Cytoskeletal association of human α-interferon-receptor complexes in interferon-sensitive and -resistant lymphoblastoid cells

Lawrence Pfeffer, N. Stebbing, D. B. Donner

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Abstract

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(d) = 20 x 10-12 M), 3000 (K(d) = 45 x 10-12 M), and 3700 (K(d) = 52 x 10-12 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.

Original languageEnglish (US)
Pages (from-to)3249-3253
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number10
DOIs
StatePublished - Jan 1 1987

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Interferon Receptors
Interferons
Cytochalasin B
Octoxynol
Interferon-alpha
Cell Communication
Solubility
Binding Sites
Ligands

All Science Journal Classification (ASJC) codes

  • General

Cite this

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title = "Cytoskeletal association of human α-interferon-receptor complexes in interferon-sensitive and -resistant lymphoblastoid cells",
abstract = "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(d) = 20 x 10-12 M), 3000 (K(d) = 45 x 10-12 M), and 3700 (K(d) = 52 x 10-12 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.",
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T1 - Cytoskeletal association of human α-interferon-receptor complexes in interferon-sensitive and -resistant lymphoblastoid cells

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AU - Stebbing, N.

AU - Donner, D. B.

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N2 - 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(d) = 20 x 10-12 M), 3000 (K(d) = 45 x 10-12 M), and 3700 (K(d) = 52 x 10-12 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.

AB - 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(d) = 20 x 10-12 M), 3000 (K(d) = 45 x 10-12 M), and 3700 (K(d) = 52 x 10-12 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.

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