic triacylglycerol lipase. In rats fed normal laboratory chow, pancreatic triacylglycerol lipase mRNA was detected in all four quarters of the small intestine, with the first quarter expressing about three times as much of this transcript as was found in the more distal three-quarters combined. Both acutely and chronically administered dietary fat were shown to regulate pancreatic triacylglycerol lipase mRNA expression and lipase activity. The synthesis of pancreatic triacylglycerol lipase protein by the small intestine was demonstrated by in vivo radiolabeling experiments using [35S]methionine/cysteine followed by immunoprecipitation with an anti-pancreatic triacylglycerol lipase antibody. Immunohistochemical studies suggest that pancreatic triacylglycerol lipase protein expression is restricted to enterocytes throughout the small intestine. To our knowledge, this is the first report identifying rat small intestinal mucosa as a site of pancreatic triacylglycerol lipase synthesis and the first demonstration of its modulation in the mucosa by dietary fat. We propose that pancreatic triacylglycerol lipase is used by the intestine to hydrolyze the mucosal triacylglycerol that is not transported in chylomicrons.

lipid absorption


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