Skip to main content
PMC home page
Molecular and Cellular Biology logoLink to Molecular and Cellular Biology
. 1987 Nov;7(11):3955–3970. doi: 10.1128/mcb.7.11.3955

Expression of transfected vimentin genes in differentiating murine erythroleukemia cells reveals divergent cis-acting regulation of avian and mammalian vimentin sequences.

J Ngai 1, V C Bond 1, B J Wold 1, E Lazarides 1
PMCID: PMC368064  PMID: 3481037

Abstract

We studied the expression of transfected chicken and hamster vimentin genes in murine erythroleukemia (MEL) cells. MEL cells normally repress the levels of endogenous mouse vimentin mRNA during inducermediated differentiation, resulting in a subsequent loss of vimentin filaments. Expression of vimentin in differentiating MEL cells reflects the disappearance of vimentin filaments during mammalian erythropoiesis in vivo. In contrast, chicken erythroid cells express high levels of vimentin mRNA and vimentin filaments during terminal differentiation. We demonstrate here that chicken vimentin mRNA levels increase significantly in differentiating transfected MEL cells, whereas similarly transfected hamster vimentin genes are negatively regulated. In conjunction with in vitro nuclear run-on transcription experiments, these results suggest that the difference in vimentin expression in avian and mammalian erythropoiesis is due to a divergence of cis-linked vimentin sequences that are responsible for transcriptional and posttranscriptional regulation of vimentin gene expression. Transfected chicken vimentin genes produce functional vimentin protein and stable vimentin filaments during MEL cell differentiation, further demonstrating that the accumulation of vimentin filaments is determined by the abundance of newly synthesized vimentin.

Full text

PDF
3959

Images in this article

3959Image
on p.3959
3960Image
on p.3960
3962Image
on p.3962
3962Image
on p.3962
3963Image
on p.3963
3964Image
on p.3964
3964Image
on p.3964

Selected References

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

  1. Alter B. P., Goff S. C. Variable globin chain synthesis in mouse erythroleukemia cells. Blood. 1978 Nov;52(5):1047–1057. [PubMed] [Google Scholar]
  2. Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1408–1412. doi: 10.1073/pnas.69.6.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Axelrod V. D., Kramer F. R. Transcription from bacteriophage T7 and SP6 RNA polymerase promoters in the presence of 3'-deoxyribonucleoside 5'-triphosphate chain terminators. Biochemistry. 1985 Oct 8;24(21):5716–5723. doi: 10.1021/bi00342a005. [DOI] [PubMed] [Google Scholar]
  4. Birnstiel M. L., Busslinger M., Strub K. Transcription termination and 3' processing: the end is in site! Cell. 1985 Jun;41(2):349–359. doi: 10.1016/s0092-8674(85)80007-6. [DOI] [PubMed] [Google Scholar]
  5. Blikstad I., Lazarides E. Vimentin filaments are assembled from a soluble precursor in avian erythroid cells. J Cell Biol. 1983 Jun;96(6):1803–1808. doi: 10.1083/jcb.96.6.1803. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bond V. C., Wold B. Poly-L-ornithine-mediated transformation of mammalian cells. Mol Cell Biol. 1987 Jun;7(6):2286–2293. doi: 10.1128/mcb.7.6.2286. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  8. Bradley R. H., Ireland M., Maisel H. The cytoskeleton of chick lens cells. Exp Eye Res. 1979 Apr;28(4):441–453. doi: 10.1016/0014-4835(79)90119-2. [DOI] [PubMed] [Google Scholar]
  9. Brock M. L., Shapiro D. J. Estrogen stabilizes vitellogenin mRNA against cytoplasmic degradation. Cell. 1983 Aug;34(1):207–214. doi: 10.1016/0092-8674(83)90151-4. [DOI] [PubMed] [Google Scholar]
  10. Capetanaki Y. G., Ngai J., Flytzanis C. N., Lazarides E. Tissue-specific expression of two mRNA species transcribed from a single vimentin gene. Cell. 1983 Dec;35(2 Pt 1):411–420. doi: 10.1016/0092-8674(83)90174-5. [DOI] [PubMed] [Google Scholar]
  11. Carey M. F., Singh K., Botchan M., Cozzarelli N. R. Induction of specific transcription by RNA polymerase III in transformed cells. Mol Cell Biol. 1986 Sep;6(9):3068–3076. doi: 10.1128/mcb.6.9.3068. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Chada K., Magram J., Costantini F. An embryonic pattern of expression of a human fetal globin gene in transgenic mice. Nature. 1986 Feb 20;319(6055):685–689. doi: 10.1038/319685a0. [DOI] [PubMed] [Google Scholar]
  13. Chao M. V., Mellon P., Charnay P., Maniatis T., Axel R. The regulated expression of beta-globin genes introduced into mouse erythroleukemia cells. Cell. 1983 Feb;32(2):483–493. doi: 10.1016/0092-8674(83)90468-3. [DOI] [PubMed] [Google Scholar]
  14. Chapman L. F. Effect of calcium on differentiation of Friend leukemia cells. Dev Biol. 1980 Sep;79(1):243–246. doi: 10.1016/0012-1606(80)90088-3. [DOI] [PubMed] [Google Scholar]
  15. Charnay P., Mellon P., Maniatis T. Linker scanning mutagenesis of the 5'-flanking region of the mouse beta-major-globin gene: sequence requirements for transcription in erythroid and nonerythroid cells. Mol Cell Biol. 1985 Jun;5(6):1498–1511. doi: 10.1128/mcb.5.6.1498. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Charnay P., Treisman R., Mellon P., Chao M., Axel R., Maniatis T. Differences in human alpha- and beta-globin gene expression in mouse erythroleukemia cells: the role of intragenic sequences. Cell. 1984 Aug;38(1):251–263. doi: 10.1016/0092-8674(84)90547-6. [DOI] [PubMed] [Google Scholar]
  17. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  18. Deisseroth A., Bode U., Fontana J., Hendrick D. Expression of human alpha-globin genes in hybrid mouse erythroleukaemia cells depends on differentiated state of human donor cell. Nature. 1980 May 1;285(5759):36–38. doi: 10.1038/285036a0. [DOI] [PubMed] [Google Scholar]
  19. Deisseroth A., Hendrick D. Activation of phenotypic expression of human globin genes from nonerythroid cells by chromosome-dependent transfer to tetraploid mouse erythroleukemia cells. Proc Natl Acad Sci U S A. 1979 May;76(5):2185–2189. doi: 10.1073/pnas.76.5.2185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Deisseroth A., Hendrick D. Human alpha-globin gene expression following chromosomal dependent gene transfer into mouse erythroleukemia cells. Cell. 1978 Sep;15(1):55–63. doi: 10.1016/0092-8674(78)90082-x. [DOI] [PubMed] [Google Scholar]
  21. Dellagi K., Vainchenker W., Vinci G., Paulin D., Brouet J. C. Alteration of vimentin intermediate filament expression during differentiation of human hemopoietic cells. EMBO J. 1983;2(9):1509–1514. doi: 10.1002/j.1460-2075.1983.tb01615.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Dodemont H. J., Soriano P., Quax W. J., Ramaekers F., Lenstra J. A., Groenen M. A., Bernardi G., Bloemendal H. The genes coding for the cytoskeletal proteins actin and vimentin in warm-blooded vertebrates. EMBO J. 1982;1(2):167–171. doi: 10.1002/j.1460-2075.1982.tb01142.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Dräger U. C. Coexistence of neurofilaments and vimentin in a neurone of adult mouse retina. Nature. 1983 May 12;303(5913):169–172. doi: 10.1038/303169a0. [DOI] [PubMed] [Google Scholar]
  24. Efstratiadis A., Posakony J. W., Maniatis T., Lawn R. M., O'Connell C., Spritz R. A., DeRiel J. K., Forget B. G., Weissman S. M., Slightom J. L. The structure and evolution of the human beta-globin gene family. Cell. 1980 Oct;21(3):653–668. doi: 10.1016/0092-8674(80)90429-8. [DOI] [PubMed] [Google Scholar]
  25. Enoch T., Zinn K., Maniatis T. Activation of the human beta-interferon gene requires an interferon-inducible factor. Mol Cell Biol. 1986 Mar;6(3):801–810. doi: 10.1128/mcb.6.3.801. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Farnham P. J., Schimke R. T. Transcriptional regulation of mouse dihydrofolate reductase in the cell cycle. J Biol Chem. 1985 Jun 25;260(12):7675–7680. [PubMed] [Google Scholar]
  27. Ferrari S., Battini R., Kaczmarek L., Rittling S., Calabretta B., de Riel J. K., Philiponis V., Wei J. F., Baserga R. Coding sequence and growth regulation of the human vimentin gene. Mol Cell Biol. 1986 Nov;6(11):3614–3620. doi: 10.1128/mcb.6.11.3614. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Franke W. W., Schmid E., Osborn M., Weber K. Different intermediate-sized filaments distinguished by immunofluorescence microscopy. Proc Natl Acad Sci U S A. 1978 Oct;75(10):5034–5038. doi: 10.1073/pnas.75.10.5034. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Friend C., Scher W., Holland J. G., Sato T. Hemoglobin synthesis in murine virus-induced leukemic cells in vitro: stimulation of erythroid differentiation by dimethyl sulfoxide. Proc Natl Acad Sci U S A. 1971 Feb;68(2):378–382. doi: 10.1073/pnas.68.2.378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Gard D. L., Bell P. B., Lazarides E. Coexistence of desmin and the fibroblastic intermediate filament subunit in muscle and nonmuscle cells: identification and comparative peptide analysis. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3894–3898. doi: 10.1073/pnas.76.8.3894. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Giudice G. J., Fuchs E. The transfection of epidermal keratin genes into fibroblasts and simple epithelial cells: evidence for inducing a type I keratin by a type II gene. Cell. 1987 Feb 13;48(3):453–463. doi: 10.1016/0092-8674(87)90196-6. [DOI] [PubMed] [Google Scholar]
  32. Granger B. L., Lazarides E. Desmin and vimentin coexist at the periphery of the myofibril Z disc. Cell. 1979 Dec;18(4):1053–1063. doi: 10.1016/0092-8674(79)90218-6. [DOI] [PubMed] [Google Scholar]
  33. Granger B. L., Lazarides E. Expression of the major neurofilament subunit in chicken erythrocytes. Science. 1983 Aug 5;221(4610):553–556. doi: 10.1126/science.6346488. [DOI] [PubMed] [Google Scholar]
  34. Granger B. L., Lazarides E. Structural associations of synemin and vimentin filaments in avian erythrocytes revealed by immunoelectron microscopy. Cell. 1982 Aug;30(1):263–275. doi: 10.1016/0092-8674(82)90032-0. [DOI] [PubMed] [Google Scholar]
  35. Granger B. L., Repasky E. A., Lazarides E. Synemin and vimentin are components of intermediate filaments in avian erythrocytes. J Cell Biol. 1982 Feb;92(2):299–312. doi: 10.1083/jcb.92.2.299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Groudine M., Peretz M., Weintraub H. Transcriptional regulation of hemoglobin switching in chicken embryos. Mol Cell Biol. 1981 Mar;1(3):281–288. doi: 10.1128/mcb.1.3.281. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Humphries R. K., Ley T., Turner P., Moulton A. D., Nienhuis A. W. Differences in human alpha-, beta- and delta-globin gene expression in monkey kidney cells. Cell. 1982 Aug;30(1):173–183. doi: 10.1016/0092-8674(82)90023-x. [DOI] [PubMed] [Google Scholar]
  38. Jones K. A., Yamamoto K. R., Tjian R. Two distinct transcription factors bind to the HSV thymidine kinase promoter in vitro. Cell. 1985 Sep;42(2):559–572. doi: 10.1016/0092-8674(85)90113-8. [DOI] [PubMed] [Google Scholar]
  39. Kafatos F. C., Jones C. W., Efstratiadis A. Determination of nucleic acid sequence homologies and relative concentrations by a dot hybridization procedure. Nucleic Acids Res. 1979 Nov 24;7(6):1541–1552. doi: 10.1093/nar/7.6.1541. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Kedinger C., Gniazdowski M., Mandel J. L., Jr, Gissinger F., Chambon P. Alpha-amanitin: a specific inhibitor of one of two DNA-pendent RNA polymerase activities from calf thymus. Biochem Biophys Res Commun. 1970 Jan 6;38(1):165–171. doi: 10.1016/0006-291x(70)91099-5. [DOI] [PubMed] [Google Scholar]
  41. Kollias G., Wrighton N., Hurst J., Grosveld F. Regulated expression of human A gamma-, beta-, and hybrid gamma beta-globin genes in transgenic mice: manipulation of the developmental expression patterns. Cell. 1986 Jul 4;46(1):89–94. doi: 10.1016/0092-8674(86)90862-7. [DOI] [PubMed] [Google Scholar]
  42. Kondoh H., Katoh K., Takahashi Y., Fujisawa H., Yokoyama M., Kimura S., Katsuki M., Saito M., Nomura T., Hiramoto Y. Specific expression of the chicken delta-crystallin gene in the lens and the pyramidal neurons of the piriform cortex in transgenic mice. Dev Biol. 1987 Mar;120(1):177–185. doi: 10.1016/0012-1606(87)90116-3. [DOI] [PubMed] [Google Scholar]
  43. Kondoh H., Yasuda K., Okada T. S. Tissue-specific expression of a cloned chick delta-crystallin gene in mouse cells. Nature. 1983 Feb 3;301(5899):440–442. doi: 10.1038/301440a0. [DOI] [PubMed] [Google Scholar]
  44. Konkel D. A., Maizel J. V., Jr, Leder P. The evolution and sequence comparison of two recently diverged mouse chromosomal beta--globin genes. Cell. 1979 Nov;18(3):865–873. doi: 10.1016/0092-8674(79)90138-7. [DOI] [PubMed] [Google Scholar]
  45. Kreis T. E., Geiger B., Schmid E., Jorcano J. L., Franke W. W. De novo synthesis and specific assembly of keratin filaments in nonepithelial cells after microinjection of mRNA for epidermal keratin. Cell. 1983 Apr;32(4):1125–1137. doi: 10.1016/0092-8674(83)90296-9. [DOI] [PubMed] [Google Scholar]
  46. Lazarides E. Intermediate filaments: a chemically heterogeneous, developmentally regulated class of proteins. Annu Rev Biochem. 1982;51:219–250. doi: 10.1146/annurev.bi.51.070182.001251. [DOI] [PubMed] [Google Scholar]
  47. Levenson R., Housman D., Cantley L. Amiloride inhibits murine erythroleukemia cell differentiation: evidence for a Ca2+ requirement for commitment. Proc Natl Acad Sci U S A. 1980 Oct;77(10):5948–5952. doi: 10.1073/pnas.77.10.5948. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Lewis J. A., Matkovich D. A. Genetic determinants of growth phase-dependent and adenovirus 5-responsive expression of the Chinese hamster thymidine kinase gene are contained within thymidine kinase mRNA sequences. Mol Cell Biol. 1986 Jun;6(6):2262–2266. doi: 10.1128/mcb.6.6.2262. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Leys E. J., Crouse G. F., Kellems R. E. Dihydrofolate reductase gene expression in cultured mouse cells is regulated by transcript stabilization in the nucleus. J Cell Biol. 1984 Jul;99(1 Pt 1):180–187. doi: 10.1083/jcb.99.1.180. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Lindell T. J., Weinberg F., Morris P. W., Roeder R. G., Rutter W. J. Specific inhibition of nuclear RNA polymerase II by alpha-amanitin. Science. 1970 Oct 23;170(3956):447–449. doi: 10.1126/science.170.3956.447. [DOI] [PubMed] [Google Scholar]
  51. Linial M., Gunderson N., Groudine M. Enhanced transcription of c-myc in bursal lymphoma cells requires continuous protein synthesis. Science. 1985 Dec 6;230(4730):1126–1132. doi: 10.1126/science.2999973. [DOI] [PubMed] [Google Scholar]
  52. Lowy I., Pellicer A., Jackson J. F., Sim G. K., Silverstein S., Axel R. Isolation of transforming DNA: cloning the hamster aprt gene. Cell. 1980 Dec;22(3):817–823. doi: 10.1016/0092-8674(80)90558-9. [DOI] [PubMed] [Google Scholar]
  53. Marks P. A., Rifkind R. A. Erythroleukemic differentiation. Annu Rev Biochem. 1978;47:419–448. doi: 10.1146/annurev.bi.47.070178.002223. [DOI] [PubMed] [Google Scholar]
  54. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  55. McKnight G. S., Palmiter R. D. Transcriptional regulation of the ovalbumin and conalbumin genes by steroid hormones in chick oviduct. J Biol Chem. 1979 Sep 25;254(18):9050–9058. [PubMed] [Google Scholar]
  56. McTavish C. F., Nelson W. J., Traub P. Synthesis of vimentin in a reticulocyte cell-free system programmed by poly(A)-rich RNA from several cell lines and rat liver. Eur J Biochem. 1983 Jan 17;130(1):211–221. doi: 10.1111/j.1432-1033.1983.tb07138.x. [DOI] [PubMed] [Google Scholar]
  57. Mellon P., Parker V., Gluzman Y., Maniatis T. Identification of DNA sequences required for transcription of the human alpha 1-globin gene in a new SV40 host-vector system. Cell. 1981 Dec;27(2 Pt 1):279–288. doi: 10.1016/0092-8674(81)90411-6. [DOI] [PubMed] [Google Scholar]
  58. Melton D. A., Krieg P. A., Rebagliati M. R., Maniatis T., Zinn K., Green M. R. Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 1984 Sep 25;12(18):7035–7056. doi: 10.1093/nar/12.18.7035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Merrill G. F., Hauschka S. D., McKnight S. L. tk Enzyme expression in differentiating muscle cells is regulated through an internal segment of the cellular tk gene. Mol Cell Biol. 1984 Sep;4(9):1777–1784. doi: 10.1128/mcb.4.9.1777. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Moon R. T., Lazarides E. Synthesis and post-translational assembly of intermediate filaments in avian erythroid cells: vimentin assembly limits the rate of synemin assembly. Proc Natl Acad Sci U S A. 1983 Sep;80(18):5495–5499. doi: 10.1073/pnas.80.18.5495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Moon R. T., Ngai J., Wold B. J., Lazarides E. Tissue-specific expression of distinct spectrin and ankyrin transcripts in erythroid and nonerythroid cells. J Cell Biol. 1985 Jan;100(1):152–160. doi: 10.1083/jcb.100.1.152. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Nalbantoglu J., Phear G. A., Meuth M. Nucleotide sequence of hamster adenine phosphoribosyl transferase (aprt) gene. Nucleic Acids Res. 1986 Feb 25;14(4):1914–1914. doi: 10.1093/nar/14.4.1914. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Nalbantoglu J., Phear G., Meuth M. DNA sequence analysis of spontaneous mutations at the aprt locus of hamster cells. Mol Cell Biol. 1987 Apr;7(4):1445–1449. doi: 10.1128/mcb.7.4.1445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Nelson W. J., Traub P. Intermediate (10 nm) filament proteins and the Ca2+-activated proteinase specific for vimentin and desmin in the cells from fish to man: an example of evolutionary conservation. J Cell Sci. 1982 Oct;57:25–49. doi: 10.1242/jcs.57.1.25. [DOI] [PubMed] [Google Scholar]
  65. Nelson W. J., Traub P. Properties of Ca2+-activated protease specific for the intermediate-sized filament protein vimentin in Ehrlich-ascites-tumour cells. Eur J Biochem. 1981 May;116(1):51–57. doi: 10.1111/j.1432-1033.1981.tb05299.x. [DOI] [PubMed] [Google Scholar]
  66. Nelson W. J., Traub P. Purification and further characterization of the Ca2+-activated proteinase specific for the intermediate filament proteins vimentin and desmin. J Biol Chem. 1982 May 25;257(10):5544–5553. [PubMed] [Google Scholar]
  67. Ngai J., Capetanaki Y. G., Lazarides E. Differentiation of murine erythroleukemia cells results in the rapid repression of vimentin gene expression. J Cell Biol. 1984 Jul;99(1 Pt 1):306–314. doi: 10.1083/jcb.99.1.306. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  69. Paek I., Axel R. Glucocorticoids enhance stability of human growth hormone mRNA. Mol Cell Biol. 1987 Apr;7(4):1496–1507. doi: 10.1128/mcb.7.4.1496. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Piatigorsky J. Lens crystallins and their gene families. Cell. 1984 Oct;38(3):620–621. doi: 10.1016/0092-8674(84)90254-x. [DOI] [PubMed] [Google Scholar]
  71. Quax W., Egberts W. V., Hendriks W., Quax-Jeuken Y., Bloemendal H. The structure of the vimentin gene. Cell. 1983 Nov;35(1):215–223. doi: 10.1016/0092-8674(83)90224-6. [DOI] [PubMed] [Google Scholar]
  72. Quax W., van den Broek L., Egberts W. V., Ramaekers F., Bloemendal H. Characterization of the hamster desmin gene: expression and formation of desmin filaments in nonmuscle cells after gene transfer. Cell. 1985 Nov;43(1):327–338. doi: 10.1016/0092-8674(85)90038-8. [DOI] [PubMed] [Google Scholar]
  73. Quinlan R. A., Franke W. W. Heteropolymer filaments of vimentin and desmin in vascular smooth muscle tissue and cultured baby hamster kidney cells demonstrated by chemical crosslinking. Proc Natl Acad Sci U S A. 1982 Jun;79(11):3452–3456. doi: 10.1073/pnas.79.11.3452. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Quinlan R. A., Franke W. W. Molecular interactions in intermediate-sized filaments revealed by chemical cross-linking. Heteropolymers of vimentin and glial filament protein in cultured human glioma cells. Eur J Biochem. 1983 May 16;132(3):477–484. doi: 10.1111/j.1432-1033.1983.tb07386.x. [DOI] [PubMed] [Google Scholar]
  75. Ramaekers F. C., Osborn M., Schimid E., Weber K., Bloemendal H., Franke W. W. Identification of the cytoskeletal proteins in lens-forming cells, a special epitheloid cell type. Exp Cell Res. 1980 Jun;127(2):309–327. doi: 10.1016/0014-4827(80)90437-1. [DOI] [PubMed] [Google Scholar]
  76. Robins D. M., Paek I., Seeburg P. H., Axel R. Regulated expression of human growth hormone genes in mouse cells. Cell. 1982 Jun;29(2):623–631. doi: 10.1016/0092-8674(82)90178-7. [DOI] [PubMed] [Google Scholar]
  77. Santiago C., Collins M., Johnson L. F. In vitro and in vivo analysis of the control of dihydrofolate reductase gene transcription in serum-stimulated mouse fibroblasts. J Cell Physiol. 1984 Jan;118(1):79–86. doi: 10.1002/jcp.1041180114. [DOI] [PubMed] [Google Scholar]
  78. Schnitzer J., Franke W. W., Schachner M. Immunocytochemical demonstration of vimentin in astrocytes and ependymal cells of developing and adult mouse nervous system. J Cell Biol. 1981 Aug;90(2):435–447. doi: 10.1083/jcb.90.2.435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Schümperli D. Cell-cycle regulation of histone gene expression. Cell. 1986 May 23;45(4):471–472. doi: 10.1016/0092-8674(86)90277-1. [DOI] [PubMed] [Google Scholar]
  80. Sharp G., Osborn M., Weber K. Occurrence of two different intermediate filament proteins in the same filament in situ within a human glioma cell line. An immunoelectron microscopical study. Exp Cell Res. 1982 Oct;141(2):385–395. doi: 10.1016/0014-4827(82)90227-0. [DOI] [PubMed] [Google Scholar]
  81. Steinert P. M., Idler W. W., Cabral F., Gottesman M. M., Goldman R. D. In vitro assembly of homopolymer and copolymer filaments from intermediate filament subunits of muscle and fibroblastic cells. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3692–3696. doi: 10.1073/pnas.78.6.3692. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Steinert P. M., Steven A. C., Roop D. R. The molecular biology of intermediate filaments. Cell. 1985 Sep;42(2):411–420. doi: 10.1016/0092-8674(85)90098-4. [DOI] [PubMed] [Google Scholar]
  83. Stewart C. J., Ito M., Conrad S. E. Evidence for transcriptional and post-transcriptional control of the cellular thymidine kinase gene. Mol Cell Biol. 1987 Mar;7(3):1156–1163. doi: 10.1128/mcb.7.3.1156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Tapscott S. J., Bennett G. S., Toyama Y., Kleinbart F., Holtzer H. Intermediate filament proteins in the developing chick spinal cord. Dev Biol. 1981 Aug;86(1):40–54. doi: 10.1016/0012-1606(81)90313-4. [DOI] [PubMed] [Google Scholar]
  85. Treisman R., Green M. R., Maniatis T. cis and trans activation of globin gene transcription in transient assays. Proc Natl Acad Sci U S A. 1983 Dec;80(24):7428–7432. doi: 10.1073/pnas.80.24.7428. [DOI] [PMC free article] [PubMed] [Google Scholar]
  86. Tuszynski G. P., Frank E. D., Damsky C. H., Buck C. A., Warren L. The detection of smooth muscle desmin-like protein in BHK21/C13 fibroblasts. J Biol Chem. 1979 Jul 10;254(13):6138–6143. [PubMed] [Google Scholar]
  87. Virtanen I., Kurkinen M., Lehto V. P. Nucleus-anchoring cytoskeleton in chicken red blood cells. Cell Biol Int Rep. 1979 Mar;3(2):157–162. doi: 10.1016/0309-1651(79)90121-8. [DOI] [PubMed] [Google Scholar]
  88. Volloch V., Housman D. Terminal differentiation of murine erythroleukemia cells: physical stabilization of end-stage cells. J Cell Biol. 1982 May;93(2):390–394. doi: 10.1083/jcb.93.2.390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  89. Wigler M., Sweet R., Sim G. K., Wold B., Pellicer A., Lacy E., Maniatis T., Silverstein S., Axel R. Transformation of mammalian cells with genes from procaryotes and eucaryotes. Cell. 1979 Apr;16(4):777–785. doi: 10.1016/0092-8674(79)90093-x. [DOI] [PubMed] [Google Scholar]
  90. Woodcock C. L. Nucleus-associated intermediate filaments from chicken erythrocytes. J Cell Biol. 1980 Jun;85(3):881–889. doi: 10.1083/jcb.85.3.881. [DOI] [PMC free article] [PubMed] [Google Scholar]
  91. Wright S., Rosenthal A., Flavell R., Grosveld F. DNA sequences required for regulated expression of beta-globin genes in murine erythroleukemia cells. Cell. 1984 Aug;38(1):265–273. doi: 10.1016/0092-8674(84)90548-8. [DOI] [PubMed] [Google Scholar]
  92. Yen S. H., Fields K. L. Antibodies to neurofilament, glial filament, and fibroblast intermediate filament proteins bind to different cell types of the nervous system. J Cell Biol. 1981 Jan;88(1):115–126. doi: 10.1083/jcb.88.1.115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  93. Zehner Z. E., Li Y., Roe B. A., Paterson B. M., Sax C. M. The chicken vimentin gene. Nucleotide sequence, regulatory elements, and comparison to the hamster gene. J Biol Chem. 1987 Jun 15;262(17):8112–8120. [PubMed] [Google Scholar]
  94. Zehner Z. E., Paterson B. M. Characterization of the chicken vimentin gene: single copy gene producing multiple mRNAs. Proc Natl Acad Sci U S A. 1983 Feb;80(4):911–915. doi: 10.1073/pnas.80.4.911. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Zehner Z. E., Paterson B. M. Vimentin gene expression during myogenesis: two functional transcripts from a single copy gene. Nucleic Acids Res. 1983 Dec 10;11(23):8317–8332. doi: 10.1093/nar/11.23.8317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. Zinn K., DiMaio D., Maniatis T. Identification of two distinct regulatory regions adjacent to the human beta-interferon gene. Cell. 1983 Oct;34(3):865–879. doi: 10.1016/0092-8674(83)90544-5. [DOI] [PubMed] [Google Scholar]

Articles from Molecular and Cellular Biology are provided here courtesy of Taylor & Francis

RESOURCES