Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1987 May;84(10):3249–3253. doi: 10.1073/pnas.84.10.3249

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

L M Pfeffer, N Stebbing, D B Donner
PMCID: PMC304846  PMID: 2953024

Abstract

Human Daudi lymphoblastoid cells, which are highly sensitive to the antiproliferative action of human leukocyte alpha-interferon (IFN-alpha), and IFN-resistant and IFN-sensitive Daudi subclones (Cl2 and Cl1, respectively), contain 2300 (Kd = 20 X 10(-12) M), 3000 (Kd = 45 X 10(-12) M), and 3700 (Kd = 52 X 10(-12) M) IFN-alpha binding sites per cell, respectively. Thus, these IFN-sensitive and IFN-resistant cells have similar numbers of high-affinity IFN-alpha 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-alpha from IFN-sensitive and IFN-resistant cells can be resolved into fast and slow components. IFN-alpha dissociates more slowly from IFN-sensitive cells than from IFN-resistant cells. Very slow dissociation of IFN-alpha 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-alpha on Daudi cells.

Full text

PDF
3249

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adams A., Strander H., Cantell K. Sensitivity of the Epstein-Barr virus transformed human lymphoid cell lines to interferon. J Gen Virol. 1975 Aug;28(2):207–217. doi: 10.1099/0022-1317-28-2-207. [DOI] [PubMed] [Google Scholar]
  2. Aguet M., Mogensen K. E. Interferon receptors. Interferon. 1983;5:1–22. [PubMed] [Google Scholar]
  3. Ben-Ze'ev A., Duerr A., Solomon F., Penman S. The outer boundary of the cytoskeleton: a lamina derived from plasma membrane proteins. Cell. 1979 Aug;17(4):859–865. doi: 10.1016/0092-8674(79)90326-x. [DOI] [PubMed] [Google Scholar]
  4. Bourgeade M. F., Chany C. Effect of sodium butyrate on the antiviral and anticellular action of interferon in normal and MSV-transformed cells. Int J Cancer. 1979 Sep 15;24(3):314–318. doi: 10.1002/ijc.2910240307. [DOI] [PubMed] [Google Scholar]
  5. Bourgeade M. F., Chany C. Inhibition of interferon action by cytochalasin B, colchicine, and vinblastine. Proc Soc Exp Biol Med. 1976 Dec;153(3):501–504. doi: 10.3181/00379727-153-39578. [DOI] [PubMed] [Google Scholar]
  6. Branca A. A., Baglioni C. Evidence that types I and II interferons have different receptors. Nature. 1981 Dec 24;294(5843):768–770. doi: 10.1038/294768a0. [DOI] [PubMed] [Google Scholar]
  7. Branca A. A., Faltynek C. R., D'Alessandro S. B., Baglioni C. Interaction of interferon with cellular receptors. Internalization and degradation of cell-bound interferon. J Biol Chem. 1982 Nov 25;257(22):13291–13296. [PubMed] [Google Scholar]
  8. Braun J., Hochman P. S., Unanue E. R. Ligand-induced association of surface immunoglobulin with the detergent-insoluble cytoskeletal matrix of the B lymphocyte. J Immunol. 1982 Mar;128(3):1198–1204. [PubMed] [Google Scholar]
  9. Brown M. S., Anderson R. G., Goldstein J. L. Recycling receptors: the round-trip itinerary of migrant membrane proteins. Cell. 1983 Mar;32(3):663–667. doi: 10.1016/0092-8674(83)90052-1. [DOI] [PubMed] [Google Scholar]
  10. Chany C., Rousset S., Bourgeade M. F., Mathieu D., Grégoire A. Role of receptors and the cytoskeleton in reverse transformation and steroidogenesis induced by interferon. Ann N Y Acad Sci. 1980;350:254–265. doi: 10.1111/j.1749-6632.1980.tb20626.x. [DOI] [PubMed] [Google Scholar]
  11. Corin R. E., Donner D. B. Insulin receptors convert to a higher affinity state subsequent to hormone binding. A two-state model for the insulin receptor. J Biol Chem. 1982 Jan 10;257(1):104–110. [PubMed] [Google Scholar]
  12. Haigler H. T., Maxfield F. R., Willingham M. C., Pastan I. Dansylcadaverine inhibits internalization of 125I-epidermal growth factor in BALB 3T3 cells. J Biol Chem. 1980 Feb 25;255(4):1239–1241. [PubMed] [Google Scholar]
  13. Jesaitis A. J., Naemura J. R., Sklar L. A., Cochrane C. G., Painter R. G. Rapid modulation of N-formyl chemotactic peptide receptors on the surface of human granulocytes: formation of high-affinity ligand-receptor complexes in transient association with cytoskeleton. J Cell Biol. 1984 Apr;98(4):1378–1387. doi: 10.1083/jcb.98.4.1378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Landreth G. E., Shooter E. M. Nerve growth factor receptors on PC12 cells: ligand-induced conversion from low- to high-affinity states. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4751–4755. doi: 10.1073/pnas.77.8.4751. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Landreth G. E., Williams L. K., Rieser G. D. Association of the epidermal growth factor receptor kinase with the detergent-insoluble cytoskeleton of A431 cells. J Cell Biol. 1985 Oct;101(4):1341–1350. doi: 10.1083/jcb.101.4.1341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. McCaleb M. L., Donner D. B. Affinity of the hepatic insulin receptor is influenced by membrane phospholipids. J Biol Chem. 1981 Nov 10;256(21):11051–11057. [PubMed] [Google Scholar]
  17. Pfeffer L. M., Landsberger F. R., Tamm I. Beta-interferon-induced time-dependent changes in the plasma membrane lipid bilayer of cultured cells. J Interferon Res. 1981;1(4):613–620. doi: 10.1089/jir.1981.1.613. [DOI] [PubMed] [Google Scholar]
  18. Pfeffer L. M., Tamm I. Effects of beta interferon on concanavalin A binding and size of HeLa cells. J Interferon Res. 1982;2(3):431–440. doi: 10.1089/jir.1982.2.431. [DOI] [PubMed] [Google Scholar]
  19. Pfeffer L. M., Wang E., Tamm I. Interferon effects on microfilament organization, cellular fibronectin distribution, and cell motility in human fibroblasts. J Cell Biol. 1980 Apr;85(1):9–17. doi: 10.1083/jcb.85.1.9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Schechter A. L., Bothwell M. A. Nerve growth factor receptors on PC12 cells: evidence for two receptor classes with differing cytoskeletal association. Cell. 1981 Jun;24(3):867–874. doi: 10.1016/0092-8674(81)90112-4. [DOI] [PubMed] [Google Scholar]
  21. Sine S., Taylor P. Functional consequences of agonist-mediated state transitions in the cholinergic receptor. Studies in cultured muscle cells. J Biol Chem. 1979 May 10;254(9):3315–3325. [PubMed] [Google Scholar]
  22. Wang E., Pfeffer L. M., Tamm I. Interferon increases the abundance of submembranous microfilaments in HeLa-S3 cells in suspension culture. Proc Natl Acad Sci U S A. 1981 Oct;78(10):6281–6285. doi: 10.1073/pnas.78.10.6281. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES