19824014

Source:http://linkedlifedata.com/resource/pubmed/id/19824014

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0205195, umls-concept:C0237401, umls-concept:C0246868, umls-concept:C0302891, umls-concept:C0441472, umls-concept:C0443469, umls-concept:C0670751
pubmed:issue	12
pubmed:dateCreated	2009-12-9
pubmed:abstractText	Pancreatic lipase (PL) and pancreatic lipase-related proteins 1 and 2 (PLRP1 and PLRP2) display different functional properties, despite close structures. The aim of the study was to compare the kinetic properties of recombinant human PLRP1, PLRP2, and PL on a physiological substrate: the milk fat under native and homogenized structures. No lipolytic activity is measured for PLRP1. PLRP2 hydrolyses milk fat with a lower catalytic efficiency than that of PL. PLRP2 activity, higher on homogenized than on native milk fat, is differently influenced by fatty acids (FA) and colipase depending on a proteolytic cleavage in the lid domain. FA enhance the activity on both milks. A colipase positive effect on the non-proteolyzed PLRP2 is observed on homogenized milk and with FA on native milk fat. Bile salts are necessary. An original observation is a synergic effect between PL and PLRP2 on the two milks. An inhibitory effect of PLRP1 on PL activity is also demonstrated. The combined action of pancreatic lipases on milk fat digestion proposes PLRPs as modulators of PL. Our study supports the hypothesis of a major role of PLRP2 in fat digestion in newborns and brings new insights to understand the physiological role of PLRPs.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101231818
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Bile Acids and Salts, http://linkedlifedata.com/resource/pubmed/chemical/Colipases, http://linkedlifedata.com/resource/pubmed/chemical/Dietary Fats, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Nonesterified, http://linkedlifedata.com/resource/pubmed/chemical/Glycolipids, http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Lipase, http://linkedlifedata.com/resource/pubmed/chemical/PNLIP protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/milk fat globule, http://linkedlifedata.com/resource/pubmed/chemical/pancreatic lipase related protein 2, http://linkedlifedata.com/resource/pubmed/chemical/pancreatic lipase-related protein 1
pubmed:status	MEDLINE
pubmed:month	Dec
pubmed:issn	1613-4133
pubmed:author	pubmed-author:BertonAmélieA, pubmed-author:CrenonIsabelleI, pubmed-author:LopezChristelleC, pubmed-author:RouvellacStéphanieS, pubmed-author:Sebban-KreuzerCorinneC
pubmed:issnType	Electronic
pubmed:volume	53
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1592-602
pubmed:meshHeading	pubmed-meshheading:19824014-Animals, pubmed-meshheading:19824014-Bile Acids and Salts, pubmed-meshheading:19824014-Colipases, pubmed-meshheading:19824014-Dietary Fats, pubmed-meshheading:19824014-Fatty Acids, Nonesterified, pubmed-meshheading:19824014-Food Handling, pubmed-meshheading:19824014-Glycolipids, pubmed-meshheading:19824014-Glycoproteins, pubmed-meshheading:19824014-Humans, pubmed-meshheading:19824014-Kinetics, pubmed-meshheading:19824014-Lipase, pubmed-meshheading:19824014-Milk, pubmed-meshheading:19824014-Recombinant Proteins
pubmed:year	2009
pubmed:articleTitle	Individual and combined action of pancreatic lipase and pancreatic lipase-related proteins 1 and 2 on native versus homogenized milk fat globules.
pubmed:affiliation	UMR INRA, INSERM U, Univ Aix-Marseille, France.
pubmed:publicationType	Journal Article, Comparative Study, Research Support, Non-U.S. Gov't