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  1. Article ; Online: Methods to monitor Fatty Acid transport proceeding through vectorial acylation.

    Arias-Barrau, Elsa / Dirusso, Concetta C / Black, Paul N

    Methods in molecular biology (Clifton, N.J.)

    2009  Volume 580, Page(s) 233–249

    Abstract: The process of fatty acid transport across the plasma membrane occurs by several mechanisms that involve distinct membrane-bound and membrane-associated proteins and enzymes. Among these are the fatty acid transport proteins (FATP) and long-chain acyl ... ...

    Abstract The process of fatty acid transport across the plasma membrane occurs by several mechanisms that involve distinct membrane-bound and membrane-associated proteins and enzymes. Among these are the fatty acid transport proteins (FATP) and long-chain acyl CoA synthetases (Acsl). Previous studies in yeast and adipocytes have shown FATP and Acsl form a physical complex at the plasma membrane and are required for fatty acid transport, which proceeds through a coupled process-linking transport with metabolic activation termed vectorial acylation. At present, six isoforms of FATP and five isoforms of ACSL have been identified in mice and man. In addition, there are a number of splice variants of different FATP and Acsl isoforms. The different FATP and Acsl isoforms have distinct tissue expression profiles and different cellular locations suggesting they function in the channeling of fatty acids into discrete metabolic pools. The concerted activity of these proteins is proposed to allow cells to discriminate different classes of fatty acids and provides the mechanistic basis underpinning the selectivity and specificity of the fatty acid transport process.
    MeSH term(s) 3T3-L1 Cells ; Acylation ; Animals ; Biochemistry/methods ; Biological Transport/physiology ; Cell Line ; Coenzyme A Ligases/metabolism ; Fatty Acid Transport Proteins/metabolism ; Fatty Acids/metabolism ; Humans ; Isoenzymes/metabolism ; Kinetics ; Mice ; Models, Biological
    Chemical Substances Fatty Acid Transport Proteins ; Fatty Acids ; Isoenzymes ; Coenzyme A Ligases (EC 6.2.1.-)
    Language English
    Publishing date 2009
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-60761-325-1_13
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Bacterial long chain fatty acid transport: gateway to a fatty acid-responsive signaling system.

    Dirusso, Concetta C / Black, Paul N

    The Journal of biological chemistry

    2004  Volume 279, Issue 48, Page(s) 49563–49566

    MeSH term(s) Bacteria/genetics ; Bacteria/metabolism ; Bacterial Outer Membrane Proteins/metabolism ; Cell Membrane/metabolism ; Coenzyme A Ligases/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Fatty Acid Transport Proteins ; Fatty Acids/metabolism ; Protein Conformation ; Signal Transduction/genetics ; Signal Transduction/physiology
    Chemical Substances Bacterial Outer Membrane Proteins ; Escherichia coli Proteins ; Fatty Acid Transport Proteins ; Fatty Acids ; fadL protein, E coli ; Coenzyme A Ligases (EC 6.2.1.-)
    Language English
    Publishing date 2004-08-30
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.R400026200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Identification and characterization of small compound inhibitors of human FATP2.

    Sandoval, Angel / Chokshi, Aalap / Jesch, Elliot D / Black, Paul N / Dirusso, Concetta C

    Biochemical pharmacology

    2009  Volume 79, Issue 7, Page(s) 990–999

    Abstract: Fatty acid transport proteins (FATPs) are bifunctional proteins, which transport long chain fatty acids into cells and activate very long chain fatty acids by esterification with coenzyme A. In an effort to understand the linkage between cellular fatty ... ...

    Abstract Fatty acid transport proteins (FATPs) are bifunctional proteins, which transport long chain fatty acids into cells and activate very long chain fatty acids by esterification with coenzyme A. In an effort to understand the linkage between cellular fatty acid transport and the pathology associated with excessive accumulation of exogenous fatty acids, we targeted FATP-mediated fatty acid transport in a high throughput screen of more than 100,000 small diverse chemical compounds in yeast expressing human FATP2 (hsFATP2). Compounds were selected for their ability to depress the transport of the fluorescent long chain fatty acid analogue, C(1)-BODIPY-C(12). Among 234 hits identified in the primary screen, 5 compounds, each representative of a structural class, were further characterized in the human Caco-2 and HepG2 cell lines, each of which normally expresses FATP2, and in 3T3-L1 adipocytes, which do not. These compounds were effective in inhibiting uptake with IC(50)s in the low micromolar range in both Caco-2 and HepG2 cells. Inhibition of transport was highly specific for fatty acids and there were no effects of these compounds on cell viability, trans-epithelial electrical resistance, glucose transport, or long chain acyl-CoA synthetase activity. The compounds were less effective when tested in 3T3-L1 adipocytes suggesting selectivity of inhibition. These results suggest fatty acid transport can be inhibited in a FATP-specific manner without causing cellular toxicity.
    MeSH term(s) 3T3-L1 Cells ; Animals ; Biological Transport/drug effects ; Caco-2 Cells ; Coenzyme A Ligases/metabolism ; Dose-Response Relationship, Drug ; Fatty Acid Transport Proteins/antagonists & inhibitors ; Fatty Acids/metabolism ; Hep G2 Cells ; High-Throughput Screening Assays ; Humans ; Mice ; Structure-Activity Relationship
    Chemical Substances Fatty Acid Transport Proteins ; Fatty Acids ; Coenzyme A Ligases (EC 6.2.1.-)
    Language English
    Publishing date 2009-11-11
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 208787-x
    ISSN 1873-2968 ; 0006-2952
    ISSN (online) 1873-2968
    ISSN 0006-2952
    DOI 10.1016/j.bcp.2009.11.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Long-chain acyl-CoA synthetase 6 preferentially promotes DHA metabolism.

    Marszalek, Joseph R / Kitidis, Claire / Dirusso, Concetta C / Lodish, Harvey F

    The Journal of biological chemistry

    2005  Volume 280, Issue 11, Page(s) 10817–10826

    Abstract: Previously we demonstrated that supplementation with the polyunsaturated fatty acids (PUFA) arachidonic acid (AA) or docosahexaenoic acid (DHA) increased neurite outgrowth of PC12 cells during differentiation, and that overexpression of rat acyl-CoA ... ...

    Abstract Previously we demonstrated that supplementation with the polyunsaturated fatty acids (PUFA) arachidonic acid (AA) or docosahexaenoic acid (DHA) increased neurite outgrowth of PC12 cells during differentiation, and that overexpression of rat acyl-CoA synthetase long-chain family member 6 (Acsl6, formerly ACS2) further increased PUFA-enhanced neurite outgrowth. However, whether Acsl6 overexpression enhanced the amount of PUFA accumulated in the cells or altered the partitioning of any fatty acids into phospholipids (PLs) or triacylglycerides (TAGs) was unknown. Here we show that Acsl6 overexpression specifically promotes DHA internalization, activation to DHA-CoA, and accumulation in differentiating PC12 cells. In contrast, oleic acid (OA) and AA internalization and activation to OA-CoA and AA-CoA were increased only marginally by Acsl6 overexpression. Additionally, the level of total cellular PLs was increased in Acsl6 overexpressing cells when the medium was supplemented with AA and DHA, but not with OA. Acsl6 overexpression increased the incorporation of [(14)C]-labeled OA, AA, or DHA into PLs and TAGs. These results do not support a role for Acsl6 in the specific targeting of fatty acids into PLs or TAGs. Rather, our data support the hypothesis that Acsl6 functions primarily in DHA metabolism, and that its overexpression increases DHA and AA internalization primarily during the first 24 h of neuronal differentiation to stimulate PL synthesis and enhance neurite outgrowth.
    MeSH term(s) Animals ; Arachidonic Acid/metabolism ; Blotting, Western ; Cell Differentiation ; Coenzyme A Ligases/metabolism ; Culture Media/metabolism ; Cyclophilins/metabolism ; Dehydroepiandrosterone/metabolism ; Docosahexaenoic Acids/metabolism ; Fatty Acids/metabolism ; Green Fluorescent Proteins/metabolism ; Lipid Bilayers/metabolism ; Lipids ; Neurons/metabolism ; Oleic Acid/metabolism ; PC12 Cells ; Peptidylprolyl Isomerase/metabolism ; Polymerase Chain Reaction ; RNA, Messenger/metabolism ; Rats ; Time Factors ; Triglycerides/metabolism
    Chemical Substances Culture Media ; Fatty Acids ; Lipid Bilayers ; Lipids ; RNA, Messenger ; Triglycerides ; cyclophilin B (137497-17-7) ; Green Fluorescent Proteins (147336-22-9) ; Docosahexaenoic Acids (25167-62-8) ; Arachidonic Acid (27YG812J1I) ; Oleic Acid (2UMI9U37CP) ; Dehydroepiandrosterone (459AG36T1B) ; Cyclophilins (EC 5.2.1.-) ; Peptidylprolyl Isomerase (EC 5.2.1.8) ; Coenzyme A Ligases (EC 6.2.1.-) ; long-chain-fatty-acid-CoA ligase (EC 6.2.1.3)
    Language English
    Publishing date 2005-01-17
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M411750200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Fatty acid transport and activation and the expression patterns of genes involved in fatty acid trafficking.

    Sandoval, Angel / Fraisl, Peter / Arias-Barrau, Elsa / Dirusso, Concetta C / Singer, Diane / Sealls, Whitney / Black, Paul N

    Archives of biochemistry and biophysics

    2008  Volume 477, Issue 2, Page(s) 363–371

    Abstract: These studies defined the expression patterns of genes involved in fatty acid transport, activation and trafficking using quantitative PCR (qPCR) and established the kinetic constants of fatty acid transport in an effort to define whether vectorial ... ...

    Abstract These studies defined the expression patterns of genes involved in fatty acid transport, activation and trafficking using quantitative PCR (qPCR) and established the kinetic constants of fatty acid transport in an effort to define whether vectorial acylation represents a common mechanism in different cell types (3T3-L1 fibroblasts and adipocytes, Caco-2 and HepG2 cells and three endothelial cell lines (b-END3, HAEC, and HMEC)). As expected, fatty acid transport protein (FATP)1 and long-chain acyl CoA synthetase (Acsl)1 were the predominant isoforms expressed in adipocytes consistent with their roles in the transport and activation of exogenous fatty acids destined for storage in the form of triglycerides. In cells involved in fatty acid processing including Caco-2 (intestinal-like) and HepG2 (liver-like), FATP2 was the predominant isoform. The patterns of Acsl expression were distinct between these two cell types with Acsl3 and Acsl5 being predominant in Caco-2 cells and Acsl4 in HepG2 cells. In the endothelial lines, FATP1 and FATP4 were the most highly expressed isoforms; the expression patterns for the different Acsl isoforms were highly variable between the different endothelial cell lines. The transport of the fluorescent long-chain fatty acid C(1)-BODIPY-C(12) in 3T3-L1 fibroblasts and 3T3-L1 adipocytes followed typical Michaelis-Menten kinetics; the apparent efficiency (k(cat)/K(T)) of this process increases over 2-fold (2.1 x 10(6)-4.5 x 10(6)s(-1)M(-1)) upon adipocyte differentiation. The V(max) values for fatty acid transport in Caco-2 and HepG2 cells were essentially the same, yet the efficiency was 55% higher in Caco-2 cells (2.3 x 10(6)s(-1)M(-1) versus 1.5 x 10(6)s(-1)M(-1)). The kinetic parameters for fatty acid transport in three endothelial cell types demonstrated they were the least efficient cell types for this process giving V(max) values that were nearly 4-fold lower than those defined form 3T3-L1 adipocytes, Caco-2 cells and HepG2 cells. The same cells had reduced efficiency for fatty acid transport (ranging from 0.82 x 10(6)s(-1)M(-1) to 1.35 x 10(6)s(-1)M(-1)).
    MeSH term(s) Animals ; Biological Transport, Active/physiology ; Fatty Acid-Binding Proteins/metabolism ; Fatty Acids/metabolism ; Gene Expression/physiology ; Humans ; Kinetics
    Chemical Substances Fatty Acid-Binding Proteins ; Fatty Acids ; Slc27a1 protein, rat
    Language English
    Publishing date 2008-09-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2008.06.010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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