Tissue and species differences in bile salt-dependent neutral cholesteryl ester hydrolase activity and gene expression.
- 1 March 1992
- journal article
- research article
- Published by Wolters Kluwer Health in Arteriosclerosis and Thrombosis: A Journal of Vascular Biology
- Vol. 12 (3) , 295-301
- https://doi.org/10.1161/01.atv.12.3.295
Abstract
Enzymatic activity and mRNA abundance for neutral bile salt-dependent cholesteryl ester hydrolase (CEH) were determined in rat and rabbit tissues. In rat liver and intestine, enzyme activity and mRNA levels varied independently. Particularly striking in most tissue samples was the absence of detectable CEH mRNA in the presence of enzymatic activity, suggesting that there was an exogenous source of enzyme. Rabbits differed from rats in four ways. First, neither CEH activity nor mRNA was present in any liver sample. Second, CEH mRNA was present in nearly all intestinal samples, and its abundance tended to correlate with enzymatic activity. Third, rabbit CEH mRNA was approximately 250 bases shorter than the rat message. Fourth, we have previously shown that rat plasma contains CEH activity, whereas in the present studies, rabbit plasma did not contain such activity. Overall, our studies indicate that CEH activity in rat liver, intestine, and plasma can be derived exogenously, most likely from the uptake and transport of pancreatic enzyme. In contrast, in rabbit the lack of CEH activity in plasma and liver and the capacity of the intestine for in situ synthesis of CEH suggest that this animal does not have the same ability to distribute pancreatic CEH. These species differences in CEH metabolism may partly explain the greater susceptibility of rabbit tissues to accumulate cholesteryl esters.Keywords
This publication has 17 references indexed in Scilit:
- Lipoprotein lipase modulates net secretory output of apolipoprotein B in vitro. A possible pathophysiologic explanation for familial combined hyperlipidemia.Journal of Clinical Investigation, 1991
- Cloning of the bovine pancreatic cholesterol esterase/lysophospholipaseBiochemical and Biophysical Research Communications, 1989
- Molecular cloning and expression of cDNA for rat pancreatic cholesterol esteraseBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1989
- Identity of a cytosolic neutral cholesterol esterase in rat liver with the bile salt stimulated cholesterol esterase in pancreasBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1989
- Independent effects of diet and nutritional status on apoprotein B gene expression in rabbit.Arteriosclerosis: An Official Journal of the American Heart Association, Inc., 1988
- Bile salt-dependent, neutral cholesteryl ester hydrolase of rat liver: Possible relationship with pancreatic cholesteryl ester hydrolaseBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1988
- Lipoprotein lipase in liver. Release by heparin and immunocytochemical localizationBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1988
- Subcellular localization of cholesterol ester hydrolase in the human intestineBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1987
- Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloningBiochemistry, 1987
- ANALYTICAL STUDY OF MICROSOMES AND ISOLATED SUBCELLULAR MEMBRANES FROM RAT LIVERThe Journal of cell biology, 1974