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Your search keyword '"Biggs, J. C."' showing total 28 results
Start Over Author "Biggs, J. C." Publisher wiley
28 results on '"Biggs, J. C."'

4. Changing results of HLA‐identical sibling bone marrow transplantation in patients with haematological malignancy during the period 1981–1990

Author

Atkinson, K., primary, Marshall, G., additional, Biggs, J. C., additional, Wilson, F., additional, Concannon, A. J., additional, Young, S., additional, Dodds, A. J., additional, Ashby, M., additional, Milliken, S., additional, Morgan, G., additional, Downs, K., additional, and Harkness, J., additional

Published
1993
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28. A recombinant GM-CSF-PE40 ligand toxin is functionally active but not cytotoxic to cells.

Author

O'Brien P, Smythe A, Biggs JC, and Smith GM

Subjects
Adenosine Diphosphate Ribose metabolism, Bacterial Toxins genetics, Bacterial Toxins metabolism, Base Sequence, Biological Transport, Active, Bone Marrow Purging, Bone Marrow Transplantation, Cell Death drug effects, DNA Primers genetics, Exotoxins genetics, Exotoxins metabolism, Granulocyte-Macrophage Colony-Stimulating Factor genetics, Granulocyte-Macrophage Colony-Stimulating Factor metabolism, Humans, Immunotoxins genetics, Immunotoxins metabolism, In Vitro Techniques, Leukemia, Myeloid therapy, Polymerase Chain Reaction, Receptors, Granulocyte-Macrophage Colony-Stimulating Factor metabolism, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Recombinant Fusion Proteins pharmacology, Transplantation Conditioning, Tumor Cells, Cultured, Pseudomonas aeruginosa Exotoxin A, ADP Ribose Transferases, Bacterial Toxins pharmacology, Exotoxins pharmacology, Granulocyte-Macrophage Colony-Stimulating Factor pharmacology, Immunotoxins pharmacology, Virulence Factors
Abstract

A granulocyte/macrophage colony-stimulating factor (GM-CSF)-Pseudomonas exotoxin (PE) 40 fusion protein was constructed for potential use in the treatment of myeloid leukaemias, as a conditioning agent prior to allogeneic bone marrow transplantation or for ex vivo purging of malignant cells prior to autologous bone marrow transplantation. The GM-CSF-PE40 fusion protein successfully binds to the GM-CSF receptor and is capable of initiating a mitogenic signal similar to native GM-CSF in the GM-CSF-dependent TF1 cell line. The toxin component also appears to be fully functional as determined by an in vitro adenosine diphosphate-ribosylation assay. The GM-CSF-PE40 fusion protein, however, was not cytotoxic to a number of myeloid leukaemia cell lines. It is suggested that the mechanism of internalization of the GM-CSF receptor is not appropriate for the translocation of PE to the cytosol where it can fulfil its cytotoxic potential.

Published
1997
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