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Identification of a novel isoform of microsomal triglyceride transfer protein.

Identification of a novel isoform of microsomal triglyceride transfer protein. Research Abstract Details 

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  • Identification of a novel isoform of microsomal triglyceride transfer protein. Abstract Text:

    peter j mohlerPeter J Mohler,mei-ying zhuMei-Ying Zhu,anna m bladeAnna M Blade,amy-joan l hamAmy-Joan L Ham,gregory s shelnessGregory S Shelness,larry l swiftLarry L Swift,

    Microsomal triglyceride transfer protein (MTP) has been studied extensively, primarily because of its role in the assembly of very low density lipoproteins by the liver and chylomicrons by the intestine. Recent studies have suggested that MTP may also play key roles in other cellular processes. In this paper we report the identification of a novel splice variant of MTP in mice. This isoform, MTP-B, has a unique first exon located approximately 2.7 kilobases upstream of canonical MTP (MTP-A) exon 1. The alternative exon encodes 35 amino acids compared with 20 amino acids encoded by exon 1 of MTP-A. MTP-B represents approximately 90% of total MTP mRNA in mouse adipocytes and 3T3-L1 cells and <5% in mouse liver and intestine. Expression of the alternate isoform in mouse liver was confirmed by mass spectrometry. Co-transfection of COS cells with truncated forms of apoB and either MTP-A or MTP-B demonstrated that both isoforms are effective in the assembly and secretion of nascent apoB-containing lipoproteins. Confocal microscopy of 3T3-L1 cells transfected with enhanced green fluorescent protein or DsRed fusions of the two proteins revealed that MTP-A is localized to the endoplasmic reticulum, whereas MTP-B localizes primarily to the Golgi complex in these cells. We conclude that MTP-B functions similarly to MTP-A in lipoprotein assembly. However, in nonlipoprotein-secreting cells, such as the adipocyte, MTP-B may have different localization properties, perhaps reflecting a distinct role in lipid storage and mobilization.

    Identification of a novel isoform of microsomal triglyceride transfer protein. Publishing Authors By Initials

    pj mohlerPJ Mohler,my zhuMY Zhu,am bladeAM Blade,aj hamAJ Ham,gs shelnessGS Shelness,ll swiftLL Swift,

    For similar investigative techniques: genetic techniques: gene transfer techniques: transfection research abstracts see: investigative techniques: genetic techniques: gene transfer techniques: transfection research

    PUBMED ID PMID:

    MEDLINE DATE:

    Identification of a novel isoform of microsomal triglyceride transfer protein. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: The Journal of biological chemistry

    VOLUME: 282

    Page Numbers: 26981-8

    Journal Abbreviation: J. Biol. Chem.

    ISSN: 0021-9258

    DAY: 16

    MONTH: 07

    YEAR: 2007

    Identification of a novel isoform of microsomal triglyceride transfer protein. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985121

    Identification of a novel isoform of microsomal triglyceride transfer protein. Keywords Mesh Terms:

    KEYWORDS: Transfection

    MESH TERMS: physiology

    Chemical & Substance for Abstract: Identification of a novel isoform of microsomal triglyceride transfer protein. Information

    Substance Name: microsomal triglyceride transfer protein

    Registry Number: 0

    Grant and Affiliation Information for Identification of a novel isoform of microsomal triglyceride transfer protein.

    AFFILIATION: Department of Internal Medicine, University of Iowa School of Medicine, Iowa City, IA 52242, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NHLBI

    GRANT: HL 57984

    ACRONYM: HL

    MEDLINETA: J Biol Chem

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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