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The lipase C-terminal domain. A novel unusual inhibitor of pancreatic lipase activity.

Identifieur interne : 000089 ( France/Analysis ); précédent : 000088; suivant : 000090

The lipase C-terminal domain. A novel unusual inhibitor of pancreatic lipase activity.

Auteurs : L. Ayvazian [France] ; B. Kerfelec ; S. Granon ; E. Foglizzo ; I. Crenon ; C. Dubois ; C. Chapus

Source :

RBID : pubmed:11154696

Mots-clés :

Abstract

In vertebrates, dietary fat digestion mainly results from the combined effect of pancreatic lipase, colipase, and bile. It has been proposed that in vivo lipase adsorption on oil-water emulsion is mediated by a preformed lipase-colipase-mixed micelle complex. The main lipase-colipase binding site is located on the C-terminal domain of the enzyme. We report here that in vitro the isolated C-terminal domain behaves as a potent noncovalent inhibitor of lipase and that the inhibitory effect is triggered by the presence of micelles. Lipase inhibition results from the formation of a nonproductive C-terminal domain-colipase-micelle ternary complex, which competes for colipase with the active lipase-colipase-micelle ternary complex, thus diverting colipase from its lipase-anchoring function. The formation of such a complex has been evidenced by molecular sieving experiments. This nonproductive complex lowers the amount of active lipase thus reducing lipolysis. Preliminary experiments performed in rats show that the C-terminal domain also behaves as an inhibitor in vivo and thus could be considered a potential new tool for specifically reducing intestinal lipolysis.


DOI: 10.1074/jbc.M010328200


Affiliations:


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pubmed:11154696

Le document en format XML

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<term>Colipases (isolation & purification)</term>
<term>Enzyme Inhibitors (pharmacology)</term>
<term>Kinetics</term>
<term>Lipase (chemistry)</term>
<term>Lipase (isolation & purification)</term>
<term>Male</term>
<term>Micelles</term>
<term>Models, Molecular</term>
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<div type="abstract" xml:lang="en">In vertebrates, dietary fat digestion mainly results from the combined effect of pancreatic lipase, colipase, and bile. It has been proposed that in vivo lipase adsorption on oil-water emulsion is mediated by a preformed lipase-colipase-mixed micelle complex. The main lipase-colipase binding site is located on the C-terminal domain of the enzyme. We report here that in vitro the isolated C-terminal domain behaves as a potent noncovalent inhibitor of lipase and that the inhibitory effect is triggered by the presence of micelles. Lipase inhibition results from the formation of a nonproductive C-terminal domain-colipase-micelle ternary complex, which competes for colipase with the active lipase-colipase-micelle ternary complex, thus diverting colipase from its lipase-anchoring function. The formation of such a complex has been evidenced by molecular sieving experiments. This nonproductive complex lowers the amount of active lipase thus reducing lipolysis. Preliminary experiments performed in rats show that the C-terminal domain also behaves as an inhibitor in vivo and thus could be considered a potential new tool for specifically reducing intestinal lipolysis.</div>
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