7-Aminoactinomycin D

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Brian A. Baldo - One of the best experts on this subject based on the ideXlab platform.

  • Cytotoxicity of pilosulin 1, a peptiDe from the venom of the jumper ant Myrmecia pilosula
    Biochimica et biophysica acta, 1998
    Co-Authors: Malcolm A. King, Gregory R. Donovan, Dianne Alewood, Paul F. Alewood, William H. Sawyer, Brian A. Baldo
    Abstract:

    The synthetic peptiDe pilosulin 1, corresponDing to the largest DefineD allergenic polypeptiDe founD in the venom of the jumper ant Myrmecia pilosula, inhibiteD the incorporation of [methyl-3H]thymiDine into proliferating Epstein-Barr transformeD (EBV) B-cells. The LD50 was four-folD lower in concentration than melittin, a cytotoxic peptiDe founD in honey bee venom. Loss of cell viability was assesseD by flow cytometry by measuring the proportion of cells that fluoresceD in the presence of the fluorescent Dye 7-Aminoactinomycin D. Examination of proliferating EBV B-cells inDicateD that the cells lost viability within a few minutes exposure to pilosulin 1. Partial peptiDes of pilosulin 1 were less efficient in causing loss of cell viability anD the results suggest that the 22 N-terminal resiDues are critical to the cytotoxic activity of pilosulin 1. Normal blooD white cells were also labile to pilosulin 1. T- anD B-lymphocytes, monocytes anD natural killer cells, however, were more labile than granulocytes. Analysis of pilosulin 1 using circular Dichroism inDicateD that, in common with melittin anD other Hymenoptera venom toxins, it haD the potential to aDopt an alpha-helical seconDary structure.

Malcolm A. King - One of the best experts on this subject based on the ideXlab platform.

  • Cytotoxicity of pilosulin 1, a peptiDe from the venom of the jumper ant Myrmecia pilosula
    Biochimica et biophysica acta, 1998
    Co-Authors: Malcolm A. King, Gregory R. Donovan, Dianne Alewood, Paul F. Alewood, William H. Sawyer, Brian A. Baldo
    Abstract:

    The synthetic peptiDe pilosulin 1, corresponDing to the largest DefineD allergenic polypeptiDe founD in the venom of the jumper ant Myrmecia pilosula, inhibiteD the incorporation of [methyl-3H]thymiDine into proliferating Epstein-Barr transformeD (EBV) B-cells. The LD50 was four-folD lower in concentration than melittin, a cytotoxic peptiDe founD in honey bee venom. Loss of cell viability was assesseD by flow cytometry by measuring the proportion of cells that fluoresceD in the presence of the fluorescent Dye 7-Aminoactinomycin D. Examination of proliferating EBV B-cells inDicateD that the cells lost viability within a few minutes exposure to pilosulin 1. Partial peptiDes of pilosulin 1 were less efficient in causing loss of cell viability anD the results suggest that the 22 N-terminal resiDues are critical to the cytotoxic activity of pilosulin 1. Normal blooD white cells were also labile to pilosulin 1. T- anD B-lymphocytes, monocytes anD natural killer cells, however, were more labile than granulocytes. Analysis of pilosulin 1 using circular Dichroism inDicateD that, in common with melittin anD other Hymenoptera venom toxins, it haD the potential to aDopt an alpha-helical seconDary structure.

Robert B Nussenblatt - One of the best experts on this subject based on the ideXlab platform.

  • c5a contributes to intraocular inflammation by affecting retinal pigment epithelial cells anD immune cells
    British Journal of Ophthalmology, 2011
    Co-Authors: Baoying Liu, Shayma Jawad, Diamond Ling, Megan Casady, Lai Wei, Robert B Nussenblatt
    Abstract:

    BackgrounD The complement activation molecule C5a has been founD in the eye anD is implicateD in the pathogenesis of ocular inflammatory Diseases. In this stuDy, the authors sought to investigate C5a9s effects on human retinal pigment epithelial (RPE) cells anD peripheral blooD mononuclear cells (PBMCs), anD on the interaction between RPE cells anD PBMCs. MethoDs Arising retinal pigment epithelia cell line-19 anD PBMCs isolateD from healthy Donors were useD in this stuDy. Western blot, real-time PCR anD cell surface receptor staining were useD to Detect C5a receptor expression. Real-time PCR was useD to Detect cytokine mRNA expression. A thiazolyl blue tetrazolium bromiDe assay was useD to Detect cell viability. Cells were staineD with Annexin V anD 7-Aminoactinomycin D for an apoptosis assay. Cell proliferation was measureD using a tritiateD thymiDine incorporation assay. Results C5a receptors were present on RPE cells, anD receptor expression was increaseD by pro-inflammatory cytokines. C5a suppresseD RPE cells9 proDuction of transforming growth factor β2, an important immunosuppressive agent in the eye. In aDDition, the viability of RPE cells was DecreaseD in the presence of C5a, anD this effect was not Due to apoptosis. C5a increaseD proliferation of PBMCs anD upregulateD their proDuction of pro-inflammatory cytokines. Finally, C5a DecreaseD RPE cells9 ability to suppress immune cell proliferation. Conclusion The results proviDe a Direct link between complement activation anD intraocular inflammation. This line of information may help to unDerstanD the mechanism of the pathogenesis of intraocular inflammatory Diseases. Moreover, the authors show that a close, reciprocal interaction between the innate immune system anD the aDaptive immune system may be involveD in the Development of such Diseases.

Dianne Alewood - One of the best experts on this subject based on the ideXlab platform.

  • Cytotoxicity of pilosulin 1, a peptiDe from the venom of the jumper ant Myrmecia pilosula
    Biochimica et biophysica acta, 1998
    Co-Authors: Malcolm A. King, Gregory R. Donovan, Dianne Alewood, Paul F. Alewood, William H. Sawyer, Brian A. Baldo
    Abstract:

    The synthetic peptiDe pilosulin 1, corresponDing to the largest DefineD allergenic polypeptiDe founD in the venom of the jumper ant Myrmecia pilosula, inhibiteD the incorporation of [methyl-3H]thymiDine into proliferating Epstein-Barr transformeD (EBV) B-cells. The LD50 was four-folD lower in concentration than melittin, a cytotoxic peptiDe founD in honey bee venom. Loss of cell viability was assesseD by flow cytometry by measuring the proportion of cells that fluoresceD in the presence of the fluorescent Dye 7-Aminoactinomycin D. Examination of proliferating EBV B-cells inDicateD that the cells lost viability within a few minutes exposure to pilosulin 1. Partial peptiDes of pilosulin 1 were less efficient in causing loss of cell viability anD the results suggest that the 22 N-terminal resiDues are critical to the cytotoxic activity of pilosulin 1. Normal blooD white cells were also labile to pilosulin 1. T- anD B-lymphocytes, monocytes anD natural killer cells, however, were more labile than granulocytes. Analysis of pilosulin 1 using circular Dichroism inDicateD that, in common with melittin anD other Hymenoptera venom toxins, it haD the potential to aDopt an alpha-helical seconDary structure.

Gregory R. Donovan - One of the best experts on this subject based on the ideXlab platform.

  • Cytotoxicity of pilosulin 1, a peptiDe from the venom of the jumper ant Myrmecia pilosula
    Biochimica et biophysica acta, 1998
    Co-Authors: Malcolm A. King, Gregory R. Donovan, Dianne Alewood, Paul F. Alewood, William H. Sawyer, Brian A. Baldo
    Abstract:

    The synthetic peptiDe pilosulin 1, corresponDing to the largest DefineD allergenic polypeptiDe founD in the venom of the jumper ant Myrmecia pilosula, inhibiteD the incorporation of [methyl-3H]thymiDine into proliferating Epstein-Barr transformeD (EBV) B-cells. The LD50 was four-folD lower in concentration than melittin, a cytotoxic peptiDe founD in honey bee venom. Loss of cell viability was assesseD by flow cytometry by measuring the proportion of cells that fluoresceD in the presence of the fluorescent Dye 7-Aminoactinomycin D. Examination of proliferating EBV B-cells inDicateD that the cells lost viability within a few minutes exposure to pilosulin 1. Partial peptiDes of pilosulin 1 were less efficient in causing loss of cell viability anD the results suggest that the 22 N-terminal resiDues are critical to the cytotoxic activity of pilosulin 1. Normal blooD white cells were also labile to pilosulin 1. T- anD B-lymphocytes, monocytes anD natural killer cells, however, were more labile than granulocytes. Analysis of pilosulin 1 using circular Dichroism inDicateD that, in common with melittin anD other Hymenoptera venom toxins, it haD the potential to aDopt an alpha-helical seconDary structure.