Activation of horse PLRP2 by bile salts does not require colipase.
Identifieur interne : 002165 ( Main/Exploration ); précédent : 002164; suivant : 002166Activation of horse PLRP2 by bile salts does not require colipase.
Auteurs : Sandrine Jayne [France] ; Brigitte Kerfelec ; Edith Foglizzo ; Simone Granon ; Juan Hermoso ; Catherine Chapus ; Isabelle CrenonSource :
- Biochemistry [ 0006-2960 ] ; 2002.
English descriptors
- KwdEn :
- Animals, Bile Acids and Salts (pharmacology), Colipases (isolation & purification), Colipases (metabolism), Enzyme Activation, Glutamine, Horses, Kinetics, Lipase (chemistry), Lipase (isolation & purification), Lipase (metabolism), Lysine, Models, Molecular, Protein Conformation, Protein Structure, Secondary.
- MESH :
- chemical , chemistry : Lipase.
- chemical , isolation & purification : Colipases, Lipase.
- chemical , metabolism : Colipases, Lipase.
- chemical , pharmacology : Bile Acids and Salts.
- Animals, Enzyme Activation, Glutamine, Horses, Kinetics, Lysine, Models, Molecular, Protein Conformation, Protein Structure, Secondary.
Abstract
Although structurally similar to pancreatic lipase (PL), the key enzyme of intestinal fat digestion, pancreatic lipase-related protein type 2 (PLRP2) differs from PL in certain functional properties. Notably, PLRP2 has a broader substrate specificity than PL, and unlike that of PL, its activity is not restored by colipase in the presence of bile salts. In the studies presented here, the activation mechanism of horse PLRP2 was studied through active site-directed inhibition experiments, and the results demonstrate fundamental differences with that of PL. The opening of the horse PLRP2 flap occurs as soon as bile salt monomers are present, is accelerated in the presence of micelles, and does not require the presence of colipase. Moreover, in contrast to PL, horse PLRP2 is able to directly interact with a bile salt micelle to form an active binary complex, without the micelle being presented by colipase, as evidenced by molecular sieving experiments. These findings, together with the sensitivity of the horse PLRP2 flap to partial proteolysis, are indicative of a higher flexibility of the flap of horse PLRP2 relative to PL. From these results, it can be concluded that PLRP2 can adopt an active conformation in the intestine, which could be important for the further understanding of the physiological role of PLRP2. Finally, this work emphasizes the essential role of colipase in lipase catalysis at the lipid-water interface in the presence of bile.
PubMed: 12081491
Affiliations:
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Le document en format XML
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last="Foglizzo">Edith Foglizzo</name></author><author><name sortKey="Granon, Simone" sort="Granon, Simone" uniqKey="Granon S" first="Simone" last="Granon">Simone Granon</name></author><author><name sortKey="Hermoso, Juan" sort="Hermoso, Juan" uniqKey="Hermoso J" first="Juan" last="Hermoso">Juan Hermoso</name></author><author><name sortKey="Chapus, Catherine" sort="Chapus, Catherine" uniqKey="Chapus C" first="Catherine" last="Chapus">Catherine Chapus</name></author><author><name sortKey="Crenon, Isabelle" sort="Crenon, Isabelle" uniqKey="Crenon I" first="Isabelle" last="Crenon">Isabelle Crenon</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:12081491</idno><idno type="pmid">12081491</idno><idno type="wicri:Area/PubMed/Corpus">000211</idno><idno type="wicri:Area/PubMed/Curation">000211</idno><idno type="wicri:Area/PubMed/Checkpoint">000203</idno><idno type="wicri:Area/Ncbi/Merge">000085</idno><idno type="wicri:Area/Ncbi/Curation">000085</idno><idno type="wicri:Area/Ncbi/Checkpoint">000085</idno><idno type="wicri:doubleKey">0006-2960:2002:Jayne S:activation:of:horse</idno><idno type="wicri:Area/Main/Merge">002211</idno><idno type="wicri:Area/Main/Curation">002165</idno><idno type="wicri:Area/Main/Exploration">002165</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Activation of horse PLRP2 by bile salts does not require colipase.</title><author><name sortKey="Jayne, Sandrine" sort="Jayne, Sandrine" uniqKey="Jayne S" first="Sandrine" last="Jayne">Sandrine Jayne</name><affiliation wicri:level="3"><nlm:affiliation>Nutrition humaine et lipides, INSERM-U476, 18 Avenue Mozart, 13009 Marseille, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Nutrition humaine et lipides, INSERM-U476, 18 Avenue Mozart, 13009 Marseille</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Kerfelec, Brigitte" sort="Kerfelec, Brigitte" uniqKey="Kerfelec B" first="Brigitte" last="Kerfelec">Brigitte Kerfelec</name></author><author><name sortKey="Foglizzo, Edith" sort="Foglizzo, Edith" uniqKey="Foglizzo E" first="Edith" last="Foglizzo">Edith Foglizzo</name></author><author><name sortKey="Granon, Simone" sort="Granon, Simone" uniqKey="Granon S" first="Simone" last="Granon">Simone Granon</name></author><author><name sortKey="Hermoso, Juan" sort="Hermoso, Juan" uniqKey="Hermoso J" first="Juan" last="Hermoso">Juan Hermoso</name></author><author><name sortKey="Chapus, Catherine" sort="Chapus, Catherine" uniqKey="Chapus C" first="Catherine" last="Chapus">Catherine Chapus</name></author><author><name sortKey="Crenon, Isabelle" sort="Crenon, Isabelle" uniqKey="Crenon I" first="Isabelle" last="Crenon">Isabelle Crenon</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Bile Acids and Salts (pharmacology)</term><term>Colipases (isolation & purification)</term><term>Colipases (metabolism)</term><term>Enzyme Activation</term><term>Glutamine</term><term>Horses</term><term>Kinetics</term><term>Lipase (chemistry)</term><term>Lipase (isolation & purification)</term><term>Lipase (metabolism)</term><term>Lysine</term><term>Models, Molecular</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lipase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Colipases</term><term>Lipase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Colipases</term><term>Lipase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Bile Acids and Salts</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Enzyme Activation</term><term>Glutamine</term><term>Horses</term><term>Kinetics</term><term>Lysine</term><term>Models, Molecular</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Although structurally similar to pancreatic lipase (PL), the key enzyme of intestinal fat digestion, pancreatic lipase-related protein type 2 (PLRP2) differs from PL in certain functional properties. Notably, PLRP2 has a broader substrate specificity than PL, and unlike that of PL, its activity is not restored by colipase in the presence of bile salts. In the studies presented here, the activation mechanism of horse PLRP2 was studied through active site-directed inhibition experiments, and the results demonstrate fundamental differences with that of PL. The opening of the horse PLRP2 flap occurs as soon as bile salt monomers are present, is accelerated in the presence of micelles, and does not require the presence of colipase. Moreover, in contrast to PL, horse PLRP2 is able to directly interact with a bile salt micelle to form an active binary complex, without the micelle being presented by colipase, as evidenced by molecular sieving experiments. These findings, together with the sensitivity of the horse PLRP2 flap to partial proteolysis, are indicative of a higher flexibility of the flap of horse PLRP2 relative to PL. From these results, it can be concluded that PLRP2 can adopt an active conformation in the intestine, which could be important for the further understanding of the physiological role of PLRP2. Finally, this work emphasizes the essential role of colipase in lipase catalysis at the lipid-water interface in the presence of bile.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Marseille</li></settlement></list><tree><noCountry><name sortKey="Chapus, Catherine" sort="Chapus, Catherine" uniqKey="Chapus C" first="Catherine" last="Chapus">Catherine Chapus</name><name sortKey="Crenon, Isabelle" sort="Crenon, Isabelle" uniqKey="Crenon I" first="Isabelle" last="Crenon">Isabelle Crenon</name><name sortKey="Foglizzo, Edith" sort="Foglizzo, Edith" uniqKey="Foglizzo E" first="Edith" last="Foglizzo">Edith Foglizzo</name><name sortKey="Granon, Simone" sort="Granon, Simone" uniqKey="Granon S" first="Simone" last="Granon">Simone Granon</name><name sortKey="Hermoso, Juan" sort="Hermoso, Juan" uniqKey="Hermoso J" first="Juan" last="Hermoso">Juan Hermoso</name><name sortKey="Kerfelec, Brigitte" sort="Kerfelec, Brigitte" uniqKey="Kerfelec B" first="Brigitte" last="Kerfelec">Brigitte Kerfelec</name></noCountry><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Jayne, Sandrine" sort="Jayne, Sandrine" uniqKey="Jayne S" first="Sandrine" last="Jayne">Sandrine Jayne</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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