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  1. Article: Live oral poliovirus vaccines and simian cytomegalovirus.

    Sierra-Honigmann, Ana M / Krause, Philip R

    Biologicals : journal of the International Association of Biological Standardization

    2002  Volume 30, Issue 3, Page(s) 167–174

    Abstract: Live oral poliovirus vaccines (OPV) are often produced in primary Cercopithecus monkey kidney (CMK) cells. The kidneys of these monkeys are often latently infected with simian cytomegalovirus (SCMV), and CMK cultures are frequently contaminated with SCMV. ...

    Abstract Live oral poliovirus vaccines (OPV) are often produced in primary Cercopithecus monkey kidney (CMK) cells. The kidneys of these monkeys are often latently infected with simian cytomegalovirus (SCMV), and CMK cultures are frequently contaminated with SCMV. We tested human, monkey and rabbit tissue culture systems, and found that MRC-5 cells are most sensitive for detection of SCMV. To address the question of whether OPV could be contaminated with infectious SCMV, we inoculated MRC-5 cells with neutralized OPV manufactured in the United States between 1972 and 1998. Infectious SCMV was not found in any of the vaccine lots tested. We also used the polymerase chain reaction (PCR) to search for SCMV DNA in live oral poliovirus vaccines; SCMV DNA sequences were found in several of the vaccine lots manufactured prior to 1992.
    MeSH term(s) Animals ; Base Sequence ; Cell Line ; Cercopithecus ; Culture Techniques ; Cytomegalovirus/genetics ; Cytomegalovirus/isolation & purification ; Cytomegalovirus/pathogenicity ; DNA, Viral/genetics ; DNA, Viral/isolation & purification ; Drug Contamination ; Humans ; Poliovirus Vaccine, Oral/adverse effects ; Poliovirus Vaccine, Oral/isolation & purification ; Polymerase Chain Reaction/statistics & numerical data ; Rabbits ; Sensitivity and Specificity
    Chemical Substances DNA, Viral ; Poliovirus Vaccine, Oral
    Language English
    Publishing date 2002-09-08
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1017370-5
    ISSN 1095-8320 ; 1045-1056
    ISSN (online) 1095-8320
    ISSN 1045-1056
    DOI 10.1006/biol.2002.0325
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 879: Show issues Location:
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  2. Article ; Online: Leptin affects endocardial cushion formation by modulating EMT and migration via Akt signaling cascades.

    Nath, Anjali K / Brown, Rachel M / Michaud, Michael / Sierra-Honigmann, M Rocio / Snyder, Michael / Madri, Joseph A

    The Journal of cell biology

    2008  Volume 181, Issue 2, Page(s) 367–380

    Abstract: Blood circulation is dependent on heart valves to direct blood flow through the heart and great vessels. Valve development relies on epithelial to mesenchymal transition (EMT), a central feature of embryonic development and metastatic cancer. Abnormal ... ...

    Abstract Blood circulation is dependent on heart valves to direct blood flow through the heart and great vessels. Valve development relies on epithelial to mesenchymal transition (EMT), a central feature of embryonic development and metastatic cancer. Abnormal EMT and remodeling contribute to the etiology of several congenital heart defects. Leptin and its receptor were detected in the mouse embryonic heart. Using an ex vivo model of cardiac EMT, the inhibition of leptin results in a signal transducer and activator of transcription 3 and Snail/vascular endothelial cadherin-independent decrease in EMT and migration. Our data suggest that an Akt signaling pathway underlies the observed phenotype. Furthermore, loss of leptin phenocopied the functional inhibition of alphavbeta3 integrin receptor and resulted in decreased alphavbeta3 integrin and matrix metalloprotease 2, suggesting that the leptin signaling pathway is involved in adhesion and migration processes. This study adds leptin to the repertoire of factors that mediate EMT and, for the first time, demonstrates a role for the interleukin 6 family in embryonic EMT.
    MeSH term(s) Animals ; Cell Movement ; Embryo, Mammalian ; Endocardial Cushions/physiology ; Epithelium/physiology ; Female ; Leptin/physiology ; Mesoderm/cytology ; Mesoderm/physiology ; Mice ; Mice, Inbred Strains ; Pregnancy ; Proto-Oncogene Proteins c-akt/physiology ; Signal Transduction/physiology
    Chemical Substances Leptin ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
    Language English
    Publishing date 2008-04-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.200708197
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: A method of isolation and culture of microvascular endothelial cells from mouse skin.

    Cha, Sung Tae / Talavera, Dodanim / Demir, Erhan / Nath, Anjali K / Sierra-Honigmann, M Rocio

    Microvascular research

    2005  Volume 70, Issue 3, Page(s) 198–204

    Abstract: Objectives: The study of isolated microvascular endothelial cells from mice has long been impeded due to the many difficulties encountered in isolating and culturing these cells. We focused on developing a method to isolate microvascular endothelial ... ...

    Abstract Objectives: The study of isolated microvascular endothelial cells from mice has long been impeded due to the many difficulties encountered in isolating and culturing these cells. We focused on developing a method to isolate microvascular endothelial cells from the skin fragments of newborn mice. We also aimed at establishing optimal culture conditions to sustain the growth of these cells.
    Methods and results: Isolation of murine dermal microvascular endothelial cells (mDMEC) from P3 newborn mice was based first on enzymatic separation of the skin epidermal layer from the dermis using dispase and then on disaggregating dermal cellular elements using collagenase. The cells obtained from the dermis were subjected to a continuous density gradient centrifugation. Cells situated between densities 1.033 and 1.047 were then cultured on collagen IV-coated culture flasks using optimized growth culture conditions. Cells were characterized by endothelial appearance and by the presence and genetic expression of endothelial markers like CD31, NOS3, VEGFR-2 and Tie-2. Uptake of acetylated low-density lipoprotein (Ac-LDL) was used as a functional assay.
    Conclusions: The methodology described herein for isolation and culture of murine microvascular endothelium offers a distinctive advantage for those using mouse models to study endothelial cell biology.
    MeSH term(s) Animals ; Antigens, CD ; Antigens, CD34/biosynthesis ; Cadherins/biosynthesis ; Cell Culture Techniques/methods ; Cells, Cultured ; Endothelial Cells/metabolism ; Endothelium, Vascular/cytology ; Endothelium, Vascular/metabolism ; Endothelium, Vascular/pathology ; Flow Cytometry ; Gene Expression Regulation ; Lipoproteins, LDL/metabolism ; Mice ; Microcirculation ; Microscopy, Fluorescence ; Microscopy, Phase-Contrast ; Models, Biological ; Phenotype ; Platelet Endothelial Cell Adhesion Molecule-1/biosynthesis ; RNA, Messenger/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Skin/metabolism ; Skin/pathology ; Vascular Endothelial Growth Factor Receptor-2/metabolism
    Chemical Substances Antigens, CD ; Antigens, CD34 ; Cadherins ; Lipoproteins, LDL ; Platelet Endothelial Cell Adhesion Molecule-1 ; RNA, Messenger ; cadherin 5 ; Vascular Endothelial Growth Factor Receptor-2 (EC 2.7.10.1)
    Language English
    Publishing date 2005-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80307-8
    ISSN 1095-9319 ; 0026-2862
    ISSN (online) 1095-9319
    ISSN 0026-2862
    DOI 10.1016/j.mvr.2005.08.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 746: Show issues Location:
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  4. Article: Simian cytomegalovirus encodes five rapidly evolving chemokine receptor homologues.

    Sahagun-Ruiz, Alfredo / Sierra-Honigmann, Ana Maria / Krause, Philip / Murphy, Philip M

    Virus genes

    2004  Volume 28, Issue 1, Page(s) 71–83

    Abstract: Many herpesviruses, poxviruses and retroviruses encode proteins related to chemokines and chemokine receptors. The first one discovered, US28 of human cytomegalovirus (HCMV), is a 7-transmembrane domain G protein-coupled chemokine receptor able to ... ...

    Abstract Many herpesviruses, poxviruses and retroviruses encode proteins related to chemokines and chemokine receptors. The first one discovered, US28 of human cytomegalovirus (HCMV), is a 7-transmembrane domain G protein-coupled chemokine receptor able to activate diverse cellular responses, including cell migration and gene expression. A related ORF named US27 is adjacent to US28, but no functions have been defined yet. Recently ORFs 3-7, a cluster of five concatenated ORFs with highest homology to US28 and mammalian chemokine receptors, were sequenced from a prototype "stealth virus", an African green monkey simian CMV (SCMV)-related entity with unusual fungal, bacterial and mammalian gene homologues. Stealth viruses have not yet been independently replicated in tissue culture, and therefore their biological significance remains unclear. ORF3, ORF4, ORF5 and ORF6 are complete ORFs whereas the sequence of ORF7 is incomplete. In the present study, we identified five corresponding ORFs in the genome of a clinical isolate of bonafide simian CMV (SCMV), strain 9610. We found substantial differences between the SCMV and "stealth virus" ORFs, especially for ORF5 where there are 31% non-identities at the amino acid level. Four conserved genes unrelated to chemokines (64K/CAP, DNBI, UL32, and IE2) in SCMV and HCMV had on average 52% identity at the deduced amino acid level, whereas the corresponding values for the SCMV ORFs versus US28 ranged from 21% to 30%, suggesting rapid gene diversification in this cluster. Consistent with this, the amino acid identity for any pairwise comparison among the SCMV ORFs is only 21-52%. The chemokine receptor homologues are estimated to comprise approximately 2-3% of the SCMV genome. HCMV US27 and US28 homologues have also been identified in the chimpanzee CMV genome, whereas mouse and rat CMV lack chemokine receptor homologues. This genomic analysis indicates that SCMV has an unusually high concentration of US28-related chemokine receptor homologues that have arisen by gene duplication and have diverged extensively from their closest relatives in mammals and other beta herpesviruses. The rate of divergence appears to be very rapid compared to other known SCMV genes, suggesting strong positive selection.
    MeSH term(s) Amino Acid Sequence ; Animals ; Cercopithecus aethiops/virology ; Cytomegalovirus/genetics ; Genome, Viral ; Humans ; Membrane Proteins/genetics ; Molecular Sequence Data ; Open Reading Frames ; Pan troglodytes/virology ; Receptors, Chemokine/genetics ; Sequence Alignment ; Sequence Analysis, DNA ; Sequence Homology
    Chemical Substances Membrane Proteins ; Receptors, Chemokine
    Language English
    Publishing date 2004-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 639496-6
    ISSN 1572-994X ; 0920-8569
    ISSN (online) 1572-994X
    ISSN 0920-8569
    DOI 10.1023/B:VIRU.0000012265.33168.b5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2397: Show issues Location:
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  5. Article: Apoptosis-inducing agents cause rapid shedding of tumor necrosis factor receptor 1 (TNFR1). A nonpharmacological explanation for inhibition of TNF-mediated activation.

    Madge, L A / Sierra-Honigmann, M R / Pober, J S

    The Journal of biological chemistry

    1999  Volume 274, Issue 19, Page(s) 13643–13649

    Abstract: Several chemical compounds not known to interact with tumor necrosis factor (TNF) signal transducing proteins inhibit TNF-mediated activation of vascular endothelial cells (EC). Four structurally diverse agents, arachidonyl trifluoromethylketone, ... ...

    Abstract Several chemical compounds not known to interact with tumor necrosis factor (TNF) signal transducing proteins inhibit TNF-mediated activation of vascular endothelial cells (EC). Four structurally diverse agents, arachidonyl trifluoromethylketone, staurosporine, sodium salicylate, and C6-ceramide, were studied. All four agents caused EC apoptosis at concentrations that inhibited TNF-induced IkappaBalpha degradation. However, evidence of apoptosis was not evident until after several (e.g. 3-12) hours of treatment, whereas 2 h of treatment was sufficient to inhibit TNF responses. IL-1-induced IkappaBalpha degradation was unaffected by these treatments. Inhibition of TNF signaling could not be prevented with either of the broad spectrum caspase inhibitors zVADfmk or yVADcmk. The inhibition of p38 kinase with SB203580 prevented the inhibition of TNF signaling by all agents except arachidonyl trifluoromethylketone. No changes in the levels or molecular weights of the adaptor proteins TRADD (TNF receptor-associated death domain), RIP (receptor-interacting protein), or TRAF2 (TNF receptor-associated factor-2) were caused by apoptogenic drugs. However, TNF receptor 1 (TNFR1) surface expression was significantly reduced by all four agents. Furthermore, TNF-dependent recruitment of TRADD to surface TNFR1 was also inhibited. These data suggest that several putative inhibitors of TNF signaling work by triggering apoptosis and that an early event coincident with the initiation of apoptosis, preceding evidence of injury, is loss of TNFR1. Consistent with this hypothesis, cotreatment of EC with the metalloproteinase inhibitor Tapi (TNF-alpha proteinase inhibitor) blocked the reduction in surface TNFR1 by apoptogenic drugs and prevented inhibition of TNF-induced IkappaBalpha degradation without blocking apoptosis. TNFR1 loss could be a mechanism to limit inflammation in response to apoptotic cell death.
    MeSH term(s) Apoptosis/drug effects ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Caspases/metabolism ; Cells, Cultured ; DNA-Binding Proteins/metabolism ; Endothelium, Vascular/cytology ; Endothelium, Vascular/drug effects ; Endothelium, Vascular/metabolism ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; I-kappa B Proteins ; Interleukin-1/metabolism ; Mitogen-Activated Protein Kinases ; NF-KappaB Inhibitor alpha ; Proteins/metabolism ; Receptors, Tumor Necrosis Factor/metabolism ; Signal Transduction ; TNF Receptor-Associated Factor 1 ; Tumor Necrosis Factor-alpha/metabolism ; p38 Mitogen-Activated Protein Kinases
    Chemical Substances DNA-Binding Proteins ; Enzyme Inhibitors ; I-kappa B Proteins ; Interleukin-1 ; NFKBIA protein, human ; Proteins ; Receptors, Tumor Necrosis Factor ; TNF Receptor-Associated Factor 1 ; Tumor Necrosis Factor-alpha ; NF-KappaB Inhibitor alpha (139874-52-5) ; Calcium-Calmodulin-Dependent Protein Kinases (EC 2.7.11.17) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Caspases (EC 3.4.22.-)
    Language English
    Publishing date 1999-05-07
    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.274.19.13643
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Quantitative and morphometric evaluation of the angiogenic effects of leptin.

    Talavera-Adame, Dodanim / Xiong, Yizhi / Zhao, Tong / Arias, Ana E / Sierra-Honigmann, M Rocio / Farkas, Daniel L

    Journal of biomedical optics

    2008  Volume 13, Issue 6, Page(s) 64017

    Abstract: Angiogenesis is a dynamic process that requires an interaction of pro-and antiangiogenic factors. It is known that the cytokine leptin stimulates endothelial cell growth and angiogenesis, but further quantitative analysis is necessary to understand ... ...

    Abstract Angiogenesis is a dynamic process that requires an interaction of pro-and antiangiogenic factors. It is known that the cytokine leptin stimulates endothelial cell growth and angiogenesis, but further quantitative analysis is necessary to understand leptin angiogenic effects. The quail chorioallantoic membrane (CAM) assay has been used to study angiogenesis in vivo by focusing on morphometric parameters that quantify vascular complexity and density. We quantify the angiogenic activity of leptin using the CAM assay by digital morphometry and a computer-assisted image analysis to evaluate more precisely vessel length, diameter, branching, and tortuousity. CAM images are obtained from ex ovo cultures of E8-E9 quail embryos. MATLAB and custom software are used for our analysis. The effects of leptin, vascular endothelial growth factor-165 (VEGF(165)), and their corresponding neutralizing antibodies are compared. Our results show that CAM treated with leptin and VEGF(165) has a significant increase in vascular complexity and density. A corresponding decrease is observed using neutralizing antibodies. Notably, leptin induced more significant changes than VEGF in vessel length and tortuousity. Conversely, VEGF induced a greater increase in vessel branching than leptin. These results underscore the importance of using multiparametric quantitative methods to assess several aspects of angiogenesis and enable us to understand the proangiogenic effects of leptin.
    MeSH term(s) Angiogenic Proteins/administration & dosage ; Animals ; Biological Assay/methods ; Chorioallantoic Membrane/blood supply ; Chorioallantoic Membrane/cytology ; Chorioallantoic Membrane/drug effects ; Chorioallantoic Membrane/physiology ; Dose-Response Relationship, Drug ; Image Interpretation, Computer-Assisted/methods ; Leptin/administration & dosage ; Neovascularization, Physiologic/drug effects ; Neovascularization, Physiologic/physiology ; Quail/anatomy & histology ; Quail/embryology ; Quail/growth & development ; Vascular Endothelial Growth Factor A/administration & dosage
    Chemical Substances Angiogenic Proteins ; Leptin ; VEGFA protein, human ; Vascular Endothelial Growth Factor A
    Language English
    Publishing date 2008-12-06
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1309154-2
    ISSN 1083-3668
    ISSN 1083-3668
    DOI 10.1117/1.3028010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 4699: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  8. Article: T cell receptor-independent immunosuppression induced by dexamethasone in murine T helper cells.

    Sierra-Honigmann, M R / Murphy, P A

    The Journal of clinical investigation

    1992  Volume 89, Issue 2, Page(s) 556–560

    Abstract: The immune and inflammatory responses are largely inhibited by glucocorticosteroids. In thymocytes, for example, glucocorticosteroids cause apoptosis, whereas they suppress the activity of phospholipase A2 and the production of eicosanoids in tissues ... ...

    Abstract The immune and inflammatory responses are largely inhibited by glucocorticosteroids. In thymocytes, for example, glucocorticosteroids cause apoptosis, whereas they suppress the activity of phospholipase A2 and the production of eicosanoids in tissues actively engaged in inflammation. The immunosuppressive action of dexamethasone (DEX) was studied in vitro by employing a model cell system, namely the murine Th2 clone D10.G4.1 (D10) and its clonotypic anti-T cell receptor (TCR) mAb 3D3. Although the proliferative response of D10 cells to 3D3 stimulation was not affected by DEX, the costimulation provided by IL-1 was dramatically inhibited. Substitution of 3D3 by exogenous IL-4 (as the IL-1 costimulant) failed to prevent the inhibition of proliferation caused by DEX. Yet, when 3D3-mediated stimulation of TCR was supplemented with IL-2, D10 cells were capable of proliferating, even in the presence of DEX. Thus, TCR stimulation on D10 cells remained intact and their resulting propagation was not compromised by DEX treatment. These results provide evidence that immunosuppression caused by DEX is TCR independent and involves an early cytokine-signalling event.
    MeSH term(s) Animals ; Cells, Cultured ; Dexamethasone/pharmacology ; Immune Tolerance/drug effects ; Interleukin-1/pharmacology ; Interleukin-4/pharmacology ; Mice ; Receptors, Antigen, T-Cell/physiology ; Receptors, Interleukin-2/analysis ; T-Lymphocytes, Helper-Inducer/drug effects ; T-Lymphocytes, Helper-Inducer/immunology
    Chemical Substances Interleukin-1 ; Receptors, Antigen, T-Cell ; Receptors, Interleukin-2 ; Interleukin-4 (207137-56-2) ; Dexamethasone (7S5I7G3JQL)
    Language English
    Publishing date 1992-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3067-3
    ISSN 1558-8238 ; 0021-9738
    ISSN (online) 1558-8238
    ISSN 0021-9738
    DOI 10.1172/JCI115620
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  9. Article: Suppression of interleukin-1 action by phospholipase-A2 inhibitors in helper T lymphocytes.

    Sierra-Honigmann, M R / Murphy, P A

    Peptide research

    1992  Volume 5, Issue 5, Page(s) 258–261

    Abstract: The mechanism by which interleukin 1 (IL-1) and T cell receptor (TCR) activation co-stimulate T helper (Th) cells is not clear. In chondrocytes, fibroblasts and several other cell types, much of the evidence suggests a linkage between IL-1 action and ... ...

    Abstract The mechanism by which interleukin 1 (IL-1) and T cell receptor (TCR) activation co-stimulate T helper (Th) cells is not clear. In chondrocytes, fibroblasts and several other cell types, much of the evidence suggests a linkage between IL-1 action and increased phospholipase-A2 (PLA2) activity. Although Th cells have very low levels of PLA2, they are well known targets for IL-1. We studied the effects of PLA2 inhibitors, i.e., lipocortin-1 (LC-1) and the synthetic peptide antiflammin-P2 (AF-2), on the enhancing effect of IL-1 upon activation of TCR. When murine D10.G4.1 Th2 cells were stimulated by their clonotypic anti-TCR antibody 3D3, both LC-1 and AF-2 inhibited the biological response to IL-1. This blockade was not seen when D10 cells were induced to proliferate with interleukin-2 (IL-2) and 3D3 in the presence of the same inhibitors, LC-1 or AF-2. These results strongly suggest that PLA2 also plays a central role in mediating the actions of IL-1 in the helper T cell.
    MeSH term(s) Amino Acid Sequence ; Animals ; Annexin A1/chemistry ; Annexin A1/pharmacology ; Cells, Cultured ; Interleukin-1/antagonists & inhibitors ; Mice ; Molecular Sequence Data ; Peptides/chemistry ; Peptides/pharmacology ; Phospholipases A/antagonists & inhibitors ; Phospholipases A2 ; T-Lymphocytes, Helper-Inducer/drug effects ; T-Lymphocytes, Helper-Inducer/metabolism
    Chemical Substances Annexin A1 ; Interleukin-1 ; Peptides ; Phospholipases A (EC 3.1.1.32) ; Phospholipases A2 (EC 3.1.1.4)
    Language English
    Publishing date 1992-09
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 1033579-1
    ISSN 1040-5704
    ISSN 1040-5704
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2947: Show issues Location:
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  10. Article: Transcriptional activation of the human leptin gene in response to hypoxia. Involvement of hypoxia-inducible factor 1.

    Ambrosini, Grazia / Nath, Anjali K / Sierra-Honigmann, M Rocío / Flores-Riveros, Jaime

    The Journal of biological chemistry

    2002  Volume 277, Issue 37, Page(s) 34601–34609

    Abstract: In addition to having a major role in energy homeostasis, leptin is emerging as a pleiotropic cytokine with multiple physiological effector functions. The recently discovered proangiogenic activity of leptin suggested the hypothesis that its production ... ...

    Abstract In addition to having a major role in energy homeostasis, leptin is emerging as a pleiotropic cytokine with multiple physiological effector functions. The recently discovered proangiogenic activity of leptin suggested the hypothesis that its production might be regulated by hypoxia, as are other angiogenic factors. To examine this proposal, the expression of leptin protein and mRNA was measured and found to be markedly up-regulated in response to ambient or chemical hypoxia (upon exposure to desferrioxamine or cobalt chloride), an effect that requires intact RNA synthesis, suggesting a transcriptional mechanism. Transient transfection of cultured cells with deletion constructs of the leptin gene promoter linked to a reporter gene revealed a functional hypoxia response element (HRE) located at position -116 within the proximal upstream region. This putative HRE harbors a characteristic 5'-RCGTG-3' core motif, a hallmark of hypoxia-sensitive genes and recognized by the hypoxia-inducible factor 1 (HIF1), which consists of a HIF1alpha/HIFbeta heterodimer. Constructs harboring this -116/HRE supported reporter gene expression in response to hypoxia but not when mutated. Expression of HIF1alpha cDNA in normoxic cells mimicked hypoxia-induced reporter gene expression in cells cotransfected with the wild type leptin -116/HRE construct but not with the mutant. Gel shift assays with a (32)P-labeled leptin promoter -116/HRE probe and nuclear extracts from hypoxia-treated cells indicated binding of the HIF1alpha/beta heterodimer, which was blocked with an excess of unlabeled -116/HRE probe or a HIF1-binding probe from the erythropoietin gene enhancer. Taken together, these observations demonstrate that the leptin gene is actively engaged by hypoxia through a transcriptional pathway commonly utilized by hypoxia-sensitive genes.
    MeSH term(s) Base Sequence ; Binding Sites ; CCAAT-Enhancer-Binding Proteins/metabolism ; Cells, Cultured ; Fibroblasts/metabolism ; Gene Expression Regulation ; Humans ; Hypoxia/metabolism ; Hypoxia-Inducible Factor 1, alpha Subunit ; Leptin/genetics ; Molecular Sequence Data ; Promoter Regions, Genetic ; Response Elements ; Transcription Factors/physiology ; Transcriptional Activation
    Chemical Substances CCAAT-Enhancer-Binding Proteins ; HIF1A protein, human ; Hypoxia-Inducible Factor 1, alpha Subunit ; Leptin ; Transcription Factors
    Language English
    Publishing date 2002-06-25
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M205172200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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