{"id":{"repo_id":"wfu","oai_identifier":"oai:wakespace.lib.wfu.edu:10339/38589"},"canonical_url":"https://search.dev.ndltd.org/etd/wfu/oai:wakespace.lib.wfu.edu:10339/38589","repository":{"repo_id":"wfu","name":"Wake Forest University","base_url":"https://wakespace.lib.wfu.edu/oai/request"},"display":{"title":"THE IMPACT OF MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN ON INTRACELLULAR HEPATIC NEUTRAL LIPID DISTRIBUTION AND TRAFFICKING","abstract":"Microsomal triglyceride transfer protein (MTP) is a multifunctional protein necessary for conversion of apolipoprotein B into precursor lipoproteins and bulk triglyceride (TG) movement into the endoplasmic reticulum (ER) for precursor lipoprotein expansion. Invertebrate forms of MTP (e.g. Drosophila; dMTP) are capable of phospholipid (PL) transfer, whereas vertebrate forms (e.g. human; hMTP) engage in PL and TG transfer. We hypothesized that PL transfer is the primordial activity of MTP necessary for precursor lipoprotein particle formation, whereas TG transfer is a vertebrate adaptation necessary for trafficking of TG into the ER for 2nd-step assembly. Hence, we assessed hMTP's ability to promote TG trafficking into the ER of transiently transfected or stable, Dox-inducible, non-hepatic cell lines. In cell lines that expressed hMTP, a 2.5 - 5.0-fold increase in microsomal TG content was observed. The lipid-transfer activity of MTP was necessary for this function as in the presence of a potent MTP inhibitor, BMS-212122, microsomal TG content was similar to mock-transfected cells. To determine if the TG-transfer activity of MTP facilitated TG translocation we compared the TG content of microsomes from hMTP and dMTP expressing cells. Compared to mock-transfected cells, hMTP increased microsomal TG content by ~2.5-fold while cells transfected with dMTP demonstrated no increase in microsomal TG content. These data indicate that MTP promotes TG trafficking into the ER and that the TG-transfer activity of MTP is essential for this function.","abstract_html":"Microsomal triglyceride transfer protein (MTP) is a multifunctional protein necessary for conversion of apolipoprotein B into precursor lipoproteins and bulk triglyceride (TG) movement into the endoplasmic reticulum (ER) for precursor lipoprotein expansion. Invertebrate forms of MTP (e.g. Drosophila; dMTP) are capable of phospholipid (PL) transfer, whereas vertebrate forms (e.g. human; hMTP) engage in PL and TG transfer. We hypothesized that PL transfer is the primordial activity of MTP necessary for precursor lipoprotein particle formation, whereas TG transfer is a vertebrate adaptation necessary for trafficking of TG into the ER for 2nd-step assembly. Hence, we assessed hMTP's ability to promote TG trafficking into the ER of transiently transfected or stable, Dox-inducible, non-hepatic cell lines. In cell lines that expressed hMTP, a 2.5 - 5.0-fold increase in microsomal TG content was observed. The lipid-transfer activity of MTP was necessary for this function as in the presence of a potent MTP inhibitor, BMS-212122, microsomal TG content was similar to mock-transfected cells. To determine if the TG-transfer activity of MTP facilitated TG translocation we compared the TG content of microsomes from hMTP and dMTP expressing cells. Compared to mock-transfected cells, hMTP increased microsomal TG content by ~2.5-fold while cells transfected with dMTP demonstrated no increase in microsomal TG content. These data indicate that MTP promotes TG trafficking into the ER and that the TG-transfer activity of MTP is essential for this function.","abstract_has_math":false,"creators":["MacArthur, Philip Scott"],"institution":"Wake Forest University","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2013,"date_issued":"2013","date_published":"2013","updated_at":"2026-07-27T22:01:39Z","subjects":["ApoB"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10339/38589","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["MacArthur, Philip Scott"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2013-06-06T21:19:41Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2015-06-06T08:30:09Z"]},{"key":"dc:date.issued","label":"Date","values":["2013"]},{"key":"dc:publisher","label":"Institution","values":["Wake Forest University"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["ApoB"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10339/38589"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Microsomal triglyceride transfer protein (MTP) is a multifunctional protein necessary for conversion of apolipoprotein B into precursor lipoproteins and bulk triglyceride (TG) movement into the endoplasmic reticulum (ER) for precursor lipoprotein expansion. Invertebrate forms of MTP (e.g. Drosophila; dMTP) are capable of phospholipid (PL) transfer, whereas vertebrate forms (e.g. human; hMTP) engage in PL and TG transfer. We hypothesized that PL transfer is the primordial activity of MTP necessary for precursor lipoprotein particle formation, whereas TG transfer is a vertebrate adaptation necessary for trafficking of TG into the ER for 2nd-step assembly. Hence, we assessed hMTP's ability to promote TG trafficking into the ER of transiently transfected or stable, Dox-inducible, non-hepatic cell lines. In cell lines that expressed hMTP, a 2.5 - 5.0-fold increase in microsomal TG content was observed. The lipid-transfer activity of MTP was necessary for this function as in the presence of a potent MTP inhibitor, BMS-212122, microsomal TG content was similar to mock-transfected cells. To determine if the TG-transfer activity of MTP facilitated TG translocation we compared the TG content of microsomes from hMTP and dMTP expressing cells. Compared to mock-transfected cells, hMTP increased microsomal TG content by ~2.5-fold while cells transfected with dMTP demonstrated no increase in microsomal TG content. These data indicate that MTP promotes TG trafficking into the ER and that the TG-transfer activity of MTP is essential for this function."]},{"key":"dc:title","label":"Title","values":["THE IMPACT OF MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN ON INTRACELLULAR HEPATIC NEUTRAL LIPID DISTRIBUTION AND TRAFFICKING"]}]}],"canonical_facts":{"dc:creator":["MacArthur, Philip Scott"],"dc:date.accessioned":["2013-06-06T21:19:41Z"],"dc:date.available":["2015-06-06T08:30:09Z"],"dc:date.issued":["2013"],"dc:description.abstract":["Microsomal triglyceride transfer protein (MTP) is a multifunctional protein necessary for conversion of apolipoprotein B into precursor lipoproteins and bulk triglyceride (TG) movement into the endoplasmic reticulum (ER) for precursor lipoprotein expansion. Invertebrate forms of MTP (e.g. Drosophila; dMTP) are capable of phospholipid (PL) transfer, whereas vertebrate forms (e.g. human; hMTP) engage in PL and TG transfer. We hypothesized that PL transfer is the primordial activity of MTP necessary for precursor lipoprotein particle formation, whereas TG transfer is a vertebrate adaptation necessary for trafficking of TG into the ER for 2nd-step assembly. Hence, we assessed hMTP's ability to promote TG trafficking into the ER of transiently transfected or stable, Dox-inducible, non-hepatic cell lines. In cell lines that expressed hMTP, a 2.5 - 5.0-fold increase in microsomal TG content was observed. The lipid-transfer activity of MTP was necessary for this function as in the presence of a potent MTP inhibitor, BMS-212122, microsomal TG content was similar to mock-transfected cells. To determine if the TG-transfer activity of MTP facilitated TG translocation we compared the TG content of microsomes from hMTP and dMTP expressing cells. Compared to mock-transfected cells, hMTP increased microsomal TG content by ~2.5-fold while cells transfected with dMTP demonstrated no increase in microsomal TG content. These data indicate that MTP promotes TG trafficking into the ER and that the TG-transfer activity of MTP is essential for this function."],"dc:identifier.uri":["http://hdl.handle.net/10339/38589"],"dc:language.iso":["en"],"dc:publisher":["Wake Forest University"],"dc:subject":["ApoB"],"dc:title":["THE IMPACT OF MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN ON INTRACELLULAR HEPATIC NEUTRAL LIPID DISTRIBUTION AND TRAFFICKING"],"dc:type":["Dissertation"]},"updated_at":"2026-07-27T22:01:39Z"}