GLORIA

GEOMAR Library Ocean Research Information Access

X

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Online Resource
    Online Resource
    Toll-like receptors in inflammation, infection and cancer
    Elsevier BV ; 2007
    In:  International Immunopharmacology Vol. 7, No. 10 ( 2007-10), p. 1271-1285
    Details
    In: International Immunopharmacology, Elsevier BV, Vol. 7, No. 10 ( 2007-10), p. 1271-1285
    Type of Medium: Online Resource
    ISSN: 1567-5769
    URL: Article
    DOI: 10.1016/j.intimp.2007.05.016
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2007
    detail.hit.zdb_id: 2049924-3
    SSG: 15,3
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 2
    Online Resource
    Online Resource
    Transactivation of the Epidermal Growth Factor Receptor by Formylpeptide Receptor Exacerbates the Malignant Behavior of Human Glioblastoma Cells
    American Association for Cancer Research (AACR) ; 2007
    In:  Cancer Research Vol. 67, No. 12 ( 2007-06-15), p. 5906-5913
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 67, No. 12 ( 2007-06-15), p. 5906-5913
    Abstract: The G protein-coupled formylpeptide receptor (FPR), which mediates leukocyte migration in response to bacterial and host-derived chemotactic peptides, promotes the chemotaxis, survival, and tumorigenesis of highly malignant human glioblastoma cells. Because glioblastoma cells may also express other receptors for growth signals, such as the epidermal growth factor (EGF) receptor (EGFR), we investigated the role of EGFR in the signaling cascade of FPR and how two receptors cross-talk to exacerbate tumor growth. We found that N-formyl-methionyl-leucyl-phenylalanine, an FPR agonist peptide, rapidly induced EGFR phosphorylation at tyrosine residue (Tyr) 992, but not residues 846, 1068, or 1173, in glioblastoma cells, whereas all these residues were phosphorylated after only EGF treatment. The FPR agonist-induced EGFR phosphorylation in tumor cells was dependent on the presence of FPR as well as Gαi proteins, and was controlled by Src tyrosine kinase. The transactivation of EGFR contributes to the biological function of FPR in glioblastoma cells because inhibition of EGFR phosphorylation significantly reduced FPR agonist-induced tumor cell chemotaxis and proliferation. Furthermore, depletion of both FPR and EGFR by short interference RNA abolished the tumorigenesis of the glioblastoma cells. Our study indicates that the glioblastoma-promoting activity of FPR is mediated in part by transactivation of EGFR and the cross-talk between two receptors exacerbates the malignant phenotype of tumor cells. Thus, targeting both receptors may yield antiglioblastoma agents superior to those targeting one of them. [Cancer Res 2007;67(12):5906–13]
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/0008-5472.CAN-07-0691
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2007
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 3
    Online Resource
    Online Resource
    Synergy of TRIF-dependent TLR3 and MyD88-dependent TLR7 in up-regulating expression of mouse FPR2, a promiscuous G-protein-coupled receptor, in microglial cells (92.9)
    The American Association of Immunologists ; 2009
    In:  The Journal of Immunology Vol. 182, No. 1_Supplement ( 2009-04-01), p. 92.9-92.9
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 182, No. 1_Supplement ( 2009-04-01), p. 92.9-92.9
    Abstract: Human G-protein-coupled formyl peptide receptor-like 1 (FPRL1) and its mouse homologue mFPR2 mediate leukocyte chemotaxis to a variety of pathogen and host-derived peptides, including amyloid â42, a key causative factor in Alzheimer's disease. In mouse microglial cells, mFPR2 is up-regulated by several TLR ligands, resulting in increased cell response to and endocytosis of A â42 peptide. Since microglial cells may be exposed to multiple TLR agonists under pathological conditions, we investigated the consequence of activating TLR3, whose signaling is dependent on the adaptor TRIF, and TLR7, which signals through MyD88. The TLR3 agonist Poly(I:C) and the TLR7 agonist R837, when used alone, each dose-dependently increased the expression of functional mFPR2 in microglial cells. Combination of suboptional concentrations of Poly(I:C) and R837 showed a marked synergistic effect on induction of mFPR2. We further observed that Poly(I:C) enhanced I êB-á phosphorylation induced by R837. Our results indicate that the TRIF-dependent TLR3 and MyD88-dependent TLR7 cooperate to regulate microglial responses which are known to be involved in brain inflammation and neurodegenerative disease.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.182.Supp.92.9
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 2009
    detail.hit.zdb_id: 1475085-5
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 4
    Online Resource
    Online Resource
    Cooperation between NOD2 and Toll-like receptor 2 ligands in the up-regulation of mouse mFPR2, a G-protein-coupled Aβ42 peptide receptor, in microglial cells
    Oxford University Press (OUP) ; 2008
    In:  Journal of Leukocyte Biology Vol. 83, No. 6 ( 2008-06-01), p. 1467-1475
    Details
    In: Journal of Leukocyte Biology, Oxford University Press (OUP), Vol. 83, No. 6 ( 2008-06-01), p. 1467-1475
    Abstract: Human G-protein-coupled formyl peptide receptor-like 1 and its mouse homologue formyl peptide receptor 2 (mFPR2) mediate the chemotactic activity of a variety of pathogen and host-derived peptides, including amyloid β42, a key causative factor in Alzheimer’s disease. In mouse microglia, mFPR2 is up-regulated by pathogen-associated molecular patterns and proinflammatory cytokines, as shown, for instance, in our previous study using peptidoglycan (PGN) of Gram+ bacteria. As PGN and its components have been reported to use TLR2 and an intracellular receptor nucleotide-binding oligomerization domain 2 (NOD2), we investigated the capacity of palmitoyl-cys[(RS)-2, 3-di(palmitoyloxy)-propyl]-Ala-Gly-OH (PamCAG), a specific TLR2 ligand, and muramyl dipeptide (MDP), a NOD2 ligand, to cooperatively regulate the expression and function of mFPR2 in microglia. We found that MDP and PamCAG as well as another TLR2-specific agonist palmitoyl-3-cysteine-serine-lysine-4 (Pam3CSK4), when used alone, each increased the expression of functional mFPR2 in microglial cells, and the combination of MDP and PamCAG or Pam3CSK4 exhibited an additive effect. Mechanistic studies revealed that MDP increased the levels of TLR2 expression on the microglial cell surface and enhanced the levels of MAPKs p-38, ERK1/2, and NF-κB activated by PamCAG. Our results suggest that TLR2 and NOD2 cooperate to up-regulate the expression of mFPR2 and therefore, may actively participate in the pathogenic processes of brain inflammation and neurodegenerative diseases.
    Type of Medium: Online Resource
    ISSN: 0741-5400 , 1938-3673
    URL: Article
    DOI: 10.1189/jlb.0907607
    RVK:
    XA 10000
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2008
    detail.hit.zdb_id: 2026833-6
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 5
    Online Resource
    Online Resource
    Regulation of the leucocyte chemoattractant receptor FPR in glioblastoma cells by cell differentiation
    Oxford University Press (OUP) ; 2009
    In:  Carcinogenesis Vol. 30, No. 2 ( 2009-2), p. 348-355
    Details
    In: Carcinogenesis, Oxford University Press (OUP), Vol. 30, No. 2 ( 2009-2), p. 348-355
    Type of Medium: Online Resource
    ISSN: 1460-2180 , 0143-3334
    URL: Article
    DOI: 10.1093/carcin/bgn266
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2009
    detail.hit.zdb_id: 1474206-8
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 6
    Online Resource
    Online Resource
    Induction of the Formyl Peptide Receptor 2 in Microglia by IFN-γ and Synergy with CD40 Ligand
    The American Association of Immunologists ; 2007
    In:  The Journal of Immunology Vol. 178, No. 3 ( 2007-02-01), p. 1759-1766
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 178, No. 3 ( 2007-02-01), p. 1759-1766
    Abstract: Human formyl peptide receptor (FPR)-like 1 (FPRL1) and its mouse homologue mFPR2 are functional receptors for a variety of exogenous and host-derived chemotactic peptides, including amyloid β 1–42 (Aβ42), a pathogenic factor in Alzheimer’s disease. Because mFPR2 in microglial cells is regulated by proinflammatory stimulants including TLR agonists, in this study we investigated the capacity of IFN-γ and the CD40 ligand (CD40L) to affect the expression and function of mFPR2. We found that IFN-γ, when used alone, induced mFPR2 mRNA expression in a mouse microglial cell line and primary microglial cells in association with increased cell migration in response to mFPR2 agonists, including Aβ42. IFN-γ also increased the endocytosis of Aβ42 by microglial cells via mFPR2. The effect of IFN-γ on mFPR2 expression in microglial cells was dependent on activation of MAPK and IκB-α. IFN-γ additionally increased the expression of CD40 by microglial cells and soluble CD40L significantly promoted cell responses to IFN-γ during a 6-h incubation period by enhancing the activation of MAPK and IκB-α signaling pathways. We additionally found that the effect of IFN-γ and its synergy with CD40L on mFPR2 expression in microglia was mediated in part by TNF-α. Our results suggest that IFN-γ and CD40L, two host-derived factors with increased concentrations in inflammatory central nervous system diseases, may profoundly affect microglial cell responses in the pathogenic process in which mFPR2 agonist peptides are elevated.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.178.3.1759
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 2007
    detail.hit.zdb_id: 1475085-5
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...