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  • 1
    Online Resource
    Online Resource
    Abstract
    Springer Science and Business Media LLC ; 1992
    In:  Annals of Hematology Vol. 65, No. S1 ( 1992-1), p. A1-A146
    Details
    In: Annals of Hematology, Springer Science and Business Media LLC, Vol. 65, No. S1 ( 1992-1), p. A1-A146
    Type of Medium: Online Resource
    ISSN: 0939-5555 , 1432-0584
    URL: Article
    DOI: 10.1007/BF02044602
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 1992
    detail.hit.zdb_id: 1458429-3
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  • 2
    Online Resource
    Online Resource
    Rotavirus NSP4: Cell type-dependent transport kinetics to the exofacial plasma membrane and release from intact infected cells
    Springer Science and Business Media LLC ; 2011
    In:  Virology Journal Vol. 8, No. 1 ( 2011-12)
    Details
    In: Virology Journal, Springer Science and Business Media LLC, Vol. 8, No. 1 ( 2011-12)
    Abstract: Rotavirus NSP4 localizes to multiple intracellular sites and is multifunctional, contributing to RV morphogenesis, replication and pathogenesis. One function of NSP4 is the induction of early secretory diarrhea by binding surface receptors to initiate signaling events. The aims of this study were to determine the transport kinetics of NSP4 to the exofacial plasma membrane (PM), the subsequent release from intact infected cells, and rebinding to naïve and/or neighboring cells in two cell types. Methods Transport kinetics was evaluated using surface-specific biotinylation/streptavidin pull-downs and exofacial exposure of NSP4 was confirmed by antibody binding to intact cells, and fluorescent resonant energy transfer. Transfected cells similarly were monitored to discern NSP4 movement in the absence of infection or other viral proteins. Endoglycosidase H digestions, preparation of CY3- or CY5- labeled F(ab) 2 fragments, confocal imaging, and determination of preferential polarized transport employed standard laboratory techniques. Mock-infected, mock-biotinylated and non-specific antibodies served as controls. Results Only full-length (FL), endoglycosidase-sensitive NSP4 was detected on the exofacial surface of two cell types, whereas the corresponding cell lysates showed multiple glycosylated forms. The C-terminus of FL NSP4 was detected on exofacial-membrane surfaces at different times in different cell types prior to its release into culture media. Transport to the PM was rapid and distinct yet FL NSP4 was secreted from both cell types at a time similar to the release of virus. NSP4-containing, clarified media from both cells bound surface molecules of naïve cells, and imaging showed secreted NSP4 from one or more infected cells bound neighboring cell membranes in culture. Preferential sorting to apical or basolateral membranes also was distinct in different polarized cells. Conclusions The intracellular transport of NSP4 to the PM, translocation across the PM, exposure of the C-terminus on the cell surface and subsequent secretion occurs via an unusual, complex and likely cell-dependent process. The exofacial exposure of the C-terminus poses several questions and suggests an atypical mechanism by which NSP4 traverses the PM and interacts with membrane lipids. Mechanistic details of the unconventional trafficking of NSP4, interactions with host-cell specific molecules and subsequent release require additional study.
    Type of Medium: Online Resource
    ISSN: 1743-422X
    URL: Article
    DOI: 10.1186/1743-422X-8-278
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2011
    detail.hit.zdb_id: 2160640-7
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  • 3
    Online Resource
    Online Resource
    Elucidation of the Rotavirus NSP4-Caveolin-1 and -Cholesterol Interactions Using Synthetic Peptides
    Hindawi Limited ; 2012
    In:  Journal of Amino Acids Vol. 2012 ( 2012-03-01), p. 1-16
    Details
    In: Journal of Amino Acids, Hindawi Limited, Vol. 2012 ( 2012-03-01), p. 1-16
    Abstract: Rotavirus (RV) NSP4, the first described viral enterotoxin, is a multifunctional glycoprotein that contributes to viral pathogenesis, morphogenesis, and replication. NSP4 binds both termini of caveolin-1 and is isolated from caveolae fractions that are rich in anionic phospholipids and cholesterol. These interactions indicate that cholesterol/caveolin-1 plays a role in NSP4 transport to the cell surface, which is essential to its enterotoxic activity. Synthetic peptides were utilized to identify target(s) of intervention by exploring the NSP4-caveolin-1 and -cholesterol interactions. NSP4 112–140 that overlaps the caveolin-1 binding domain and a cholesterol recognition amino acid consensus (CRAC) motif and both termini of caveolin-1 (N-caveolin-1 2–20 ,   19–40 and C-caveolin-1 161–180 ) were synthesized. Direct fluorescence-binding assays were employed to determine binding affinities of the NSP4-caveolin-1 peptides and cholesterol. Intracellular cholesterol alteration revealed a redistribution of NSP4 and disintegration of viroplasms. These data further imply interruption of NSP4 112–140 -N-caveolin-1 19–40 and cholesterol interactions may block NSP4 intracellular transport, hence enterotoxicity.
    Type of Medium: Online Resource
    ISSN: 2090-0104 , 2090-0112
    URL: Article
    DOI: 10.1155/2012/575180
    Language: English
    Publisher: Hindawi Limited
    Publication Date: 2012
    detail.hit.zdb_id: 2573907-4
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  • 4
    Online Resource
    Online Resource
    A New N-Terminal Recognition Domain in Caveolin-1 Interacts with Sterol Carrier Protein-2 (SCP-2)
    American Chemical Society (ACS) ; 2007
    In:  Biochemistry Vol. 46, No. 28 ( 2007-07-01), p. 8301-8314
    Details
    In: Biochemistry, American Chemical Society (ACS), Vol. 46, No. 28 ( 2007-07-01), p. 8301-8314
    Type of Medium: Online Resource
    ISSN: 0006-2960 , 1520-4995
    URL: Article
    DOI: 10.1021/bi7002636
    RVK:
    WA 15000
    Language: English
    Publisher: American Chemical Society (ACS)
    Publication Date: 2007
    detail.hit.zdb_id: 1472258-6
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    Mutational analysis of the rotavirus NSP4 enterotoxic domain that binds to caveolin-1
    Springer Science and Business Media LLC ; 2013
    In:  Virology Journal Vol. 10, No. 1 ( 2013-12)
    Details
    In: Virology Journal, Springer Science and Business Media LLC, Vol. 10, No. 1 ( 2013-12)
    Abstract: Rotavirus (RV) nonstructural protein 4 (NSP4) is the first described viral enterotoxin, which induces early secretory diarrhea in neonatal rodents. Our previous data show a direct interaction between RV NSP4 and the structural protein of caveolae, caveolin-1 (cav-1), in yeast and mammalian cells. The binding site of cav-1 mapped to the NSP4 amphipathic helix, and led us to examine which helical face was responsible for the interaction. Methods A panel of NSP4 mutants were prepared and tested for binding to cav-1 by yeast two hybrid and direct binding assays. The charged residues of the NSP4 amphipathic helix were changed to alanine (NSP4 46-175 -ala6); and three residues in the hydrophobic face were altered to charged amino acids (NSP4 46-175 -HydroMut). In total, twelve mutants of NSP4 were generated to define the cav-1 binding site. Synthetic peptides corresponding to the hydrophobic and charged faces of NSP4 were examined for structural changes by circular dichroism (CD) and diarrhea induction by a neonatal mouse study. Results Mutations of the hydrophilic face (NSP4 46-175 -Ala6) bound cav-1 akin to wild type NSP4. In contrast, disruption of the hydrophobic face (NSP4 46-175 -HydroMut) failed to bind cav-1. These data suggest NSP4 and cav-1 associate via a hydrophobic interaction. Analyses of mutant synthetic peptides in which the hydrophobic residues in the enterotoxic domain of NSP4 were altered suggested a critical hydrophobic residue. Both NSP4 HydroMut112-140, that contains three charged amino acids (aa113, 124, 131) changed from the original hydrophobic residues and NSP4 AlaAcidic112-140 that contained three alanine residues substituted for negatively charged (aa114, 125, 132) amino acids failed to induce diarrhea. Whereas peptides NSP4wild type 112 −140 and NSP4 AlaBasic112-140 that contained three alanine substituted for positively charged (aa115, 119, 133) amino acids, induced diarrhea. Conclusions These data show that the cav-1 binding domain is within the hydrophobic face of the NSP4 amphipathic helix. The integrity of the helical structure is important for both cav-1 binding and diarrhea induction implying a connection between NSP4 functional and binding activities.
    Type of Medium: Online Resource
    ISSN: 1743-422X
    URL: Article
    DOI: 10.1186/1743-422X-10-336
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2013
    detail.hit.zdb_id: 2160640-7
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  • 6
    Online Resource
    Online Resource
    Sterol carrier protein-2 expression alters sphingolipid metabolism in transfected mouse L-cell fibroblasts
    Springer Science and Business Media LLC ; 2006
    In:  Molecular and Cellular Biochemistry Vol. 283, No. 1-2 ( 2006-2), p. 57-66
    Details
    In: Molecular and Cellular Biochemistry, Springer Science and Business Media LLC, Vol. 283, No. 1-2 ( 2006-2), p. 57-66
    Type of Medium: Online Resource
    ISSN: 0300-8177 , 1573-4919
    URL: Article
    DOI: 10.1007/s11010-006-2270-1
    RVK:
    WD 5725
    RVK:
    WD 5275
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2006
    detail.hit.zdb_id: 2003615-2
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Acyl-CoA binding proteins interact with the acyl-CoA binding domain of mitochondrial carnitine palmitoyl transferase I
    Springer Science and Business Media LLC ; 2011
    In:  Molecular and Cellular Biochemistry Vol. 355, No. 1-2 ( 2011-9), p. 135-148
    Details
    In: Molecular and Cellular Biochemistry, Springer Science and Business Media LLC, Vol. 355, No. 1-2 ( 2011-9), p. 135-148
    Type of Medium: Online Resource
    ISSN: 0300-8177 , 1573-4919
    URL: Article
    DOI: 10.1007/s11010-011-0847-9
    RVK:
    WD 5725
    RVK:
    WD 5275
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2011
    detail.hit.zdb_id: 2003615-2
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    Adrenergic regulation of fat-cell lipolysis in multiple symmetric lipomatosis
    Wiley ; 1982
    In:  European Journal of Clinical Investigation Vol. 12, No. 6 ( 1982-12), p. 471-474
    Details
    In: European Journal of Clinical Investigation, Wiley, Vol. 12, No. 6 ( 1982-12), p. 471-474
    Type of Medium: Online Resource
    ISSN: 0014-2972 , 1365-2362
    URL: Article
    DOI: 10.1111/j.1365-2362.1982.tb02227.x
    Language: English
    Publisher: Wiley
    Publication Date: 1982
    detail.hit.zdb_id: 2004971-7
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  • 9
    Online Resource
    Online Resource
    Calcium Modulates Fatty Acid Dynamics in Rat Liver Plasma Membranes
    Wiley ; 1983
    In:  European Journal of Biochemistry Vol. 132, No. 3 ( 1983-05), p. 517-524
    Details
    In: European Journal of Biochemistry, Wiley, Vol. 132, No. 3 ( 1983-05), p. 517-524
    Abstract: Modulation of free fatty acid binding in isolated rat liver plasma membrances was evaluated using the fluorecent fatty acids trans ‐parinaric and cis ‐parinaric acid as analogues for saturated and unsaturated fatty acids, respectigvely. Binding of trans ‐parinarate but not cis ‐parinarate was inhibited by physiological levels of Ca 2+ . The effect was revedrsed by addition of excess EGTA. Calcium decreased the aqueous to lipid partition coefficient, K p , of trans ‐parinaric acid for liver plasma membrances while increasing the K p for trans ‐parinaric acid. In addition, Ca 2+ also altered the fluorescence lifetime, the quantum yield, and the relative partitioning of trans ‐parinaric and cis ‐parinaric acid into fluid and solid phases. Calcium and EGTA did not affect the binding of 1, 6‐diphenyl‐1,3,5‐hexatriene. The effect of Ca 2+ on the liver plasma membrane structure was to increase the rigidity of the membrane, primarily the solid domain. The fluorescence polarization of trans ‐parinarate, cis ‐parinarate, and 1,6‐diphenyl‐1,3,5‐hexatriene at 24°C in liver plasma membranes in the absence of Ca 2+ was 0.295 ± 0.008, 0.253 ± 0.007, and 0.284 ± 0.005, respectively. Calcium (2.4 mM) increased the polarization of these probe molecules in liver plasma membrances by 8–10%. EGTA (3.4 mM) reversed or abolished the increase in polarization. Thus, the fluorescent fatty acids trans ‐parinarate and cis ‐parinarate may be used to monitor fatty acid binding by isolated membranes, to evaluate factors such as Ca 2+ which modulate fatty acid binding, and to investigate the microenvironemtn in which the fatty acids reside. The data suggest that Ca 2+ may be an important regulator of fatty acid uptake by the liver plasma membrane, and therby interact with intermediary metabolism of lipids at a step not involging lipolytic or synthetic enzymes.
    Type of Medium: Online Resource
    ISSN: 0014-2956 , 1432-1033
    URL: Issue
    URL: Article
    DOI: 10.1111/ejb.1983.132.issue-3
    DOI: 10.1111/j.1432-1033.1983.tb07392.x
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1983
    detail.hit.zdb_id: 1398347-7
    detail.hit.zdb_id: 2172518-4
    SSG: 12
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  • 10
    Online Resource
    Online Resource
    Liver fatty-acid-binding protein (L-FABP) gene ablation alters liver bile acid metabolism in male mice
    Portland Press Ltd. ; 2005
    In:  Biochemical Journal Vol. 391, No. 3 ( 2005-11-01), p. 549-560
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 391, No. 3 ( 2005-11-01), p. 549-560
    Abstract: Although the physiological roles of the individual bile acid synthetic enzymes have been extensively examined, relatively little is known regarding the function of intracellular bile acid-binding proteins. Male L-FABP (liver fatty-acid-binding protein) gene-ablated mice were used to determine a role for L-FABP, the major liver bile acid-binding protein, in bile acid and biliary cholesterol metabolism. First, in control-fed mice L-FABP gene ablation alone increased the total bile acid pool size by 1.5-fold, especially in gall-bladder and liver, but without altering the proportions of bile acid, cholesterol and phospholipid. Loss of liver L-FABP was more than compensated by up-regulation of: other liver cytosolic bile acid-binding proteins [GST (glutathione S-transferase), 3α-HSD (3α-hydroxysteroid dehydrogenase)], key hepatic bile acid synthetic enzymes [CYP7A1 (cholesterol 7α-hydroxylase) and CYP27A1 (sterol 27α-hydroxylase)] , membrane bile acid translocases [canalicular BSEP (bile salt export pump), canalicular MRP2 (multidrug resistance associated protein 2), and basolateral/serosal OATP-1 (organic anion transporting polypeptide 1)], and positive alterations in nuclear receptors [more LXRα (liver X receptor α) and less SHP (short heterodimer partner)] . Secondly, L-FABP gene ablation reversed the cholesterol-responsiveness of bile acid metabolic parameters such that total bile acid pool size, especially in gall-bladder and liver, was reduced 4-fold, while the mass of biliary cholesterol increased 1.9-fold. The dramatically reduced bile acid levels in cholesterol-fed male L-FABP (−/−) mice were associated with reduced expression of: (i) liver cytosolic bile acid-binding proteins (L-FABP, GST and 3α-HSD), (ii) hepatic bile acid synthetic enzymes [CYP7A1, CYP27A1 and SCP-x (sterol carrier protein-x/3-ketoacyl-CoA thiolase)] concomitant with decreased positive nuclear receptor alterations (i.e. less LXRα and more SHP), and (iii) membrane bile acid transporters (BSEP, MRP2 and OATP-1). These are the first results suggesting a physiological role for the major cytosolic bile acid-binding protein (L-FABP) in influencing liver bile metabolic phenotype and gall-bladder bile lipids of male mice, especially in response to dietary cholesterol.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/BJ20050296
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 2005
    detail.hit.zdb_id: 1473095-9
    SSG: 12
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