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Article: Cloning and regulation of hamster microsomal triglyceride transfer protein. The regulation is independent from that of other hepatic and intestinal proteins which participate in the transport of fatty acids and triglycerides

TitleCloning and regulation of hamster microsomal triglyceride transfer protein. The regulation is independent from that of other hepatic and intestinal proteins which participate in the transport of fatty acids and triglycerides
Authors
Issue Date1994
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1994, v. 269 n. 46, p. 29138-29145 How to Cite?
AbstractMicrosomal triglyceride transfer protein (MTP) is a heterodimer consisting of protein disulfide isomerase and a unique large subunit. Recent studies showing that an absence of MTP is a cause of abetalipoproteinemia indicate that MTP is required for the assembly of very low density lipoproteins in the liver and chylomicrons in the intestine. In this study, complementary DNA encoding the large subunit of hamster MTP was cloned. The cDNA sequence was used to design a 50-base pair oligonucleotide probe for a solution hybridization assay to quantitate MTP large subunit mRNA levels in a study of MTP regulation in male Syrian Golden hamsters. In animals fed a low fat diet, MTP exhibited a proximal to distal gradient of expression in the intestine. MTP activity and large subunit mRNA levels in the liver were about 25 and 10% that found in the proximal intestine, respectively. To investigate the effect of diet on MTP, hamsters were maintained for 31 days on one of four diets: 1) control low fat, 2) high fat, 3) low fat, high sucrose, or 4) diet 1 followed by a 48-h fast. The high fat diet increased MTP large subunit mRNA levels in the liver and throughout the small and large intestine. A 55 and 126% increase was observed in the liver and intestine (duodenum and jejunum), respectively. A 40% increase of intestinal MTP protein mass was also observed. The high sucrose diet caused a significant 55% increase in hepatic MTP mRNA levels but did not significantly affect the intestinal mRNA levels. MTP mRNA levels were unchanged in response to fasting. A short term dietary study showed that intestinal MTP mRNA was up-regulated within 24 h after initiating a high fat diet. An acute hepatic response was not observed. The regulation of MTP mRNA levels by high fat diets was compared to that of the liver fatty acid binding protein (L-FABP) and apolipoprotein B (apoB). ApoB mRNA levels were not significantly affected by a high fat diet. Although L- FABP mRNA levels were increased in the liver and intestine, the onset of the changes did not parallel that of MTP. These results suggest that L-FABP, apoB, and MTP, three proteins which play important roles in the transport of fatty acids and triglyceride in the liver and intestine, are not coordinately regulated by diet in hamsters.
Persistent Identifierhttp://hdl.handle.net/10722/167517
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLin, MCMen_US
dc.contributor.authorArbeeny, Cen_US
dc.contributor.authorBergquist, Ken_US
dc.contributor.authorKienzle, Ben_US
dc.contributor.authorGordon, DAen_US
dc.contributor.authorWetterau, JRen_US
dc.date.accessioned2012-10-08T03:07:59Z-
dc.date.available2012-10-08T03:07:59Z-
dc.date.issued1994en_US
dc.identifier.citationJournal Of Biological Chemistry, 1994, v. 269 n. 46, p. 29138-29145en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/167517-
dc.description.abstractMicrosomal triglyceride transfer protein (MTP) is a heterodimer consisting of protein disulfide isomerase and a unique large subunit. Recent studies showing that an absence of MTP is a cause of abetalipoproteinemia indicate that MTP is required for the assembly of very low density lipoproteins in the liver and chylomicrons in the intestine. In this study, complementary DNA encoding the large subunit of hamster MTP was cloned. The cDNA sequence was used to design a 50-base pair oligonucleotide probe for a solution hybridization assay to quantitate MTP large subunit mRNA levels in a study of MTP regulation in male Syrian Golden hamsters. In animals fed a low fat diet, MTP exhibited a proximal to distal gradient of expression in the intestine. MTP activity and large subunit mRNA levels in the liver were about 25 and 10% that found in the proximal intestine, respectively. To investigate the effect of diet on MTP, hamsters were maintained for 31 days on one of four diets: 1) control low fat, 2) high fat, 3) low fat, high sucrose, or 4) diet 1 followed by a 48-h fast. The high fat diet increased MTP large subunit mRNA levels in the liver and throughout the small and large intestine. A 55 and 126% increase was observed in the liver and intestine (duodenum and jejunum), respectively. A 40% increase of intestinal MTP protein mass was also observed. The high sucrose diet caused a significant 55% increase in hepatic MTP mRNA levels but did not significantly affect the intestinal mRNA levels. MTP mRNA levels were unchanged in response to fasting. A short term dietary study showed that intestinal MTP mRNA was up-regulated within 24 h after initiating a high fat diet. An acute hepatic response was not observed. The regulation of MTP mRNA levels by high fat diets was compared to that of the liver fatty acid binding protein (L-FABP) and apolipoprotein B (apoB). ApoB mRNA levels were not significantly affected by a high fat diet. Although L- FABP mRNA levels were increased in the liver and intestine, the onset of the changes did not parallel that of MTP. These results suggest that L-FABP, apoB, and MTP, three proteins which play important roles in the transport of fatty acids and triglyceride in the liver and intestine, are not coordinately regulated by diet in hamsters.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshApolipoproteins B - Geneticsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshBiological Transporten_US
dc.subject.meshCarrier Proteins - Genetics - Metabolismen_US
dc.subject.meshCholesterol Ester Transfer Proteinsen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshCricetinaeen_US
dc.subject.meshDna, Complementaryen_US
dc.subject.meshDietary Fats - Administration & Dosageen_US
dc.subject.meshFatty Acid-Binding Proteinsen_US
dc.subject.meshFatty Acids - Metabolismen_US
dc.subject.meshGlycoproteinsen_US
dc.subject.meshIntestines - Metabolismen_US
dc.subject.meshMaleen_US
dc.subject.meshMesocricetusen_US
dc.subject.meshMicrosomes, Liver - Metabolismen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNeoplasm Proteinsen_US
dc.subject.meshRna, Messenger - Genetics - Metabolismen_US
dc.subject.meshTriglycerides - Metabolismen_US
dc.titleCloning and regulation of hamster microsomal triglyceride transfer protein. The regulation is independent from that of other hepatic and intestinal proteins which participate in the transport of fatty acids and triglyceridesen_US
dc.typeArticleen_US
dc.identifier.emailLin, MCM:mcllin@hkucc.hku.hken_US
dc.identifier.authorityLin, MCM=rp00746en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.pmid7961879-
dc.identifier.scopuseid_2-s2.0-0028052292en_US
dc.identifier.volume269en_US
dc.identifier.issue46en_US
dc.identifier.spage29138en_US
dc.identifier.epage29145en_US
dc.identifier.isiWOS:A1994PU16800091-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLin, MCM=7404816359en_US
dc.identifier.scopusauthoridArbeeny, C=6701395075en_US
dc.identifier.scopusauthoridBergquist, K=6701851981en_US
dc.identifier.scopusauthoridKienzle, B=6603360124en_US
dc.identifier.scopusauthoridGordon, DA=35396397000en_US
dc.identifier.scopusauthoridWetterau, JR=7003768777en_US

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