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Media type:
E-Article
Title:
Cytoskeletal Association of Human α -interferon-receptor Complexes in Interferon-Sensitive and -Resistant Lymphoblastoid Cells
Contributor:
Pfeffer, Lawrence M.;
Stebbing, Nowell;
Donner, David B.
imprint:
National Academy of Sciences of the United States of America, 1987
Published in:Proceedings of the National Academy of Sciences of the United States of America
Language:
English
ISSN:
0027-8424
Origination:
Footnote:
Description:
<p>Human Daudi lymphoblastoid cells, which are highly sensitive to the antiproliferative action of human leukocyte α -interferon (IFN-α ), and IFN-resistant and IFN-sensitive Daudi subclones (C12 and C11, respectively), contain 2300 (K<sub>d</sub>= 20 × 10<sup>-12</sup>M), 3000 (K<sub>d</sub>= 45 × 10<sup>-12</sup>M), and 3700 (K<sub>d</sub>= 52 × 10<sup>-12</sup>M) IFN-α binding sites per cell, respectively. Thus, these IFN-sensitive and IFN-resistant cells have similar numbers of high-affinity IFN-α receptors. IFN-receptor complexes that are insoluble in Triton X-100 accumulate in IFN-sensitive but not in IFN-resistant cells. The ligand-induced accumulation of Triton-insoluble complexes in IFN-sensitive cells was inhibited by cytochalasin B. This suggests that the solubility change of IFN-receptor complexes results from their interaction with the cytoskeletal matrix. The dissociation of IFN-α from IFN-sensitive and IFN-resistant cells can be resolved into fast and slow components. IFN-α dissociates more slowly from IFN-sensitive cells than from IFN-resistant cells. Very slow dissociation of IFN-α from Triton-insoluble complexes correlates with this difference. These observations suggest that IFN-receptor complexes become coupled to the cytoskeletal matrix in IFN-sensitive but not in IFN-resistant cells, and that such interaction is an important element in the mechanism of the antiproliferative action of IFN-α on Daudi cells.</p>