Lipolytic Enzymes of the Human Pancreas

Meyer-Bertenrath, J. G.

doi:10.1159/000459120

Enzyme

1982

DOI: 10.1159/000459120

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Lipolytic Enzymes of the Human Pancreas

J. G. Meyer-Bertenrath¹

Abstract: Cholesterol erster hydrolase (cholesterol esterase, EC 3.1.1.13) does not only act on cholesterol esters, but also on esters of fluorescein. Diesters as well as monoesters of this dye show neither color nor fluorescence, so that these compounds may be used as chromogenic or fluorogenic substrates. Splitting off the ester bonds immediately causes the return of the original properties of the fluorescein. Its dilaurate was found to be a specific substrate of cholesterol esterase, allowing the measurement of activ… Show more

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1989

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Cited by 4 publications

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Lipolytic enzymes of the human pancreas

1990

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In the oral exocrine pancreatic function test using fluorescein dilaurate, this synthetic substrate attaches primarily to the triglyceride surfaces of the neutral lipids administered as part of the breakfast: these fluorescein dilaurate molecules cannot be attacked by cholesterol esterase. In the course of triglyceride saponification by lipase and colipase, however, the fluorescein dilaurate is liberated and hydrolyzed by cholesterol esterase. The pancreatic function test, therefore, measures the lipolytic activities not merely of cholesterol esterase, but indirectly of lipase, as well.

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Lipolytic enzymes of the human pancreas

1990

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Validation of the reconstituted high-density lipoprotein (rHDL) drug delivery platform using dilauryl fluorescein (DLF)

McConathy

Paranjape

Mooberry

et al. 2011

Drug Deliv. and Transl. Res.

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Dilauryl fluorescein (DLF) is a lipid soluble molecule that becomes fluorescent when lauric acid is removed by hydrolysis The purpose of these studies was to evaluate DLF as a potential probe for the function of reconstituted high-density lipoproteins (rHDL) as hydrophobic drug transport vehicles. The DLF containing rHDL nanoparticles were characterized regarding their physical/chemical properties, including molecular diameter, molecular weight, chemical composition, and buoyant density. We investigated the uptake of DLF from rHDL in cells that overexpress the scavenger receptor (SR-B1), known to facilitate the selective cellular uptake of cholesteryl esters from HDL. These studies show that DLF can be incorporated into rHDL and redistributed in the plasma compartment. In addition, these studies demonstrated an enhanced uptake and hydrolysis of DLF from rHDL by cells that overexpress the SR-B1 receptor, suggesting the involvement of a receptor mediated mechanism. The incorporation of DLF into the rHDL nanoparticles appear to protect against hydrolysis in the systemic circulation based on the lower rate of rHDL/DLF hydrolysis compared with the free DLF during incubation with human plasma. DLF may thus be used as a probe to track the movement and metabolism of HDL core constituents, including cancer chemotherapeutic agents.

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Lipolytic enzymes of the human pancreas. II. Purification and properties of cholesterol ester hydrolase

Meyer¹

1989

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metaboli

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Lipolytic Enzymes of the Human Pancreas

Cited by 4 publications

References 11 publications

Lipolytic enzymes of the human pancreas

Lipolytic enzymes of the human pancreas

Validation of the reconstituted high-density lipoprotein (rHDL) drug delivery platform using dilauryl fluorescein (DLF)

Lipolytic enzymes of the human pancreas. II. Purification and properties of cholesterol ester hydrolase

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