LIVIVO - Das Suchportal für Lebenswissenschaften

switch to English language
Erweiterte Suche

Ihre letzten Suchen

  1. AU="Buitendijk, Maarten"
  2. AU="Vollmuth, Veronika"
  3. AU=Kobayashi Tetsuo
  4. AU="Grabauskas, Titas"
  5. AU=Sra Harnoor Kaur
  6. AU="Petra Macaskill"
  7. AU=Bramwell Edwin
  8. AU="Enríquez, Paula"
  9. AU="Uysal, Ismihan Ilknur"
  10. AU="Fernandes, Adriana Barrinha"
  11. AU="Goodwin, David G"
  12. AU="Hill, Jonathan C"
  13. AU="Chankasingh, Kyle"
  14. AU="Narayanasami, Uma"
  15. AU="Chen, Ruichao"
  16. AU=Li Xuefeng AU=Li Xuefeng
  17. AU="Stef J.F. Letteboer"
  18. AU="Gewurz, H"
  19. AU="Linares, Mauricio"
  20. AU="Gnesi, Marco"
  21. AU="Park, Jinny"
  22. AU="Hill, Benjamin D"
  23. AU=Huang Chunfa
  24. AU="Skonieczny, Paul"
  25. AU="LIVINGSTON, M S"
  26. AU="Lidia Gonzalez-Quereda"
  27. AU="Korkmaz, Asli"
  28. AU="Patel, Mrinal"
  29. AU="Louis Chauvel"
  30. AU="Jampen, Laurent"
  31. AU="Tan, Jiacheng"
  32. AU="Weiss, Jonathan D"

Suchergebnis

Treffer 1 - 6 von insgesamt 6

Suchoptionen

  1. Artikel ; Online: Is the kidney a major storage site for thyroxine as thyroxine glucuronide?

    Buitendijk, Maarten / Galton, Valerie Anne

    Thyroid : official journal of the American Thyroid Association

    2011  Band 22, Heft 2, Seite(n) 187–191

    Abstract: Background: Previous studies have shown that thyroxine (T4) is stored as T4 glucuronide (T4G) in the kidney, and that 24 hours after administration of [(125)I]T4 to mice, 17% of the radioactivity was present in the kidneys, whereas only 4% was found in ... ...

    Abstract Background: Previous studies have shown that thyroxine (T4) is stored as T4 glucuronide (T4G) in the kidney, and that 24 hours after administration of [(125)I]T4 to mice, 17% of the radioactivity was present in the kidneys, whereas only 4% was found in the liver. The present study was carried out to determine the relative amounts of conjugated and unconjugated T4 and 3,5,3'-triiodothyronine (T3) in the kidney and liver, and whether the conjugated hormones are extracted from tissues using our established extraction protocols, and detected in our radioimmunoassays (RIAs) for T4 and T3.
    Methods: Mice were injected with 10 μCi [(125)I]T4 or [(125)I]T3 and 24 hours later, the labeled compounds present in serum, kidney, liver, and urine were extracted and analyzed by paper chromatography before and after treatment with β-glucuronidase. In addition, the amounts of endogenous T4 and T3 in extracts of mouse kidney and liver were measured by RIA before and after treatment with β-glucuronidase.
    Results: After [(125)I]T4, more than 95% of the total kidney and liver radioactivity was extracted, and in the kidney, almost all of it was present in a conjugated form, mostly as T4G. The liver also contained T4G, but none was present in serum or urine. T3 glucuronide (T3G) was also found in the kidney and liver after the administration of [(125)I]T3. Analysis by RIA of the endogenous T4 content in extracts of kidney before and after hydrolysis by β-glucuronidase revealed that a substantial fraction of the T4 in both tissues was present as T4G, and the T4G was not detected in the RIA. Furthermore, the combined T4+T4G content in the kidney expressed per gram of tissue was significantly higher than that in the liver or serum. In contrast, the kidney content of T3+T3G was very low compared with that of T4+T4G.
    Conclusions: In summary, we have shown that the kidney stores a significant amount of T4 as T4G. Since T4G deconjugation can occur rapidly in the kidney, it is possible that this tissue participates in maintaining extrathyroidal serum T4 homeostasis.
    Mesh-Begriff(e) Animals ; Glucuronates/analysis ; Glucuronates/metabolism ; Glucuronidase/metabolism ; Kidney/chemistry ; Kidney/metabolism ; Liver/chemistry ; Mice ; Mice, Knockout ; Thyroxine/administration & dosage ; Thyroxine/analogs & derivatives ; Thyroxine/analysis ; Thyroxine/metabolism
    Chemische Substanzen Glucuronates ; thyroxine glucuronide (21462-56-6) ; Glucuronidase (EC 3.2.1.31) ; Thyroxine (Q51BO43MG4)
    Sprache Englisch
    Erscheinungsdatum 2011-12-16
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1086044-7
    ISSN 1557-9077 ; 1050-7256
    ISSN (online) 1557-9077
    ISSN 1050-7256
    DOI 10.1089/thy.2011.0307
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  2. Artikel ; Online: Toll-like receptor agonists are potent inhibitors of human immunodeficiency virus-type 1 replication in peripheral blood mononuclear cells.

    Buitendijk, Maarten / Eszterhas, Susan K / Howell, Alexandra L

    AIDS research and human retroviruses

    2014  Band 30, Heft 5, Seite(n) 457–467

    Abstract: Innate immune responses to microbial pathogens are initiated following the binding of ligand to specific pattern recognition receptors. Each pattern recognition receptor, which includes members of the Toll-like receptor (TLR) family, is specific for a ... ...

    Abstract Innate immune responses to microbial pathogens are initiated following the binding of ligand to specific pattern recognition receptors. Each pattern recognition receptor, which includes members of the Toll-like receptor (TLR) family, is specific for a particular type of pathogen associated molecular pattern ensuring that the organism can respond rapidly to a wide range of pathogens including bacteria, viruses, and fungi. We studied the extent to which agonists to endosomal TLR could induce anti-HIV-1 activity in peripheral blood mononuclear cells (PBMCs). When agonists to TLR3, TLR7, TLR8 and TLR9 were added prior to infection with HIV-1, they significantly reduced infection of peripheral blood mononuclear cells. Interestingly, agonists to TLR8 and TLR9 were highly effective at blocking HIV replication even when added as late as 48 h or 72 h, respectively, after HIV-1 infection, indicating that the anti-viral effect was durable and long lasting. Analysis of the induction of anti-viral genes after agonist activation of TLR indicated that all of the agonists induced expression of the type I interferons and interferon stimulated genes, although to variable levels that depended on the agonist used. Interestingly, only the agonist to TLR9, ODN2395 DNA, induced expression of type II interferon and the anti-HIV proteins Apobec3G and SAMHD1. By blocking TLR activity using an inhibitor to the MyD88 adaptor protein, we demonstrated that, at least for TLR8 and TLR9, the anti-HIV activity was not entirely mediated by TLR activation, but likely by the activation of additional anti-viral sensors in HIV target cells. These findings suggest that agonists to the endosomal TLR function to induce expression of anti-HIV molecules by both TLR-mediated and non-TLR-mediated mechanisms. Moreover, the non-TLR-mediated mechanisms induced by these agonists could potentially be exploited to block HIV-1 replication in recently HIV-exposed individuals.
    Mesh-Begriff(e) Adult ; Female ; Gene Expression Profiling ; HIV-1/physiology ; Humans ; Immunity, Innate ; Leukocytes, Mononuclear/drug effects ; Leukocytes, Mononuclear/immunology ; Leukocytes, Mononuclear/virology ; Male ; Middle Aged ; Toll-Like Receptors/agonists ; Virus Replication ; Young Adult
    Chemische Substanzen Toll-Like Receptors
    Sprache Englisch
    Erscheinungsdatum 2014-05
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 639130-8
    ISSN 1931-8405 ; 0889-2229
    ISSN (online) 1931-8405
    ISSN 0889-2229
    DOI 10.1089/AID.2013.0199
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  3. Artikel ; Online: Gardiquimod: a Toll-like receptor-7 agonist that inhibits HIV type 1 infection of human macrophages and activated T cells.

    Buitendijk, Maarten / Eszterhas, Susan K / Howell, Alexandra L

    AIDS research and human retroviruses

    2013  Band 29, Heft 6, Seite(n) 907–918

    Abstract: Immune response modifiers are being studied as therapeutic agents for viral infections and cancer. These molecules include agonists for the Toll-like receptors (TLR), a family of innate immune receptors. TLR7 and 8, located in cellular endosomes, bind ... ...

    Abstract Immune response modifiers are being studied as therapeutic agents for viral infections and cancer. These molecules include agonists for the Toll-like receptors (TLR), a family of innate immune receptors. TLR7 and 8, located in cellular endosomes, bind single-stranded RNA characteristic of viral genomes, and trigger intracellular signaling pathways that induce inflammatory cytokines and antiviral innate immune factors. We studied the anti-HIV-1 effects of gardiquimod, a specific TLR7 agonist when used at concentrations below 10 μM, in macrophages and activated peripheral blood mononuclear cells (PBMCs). Gardiquimod, added prior to or within 2 days after infection with X4, R5, or dual-tropic (R5/X4) strains of HIV-1, significantly reduced infection in these cells. Cocultures of activated PBMCs added to gardiquimod-treated and HIV-1-exposed macrophages demonstrated minimal HIV-1 replication for up to 10 days, suggesting that gardiquimod inhibited activated PBMCs viral amplification from HIV-1-exposed macrophages. Gardiquimod treatment of both activated PBMCs and macrophages induced interferon-alpha (IFN-α) transcription within hours of addition, and sustained IFN-α protein secretion for several days. Treatment of cells with a peptide inhibitor to the MyD88 adaptor protein blocked the induction of IFN-α by gardiquimod, and partially reversed the anti-HIV effects in activated PBMCs. Blocking the IFN-α receptor with a neutralizing antibody also reduced the anti-HIV effect of gardiquimod. Gardiquimod inhibited HIV-1 reverse transcriptase, an early step in the life cycle of HIV-1. These findings suggest that gardiquimod, functioning as both an immune system modifier and a reverse transcriptase inhibitor, could be developed as a novel therapeutic agent to block systemic and mucosal transmission of HIV-1.
    Mesh-Begriff(e) Aminoquinolines/therapeutic use ; Anti-HIV Agents/therapeutic use ; Cell Line ; DNA, Viral/genetics ; HIV Infections/drug therapy ; HIV-1/drug effects ; HIV-1/physiology ; Humans ; Imidazoles/therapeutic use ; Interferon-alpha/biosynthesis ; Leukocytes, Mononuclear/drug effects ; Leukocytes, Mononuclear/virology ; Macrophages/drug effects ; Macrophages/virology ; Real-Time Polymerase Chain Reaction ; T-Lymphocytes/drug effects ; T-Lymphocytes/virology ; Toll-Like Receptor 7/agonists ; Virus Replication/drug effects
    Chemische Substanzen Aminoquinolines ; Anti-HIV Agents ; DNA, Viral ; Imidazoles ; Interferon-alpha ; Toll-Like Receptor 7 ; gardiquimod
    Sprache Englisch
    Erscheinungsdatum 2013-02-05
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 639130-8
    ISSN 1931-8405 ; 0889-2229
    ISSN (online) 1931-8405
    ISSN 0889-2229
    DOI 10.1089/AID.2012.0313
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  4. Artikel ; Online: Antiangiogenic activity of rPAI-1(23) promotes vasa vasorum regression in hypercholesterolemic mice through a plasmin-dependent mechanism.

    Mollmark, Jessica / Ravi, Saranya / Sun, Baiming / Shipman, Samantha / Buitendijk, Maarten / Simons, Michael / Mulligan-Kehoe, Mary Jo

    Circulation research

    2011  Band 108, Heft 12, Seite(n) 1419–1428

    Abstract: Rationale: The antiangiogenic activity of rPAI-1(23), a truncated plasminogen activator inhibitor-1 (PAI-1) protein, induces vasa vasorum collapse and significantly reduces plaque area and plaque cholesterol in hypercholesterolemic low-density ... ...

    Abstract Rationale: The antiangiogenic activity of rPAI-1(23), a truncated plasminogen activator inhibitor-1 (PAI-1) protein, induces vasa vasorum collapse and significantly reduces plaque area and plaque cholesterol in hypercholesterolemic low-density lipoprotein receptor-deficient/apolipoprotein B48-deficient mice.
    Objective: The objective of this study was to examine rPAI-1(23)-stimulated mechanisms that cause vasa vasorum collapse.
    Methods and results: The rPAI-1(23) protein opposed PAI-1 antiproteolytic function by stimulating a 1.6-fold increase in plasmin activity compared with the saline-treated counterpart. The increased proteolytic activity corresponded to increased activity of matrix metalloproteinase-3 and degradation of fibrin(ogen), nidogen, and perlecan in the adventitia of descending aortas. PAI-1 activity was reduced by 48% in response to rPAI-1(23); however, PAI-1 protein expression levels were similar in the rPAI-1(23)- and saline-treated hypercholesterolemic mice. Coimmunoprecipitation assays demonstrated a novel PAI-1-plasminogen complex in protein from the descending aorta of rPAI-1(23)- and saline-treated mice, but complexed PAI-1 was 1.6-fold greater in rPAI-1(23)-treated mice. Biochemical analyses demonstrated that rPAI-1(23) and PAI-1 binding interactions with plasminogen increased plasmin activity and reduced PAI-1 antiproteolytic activity.
    Conclusions: We conclude that rPAI-1(23) causes regression or collapse of adventitial vasa vasorum in hypercholesterolemic mice by stimulating an increase in plasmin activity. The rPAI-1(23)-enhanced plasmin activity was achieved through a novel mechanism by which rPAI-1(23) and PAI-1 bound plasminogen in a cooperative manner to increase plasmin activity and reduce PAI-1 activity.
    Mesh-Begriff(e) Angiogenesis Inhibitors/pharmacology ; Animals ; Fibrinolysin/genetics ; Fibrinolysin/metabolism ; Hypercholesterolemia/genetics ; Hypercholesterolemia/metabolism ; Hypercholesterolemia/pathology ; Mice ; Mice, Knockout ; Plasminogen/genetics ; Plasminogen/metabolism ; Serpin E2/pharmacology ; Vasa Vasorum/metabolism ; Vasa Vasorum/pathology
    Chemische Substanzen Angiogenesis Inhibitors ; Serpin E2 ; Serpine2 protein, mouse ; Plasminogen (9001-91-6) ; Fibrinolysin (EC 3.4.21.7)
    Sprache Englisch
    Erscheinungsdatum 2011-05-05
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 80100-8
    ISSN 1524-4571 ; 0009-7330 ; 0931-6876
    ISSN (online) 1524-4571
    ISSN 0009-7330 ; 0931-6876
    DOI 10.1161/CIRCRESAHA.111.246249
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  5. Artikel ; Online: The diaphragms of fenestrated endothelia: gatekeepers of vascular permeability and blood composition.

    Stan, Radu V / Tse, Dan / Deharvengt, Sophie J / Smits, Nicole C / Xu, Yan / Luciano, Marcus R / McGarry, Caitlin L / Buitendijk, Maarten / Nemani, Krishnamurthy V / Elgueta, Raul / Kobayashi, Takashi / Shipman, Samantha L / Moodie, Karen L / Daghlian, Charles P / Ernst, Patricia A / Lee, Hong-Kee / Suriawinata, Arief A / Schned, Alan R / Longnecker, Daniel S /
    Fiering, Steven N / Noelle, Randolph J / Gimi, Barjor / Shworak, Nicholas W / Carrière, Catherine

    Developmental cell

    2017  Band 23, Heft 6, Seite(n) 1203–1218

    Abstract: Fenestral and stomatal diaphragms are endothelial subcellular structures of unknown function that form on organelles implicated in vascular permeability: fenestrae, transendothelial channels, and caveolae. PV1 protein is required for diaphragm formation ... ...

    Abstract Fenestral and stomatal diaphragms are endothelial subcellular structures of unknown function that form on organelles implicated in vascular permeability: fenestrae, transendothelial channels, and caveolae. PV1 protein is required for diaphragm formation in vitro. Here, we report that deletion of the PV1-encoding Plvap gene in mice results in the absence of diaphragms and decreased survival. Loss of diaphragms did not affect the fenestrae and transendothelial channels formation but disrupted the barrier function of fenestrated capillaries, causing a major leak of plasma proteins. This disruption results in early death of animals due to severe noninflammatory protein-losing enteropathy. Deletion of PV1 in endothelium, but not in the hematopoietic compartment, recapitulates the phenotype of global PV1 deletion, whereas endothelial reconstitution of PV1 rescues the phenotype. Taken together, these data provide genetic evidence for the critical role of the diaphragms in fenestrated capillaries in the maintenance of blood composition.
    Mesh-Begriff(e) Animals ; Blood Proteins/metabolism ; Capillaries/physiology ; Capillaries/ultrastructure ; Capillary Permeability ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Caveolae/physiology ; Cell Membrane/metabolism ; Endothelium, Vascular/cytology ; Endothelium, Vascular/physiology ; Endothelium, Vascular/ultrastructure ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Mice, Transgenic ; Protein-Losing Enteropathies/physiopathology
    Chemische Substanzen Blood Proteins ; Carrier Proteins ; Membrane Proteins ; Plvap protein, mouse
    Sprache Englisch
    Erscheinungsdatum 2017-03-16
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2012.11.003
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  6. Artikel: The Diaphragms of Fenestrated Endothelia: Gatekeepers of Vascular Permeability and Blood Composition

    Stan, Radu V / Tse, Dan / Deharvengt, Sophie J / Smits, Nicole C / Xu, Yan / Luciano, Marcus R / McGarry, Caitlin L / Buitendijk, Maarten / Nemani, Krishnamurthy V / Elgueta, Raul / Kobayashi, Takashi / Shipman, Samantha L / Moodie, Karen L / Daghlian, Charles P / Ernst, Patricia A / Lee, Hong-Kee / Suriawinata, Arief A / Schned, Alan R / Longnecker, Daniel S /
    Fiering, Steven N / Noelle, Randolph J / Gimi, Barjor / Shworak, Nicholas W / Carrière, Catherine

    Developmental cell. 2012 Dec. 11, v. 23, no. 6

    2012  

    Abstract: Fenestral and stomatal diaphragms are endothelial subcellular structures of unknown function that form on organelles implicated in vascular permeability: fenestrae, transendothelial channels, and caveolae. PV1 protein is required for diaphragm formation ... ...

    Abstract Fenestral and stomatal diaphragms are endothelial subcellular structures of unknown function that form on organelles implicated in vascular permeability: fenestrae, transendothelial channels, and caveolae. PV1 protein is required for diaphragm formation in vitro. Here, we report that deletion of the PV1-encoding Plvap gene in mice results in the absence of diaphragms and decreased survival. Loss of diaphragms did not affect the fenestrae and transendothelial channels formation but disrupted the barrier function of fenestrated capillaries, causing a major leak of plasma proteins. This disruption results in early death of animals due to severe noninflammatory protein-losing enteropathy. Deletion of PV1 in endothelium, but not in the hematopoietic compartment, recapitulates the phenotype of global PV1 deletion, whereas endothelial reconstitution of PV1 rescues the phenotype. Taken together, these data provide genetic evidence for the critical role of the diaphragms in fenestrated capillaries in the maintenance of blood composition.
    Schlagwörter blood proteins ; death ; diaphragm ; digestive system diseases ; endothelium ; genes ; mice ; organelles ; permeability ; phenotype
    Sprache Englisch
    Erscheinungsverlauf 2012-1211
    Umfang p. 1203-1218.
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2012.11.003
    Datenquelle NAL Katalog (AGRICOLA)

    Zusatzmaterialien

    Kategorien

Zum Seitenanfang