Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1993 Nov 2;123(4):1037–1045. doi: 10.1083/jcb.123.4.1037

Downregulation of tenascin expression by glucocorticoids in bone marrow stromal cells and in fibroblasts

PMCID: PMC2200139  PMID: 7693719

Abstract

Tenascin, a predominantly mesenchymal extracellular matrix (ECM) glycoprotein has a rather restricted tissue distribution, but until now factors that inhibit its expression have not been identified. Glucocorticoids are known to be beneficial for establishment of myelopoiesis in long-term bone marrow cultures. Tenascin was found to be expressed in the bone marrow, and glucocorticoids were found to affect bone marrow tenascin expression. Both tenascin mRNAs and the mRNA of another ECM protein, laminin B1 chain, were drastically downregulated by glucocorticoids during initiation of bone marrow cultures. However, in already established long-term cultures glucocorticoids did not affect laminin B1 chain mRNA levels although tenascin mRNAs continued to be downregulated. Studies with a stromal cell line (MC3T3-G2/PA6) and fibroblasts (3T3) suggested that glucocorticoids act directly on the stromal cells that produce tenascin. In 3T3 cells this downregulation occurred within 12 h of glucocorticoid-treatment, suggesting that glucocorticoids acted through cis regulatory elements of the tenascin gene. We suggest that glucocorticoids in part regulate hematopoiesis by modifying the ECM. Furthermore, downregulation of tenascin expression by glucocorticoids may in part explain the restricted tissue distribution of tenascin in other tissues.

Full Text

The Full Text of this article is available as a PDF (2.7 MB).

Selected References

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

  1. Aufderheide E., Ekblom P. Tenascin during gut development: appearance in the mesenchyme, shift in molecular forms, and dependence on epithelial-mesenchymal interactions. J Cell Biol. 1988 Dec;107(6 Pt 1):2341–2349. doi: 10.1083/jcb.107.6.2341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Auffray C., Rougeon F. Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA. Eur J Biochem. 1980 Jun;107(2):303–314. doi: 10.1111/j.1432-1033.1980.tb06030.x. [DOI] [PubMed] [Google Scholar]
  3. Bentley S. A., Foidart J. M. Some properties of marrow derived adherent cells in tissue culture. Blood. 1980 Dec;56(6):1006–1012. [PubMed] [Google Scholar]
  4. Bristow J., Tee M. K., Gitelman S. E., Mellon S. H., Miller W. L. Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B. J Cell Biol. 1993 Jul;122(1):265–278. doi: 10.1083/jcb.122.1.265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Campbell A., Wicha M. S., Long M. Extracellular matrix promotes the growth and differentiation of murine hematopoietic cells in vitro. J Clin Invest. 1985 Jun;75(6):2085–2090. doi: 10.1172/JCI111928. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chiquet-Ehrismann R., Kalla P., Pearson C. A., Beck K., Chiquet M. Tenascin interferes with fibronectin action. Cell. 1988 May 6;53(3):383–390. doi: 10.1016/0092-8674(88)90158-4. [DOI] [PubMed] [Google Scholar]
  7. Chiquet-Ehrismann R., Mackie E. J., Pearson C. A., Sakakura T. Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis. Cell. 1986 Oct 10;47(1):131–139. doi: 10.1016/0092-8674(86)90374-0. [DOI] [PubMed] [Google Scholar]
  8. Chiquet-Ehrismann R., Matsuoka Y., Hofer U., Spring J., Bernasconi C., Chiquet M. Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues. Cell Regul. 1991 Nov;2(11):927–938. doi: 10.1091/mbc.2.11.927. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Chiquet M., Fambrough D. M. Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits. J Cell Biol. 1984 Jun;98(6):1937–1946. doi: 10.1083/jcb.98.6.1937. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 1987 Apr;162(1):156–159. doi: 10.1006/abio.1987.9999. [DOI] [PubMed] [Google Scholar]
  11. Church G. M., Gilbert W. Genomic sequencing. Proc Natl Acad Sci U S A. 1984 Apr;81(7):1991–1995. doi: 10.1073/pnas.81.7.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Coulombel L., Vuillet M. H., Leroy C., Tchernia G. Lineage- and stage-specific adhesion of human hematopoietic progenitor cells to extracellular matrices from marrow fibroblasts. Blood. 1988 Feb;71(2):329–334. [PubMed] [Google Scholar]
  13. Del Rosso M., Cappelletti R., Dini G., Fibbi G., Vannucchi S., Chiarugi V., Guazzelli C. Involvement of glycosaminoglycans in detachment of early myeloid precursors from bone-marrow stromal cells. Biochim Biophys Acta. 1981 Aug 17;676(2):129–136. doi: 10.1016/0304-4165(81)90180-x. [DOI] [PubMed] [Google Scholar]
  14. Deutzmann R., Aumailley M., Wiedemann H., Pysny W., Timpl R., Edgar D. Cell adhesion, spreading and neurite stimulation by laminin fragment E8 depends on maintenance of secondary and tertiary structure in its rod and globular domain. Eur J Biochem. 1990 Jul 31;191(2):513–522. doi: 10.1111/j.1432-1033.1990.tb19151.x. [DOI] [PubMed] [Google Scholar]
  15. Dexter T. M., Allen T. D., Lajtha L. G. Conditions controlling the proliferation of haemopoietic stem cells in vitro. J Cell Physiol. 1977 Jun;91(3):335–344. doi: 10.1002/jcp.1040910303. [DOI] [PubMed] [Google Scholar]
  16. Dexter T. M., Spooncer E. Growth and differentiation in the hemopoietic system. Annu Rev Cell Biol. 1987;3:423–441. doi: 10.1146/annurev.cb.03.110187.002231. [DOI] [PubMed] [Google Scholar]
  17. Diamond M. I., Miner J. N., Yoshinaga S. K., Yamamoto K. R. Transcription factor interactions: selectors of positive or negative regulation from a single DNA element. Science. 1990 Sep 14;249(4974):1266–1272. doi: 10.1126/science.2119054. [DOI] [PubMed] [Google Scholar]
  18. Dorshkind K. Regulation of hemopoiesis by bone marrow stromal cells and their products. Annu Rev Immunol. 1990;8:111–137. doi: 10.1146/annurev.iy.08.040190.000551. [DOI] [PubMed] [Google Scholar]
  19. Ekblom M., Klein G., Mugrauer G., Fecker L., Deutzmann R., Timpl R., Ekblom P. Transient and locally restricted expression of laminin A chain mRNA by developing epithelial cells during kidney organogenesis. Cell. 1990 Jan 26;60(2):337–346. doi: 10.1016/0092-8674(90)90748-4. [DOI] [PubMed] [Google Scholar]
  20. Ekblom P., Aufderheide E. Stimulation of tenascin expression in mesenchyme by epithelial-mesenchymal interactions. Int J Dev Biol. 1989 Mar;33(1):71–79. [PubMed] [Google Scholar]
  21. Eliason J. F. Long-term production of hemopoietic progenitors in cultures containing low levels of serum. Exp Hematol. 1984 Aug;12(7):559–567. [PubMed] [Google Scholar]
  22. Erickson H. P., Bourdon M. A. Tenascin: an extracellular matrix protein prominent in specialized embryonic tissues and tumors. Annu Rev Cell Biol. 1989;5:71–92. doi: 10.1146/annurev.cb.05.110189.000443. [DOI] [PubMed] [Google Scholar]
  23. Faissner A., Kruse J. J1/tenascin is a repulsive substrate for central nervous system neurons. Neuron. 1990 Nov;5(5):627–637. doi: 10.1016/0896-6273(90)90217-4. [DOI] [PubMed] [Google Scholar]
  24. Giancotti F. G., Comoglio P. M., Tarone G. Fibronectin-plasma membrane interaction in the adhesion of hemopoietic cells. J Cell Biol. 1986 Aug;103(2):429–437. doi: 10.1083/jcb.103.2.429. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Green H., Meuth M. An established pre-adipose cell line and its differentiation in culture. Cell. 1974 Oct;3(2):127–133. doi: 10.1016/0092-8674(74)90116-0. [DOI] [PubMed] [Google Scholar]
  26. Greenberger J. S. Sensitivity of corticosteroid-dependent insulin-resistant lipogenesis in marrow preadipocytes of obese-diabetic (db/db) mice. Nature. 1978 Oct 26;275(5682):752–754. doi: 10.1038/275752a0. [DOI] [PubMed] [Google Scholar]
  27. Hamilton R., Campbell F. R. Immunochemical localization of extracellular materials in bone marrow of rats. Anat Rec. 1991 Oct;231(2):218–224. doi: 10.1002/ar.1092310210. [DOI] [PubMed] [Google Scholar]
  28. Hemler M. E. Adhesive protein receptors on hematopoietic cells. Immunol Today. 1988 Apr;9(4):109–113. doi: 10.1016/0167-5699(88)91280-7. [DOI] [PubMed] [Google Scholar]
  29. Hoffman S., Crossin K. L., Edelman G. M. Molecular forms, binding functions, and developmental expression patterns of cytotactin and cytotactin-binding proteoglycan, an interactive pair of extracellular matrix molecules. J Cell Biol. 1988 Feb;106(2):519–532. doi: 10.1083/jcb.106.2.519. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Husmann K., Faissner A., Schachner M. Tenascin promotes cerebellar granule cell migration and neurite outgrowth by different domains in the fibronectin type III repeats. J Cell Biol. 1992 Mar;116(6):1475–1486. doi: 10.1083/jcb.116.6.1475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Jonat C., Rahmsdorf H. J., Park K. K., Cato A. C., Gebel S., Ponta H., Herrlich P. Antitumor promotion and antiinflammation: down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone. Cell. 1990 Sep 21;62(6):1189–1204. doi: 10.1016/0092-8674(90)90395-u. [DOI] [PubMed] [Google Scholar]
  32. Jones F. S., Hoffman S., Cunningham B. A., Edelman G. M. A detailed structural model of cytotactin: protein homologies, alternative RNA splicing, and binding regions. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1905–1909. doi: 10.1073/pnas.86.6.1905. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Kincade P. W., Lee G., Pietrangeli C. E., Hayashi S., Gimble J. M. Cells and molecules that regulate B lymphopoiesis in bone marrow. Annu Rev Immunol. 1989;7:111–143. doi: 10.1146/annurev.iy.07.040189.000551. [DOI] [PubMed] [Google Scholar]
  34. Klein G., Ekblom M., Fecker L., Timpl R., Ekblom P. Differential expression of laminin A and B chains during development of embryonic mouse organs. Development. 1990 Nov;110(3):823–837. doi: 10.1242/dev.110.3.823. [DOI] [PubMed] [Google Scholar]
  35. Klein G., Langegger M., Timpl R., Ekblom P. Role of laminin A chain in the development of epithelial cell polarity. Cell. 1988 Oct 21;55(2):331–341. doi: 10.1016/0092-8674(88)90056-6. [DOI] [PubMed] [Google Scholar]
  36. Kodama H. A., Amagai Y., Koyama H., Kasai S. A new preadipose cell line derived from newborn mouse calvaria can promote the proliferation of pluripotent hemopoietic stem cells in vitro. J Cell Physiol. 1982 Jul;112(1):89–95. doi: 10.1002/jcp.1041120114. [DOI] [PubMed] [Google Scholar]
  37. Koenigsmann M., Griffin J. D., DiCarlo J., Cannistra S. A. Myeloid and erythroid progenitor cells from normal bone marrow adhere to collagen type I. Blood. 1992 Feb 1;79(3):657–665. [PubMed] [Google Scholar]
  38. Koukoulis G. K., Gould V. E., Bhattacharyya A., Gould J. E., Howeedy A. A., Virtanen I. Tenascin in normal, reactive, hyperplastic, and neoplastic tissues: biologic and pathologic implications. Hum Pathol. 1991 Jul;22(7):636–643. doi: 10.1016/0046-8177(91)90285-w. [DOI] [PubMed] [Google Scholar]
  39. Kupiec-Weglinski J. W., De Sousa M. Lymphocyte traffic is modified in vivo by anti-laminin antibody. Immunology. 1991 Feb;72(2):312–313. [PMC free article] [PubMed] [Google Scholar]
  40. Lanotte M., Schor S., Dexter T. M. Collagen gels as a matrix for haemopoiesis. J Cell Physiol. 1981 Feb;106(2):269–277. doi: 10.1002/jcp.1041060213. [DOI] [PubMed] [Google Scholar]
  41. Liesveld J. L., Abboud C. N., Duerst R. E., Ryan D. H., Brennan J. K., Lichtman M. A. Characterization of human marrow stromal cells: role in progenitor cell binding and granulopoiesis. Blood. 1989 May 15;73(7):1794–1800. [PubMed] [Google Scholar]
  42. Lochter A., Vaughan L., Kaplony A., Prochiantz A., Schachner M., Faissner A. J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth. J Cell Biol. 1991 Jun;113(5):1159–1171. doi: 10.1083/jcb.113.5.1159. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Long M. W., Dixit V. M. Thrombospondin functions as a cytoadhesion molecule for human hematopoietic progenitor cells. Blood. 1990 Jun 15;75(12):2311–2318. [PubMed] [Google Scholar]
  44. Lotz M. M., Burdsal C. A., Erickson H. P., McClay D. R. Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response. J Cell Biol. 1989 Oct;109(4 Pt 1):1795–1805. doi: 10.1083/jcb.109.4.1795. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Mann K., Deutzmann R., Timpl R. Characterization of proteolytic fragments of the laminin-nidogen complex and their activity in ligand-binding assays. Eur J Biochem. 1988 Dec 1;178(1):71–80. doi: 10.1111/j.1432-1033.1988.tb14430.x. [DOI] [PubMed] [Google Scholar]
  46. Minty A. J., Alonso S., Guénet J. L., Buckingham M. E. Number and organization of actin-related sequences in the mouse genome. J Mol Biol. 1983 Jun 15;167(1):77–101. doi: 10.1016/s0022-2836(83)80035-7. [DOI] [PubMed] [Google Scholar]
  47. Miyake K., Medina K. L., Hayashi S., Ono S., Hamaoka T., Kincade P. W. Monoclonal antibodies to Pgp-1/CD44 block lympho-hemopoiesis in long-term bone marrow cultures. J Exp Med. 1990 Feb 1;171(2):477–488. doi: 10.1084/jem.171.2.477. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Murphy-Ullrich J. E., Lightner V. A., Aukhil I., Yan Y. Z., Erickson H. P., Hök M. Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J Cell Biol. 1991 Nov;115(4):1127–1136. doi: 10.1083/jcb.115.4.1127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Natali P. G., Nicotra M. R., Bigotti A., Botti C., Castellani P., Risso A. M., Zardi L. Comparative analysis of the expression of the extracellular matrix protein tenascin in normal human fetal, adult and tumor tissues. Int J Cancer. 1991 Apr 1;47(6):811–816. doi: 10.1002/ijc.2910470603. [DOI] [PubMed] [Google Scholar]
  50. Nies D. E., Hemesath T. J., Kim J. H., Gulcher J. R., Stefansson K. The complete cDNA sequence of human hexabrachion (Tenascin). A multidomain protein containing unique epidermal growth factor repeats. J Biol Chem. 1991 Feb 15;266(5):2818–2823. [PubMed] [Google Scholar]
  51. Nörenberg U., Wille H., Wolff J. M., Frank R., Rathjen F. G. The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs. Neuron. 1992 May;8(5):849–863. doi: 10.1016/0896-6273(92)90199-n. [DOI] [PubMed] [Google Scholar]
  52. Oliver N., Newby R. F., Furcht L. T., Bourgeois S. Regulation of fibronectin biosynthesis by glucocorticoids in human fibrosarcoma cells and normal fibroblasts. Cell. 1983 May;33(1):287–296. doi: 10.1016/0092-8674(83)90357-4. [DOI] [PubMed] [Google Scholar]
  53. Patel V. P., Lodish H. F. A fibronectin matrix is required for differentiation of murine erythroleukemia cells into reticulocytes. J Cell Biol. 1987 Dec;105(6 Pt 2):3105–3118. doi: 10.1083/jcb.105.6.3105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Paulsson M., Aumailley M., Deutzmann R., Timpl R., Beck K., Engel J. Laminin-nidogen complex. Extraction with chelating agents and structural characterization. Eur J Biochem. 1987 Jul 1;166(1):11–19. doi: 10.1111/j.1432-1033.1987.tb13476.x. [DOI] [PubMed] [Google Scholar]
  55. Prieto A. L., Andersson-Fisone C., Crossin K. L. Characterization of multiple adhesive and counteradhesive domains in the extracellular matrix protein cytotactin. J Cell Biol. 1992 Nov;119(3):663–678. doi: 10.1083/jcb.119.3.663. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Probstmeier R., Martini R., Schachner M. Expression of J1/tenascin in the crypt-villus unit of adult mouse small intestine: implications for its role in epithelial cell shedding. Development. 1990 Jun;109(2):313–321. doi: 10.1242/dev.109.2.313. [DOI] [PubMed] [Google Scholar]
  57. Roldán E., García-Pardo A., Brieva J. A. VLA-4-fibronectin interaction is required for the terminal differentiation of human bone marrow cells capable of spontaneous and high rate immunoglobulin secretion. J Exp Med. 1992 Jun 1;175(6):1739–1747. doi: 10.1084/jem.175.6.1739. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Russell S. B., Trupin J. S., Myers J. C., Broquist A. H., Smith J. C., Myles M. E., Russell J. D. Differential glucocorticoid regulation of collagen mRNAs in human dermal fibroblasts. Keloid-derived and fetal fibroblasts are refractory to down-regulation. J Biol Chem. 1989 Aug 15;264(23):13730–13735. [PubMed] [Google Scholar]
  59. Rüegg C. R., Chiquet-Ehrismann R., Alkan S. S. Tenascin, an extracellular matrix protein, exerts immunomodulatory activities. Proc Natl Acad Sci U S A. 1989 Oct;86(19):7437–7441. doi: 10.1073/pnas.86.19.7437. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Saga Y., Tsukamoto T., Jing N., Kusakabe M., Sakakura T. Murine tenascin: cDNA cloning, structure and temporal expression of isoforms. Gene. 1991 Aug 15;104(2):177–185. doi: 10.1016/0378-1119(91)90248-a. [DOI] [PubMed] [Google Scholar]
  61. Siczkowski M., Clarke D., Gordon M. Y. Binding of primitive hematopoietic progenitor cells to marrow stromal cells involves heparan sulfate. Blood. 1992 Aug 15;80(4):912–919. [PubMed] [Google Scholar]
  62. Siri A., Carnemolla B., Saginati M., Leprini A., Casari G., Baralle F., Zardi L. Human tenascin: primary structure, pre-mRNA splicing patterns and localization of the epitopes recognized by two monoclonal antibodies. Nucleic Acids Res. 1991 Feb 11;19(3):525–531. doi: 10.1093/nar/19.3.525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Sorokin L. M., Conzelmann S., Ekblom P., Battaglia C., Aumailley M., Timpl R. Monoclonal antibodies against laminin A chain fragment E3 and their effects on binding to cells and proteoglycan and on kidney development. Exp Cell Res. 1992 Jul;201(1):137–144. doi: 10.1016/0014-4827(92)90357-e. [DOI] [PubMed] [Google Scholar]
  64. Spooncer E., Gallagher J. T., Krizsa F., Dexter T. M. Regulation of haemopoiesis in long-term bone marrow cultures. IV. Glycosaminoglycan synthesis and the stimulation of haemopoiesis by beta-D-xylosides. J Cell Biol. 1983 Feb;96(2):510–514. doi: 10.1083/jcb.96.2.510. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Spring J., Beck K., Chiquet-Ehrismann R. Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments. Cell. 1989 Oct 20;59(2):325–334. doi: 10.1016/0092-8674(89)90294-8. [DOI] [PubMed] [Google Scholar]
  66. Suda T., Dexter T. M. Effect of hydrocortisone on long-term human marrow cultures. Br J Haematol. 1981 Aug;48(4):661–664. doi: 10.1111/j.1365-2141.1981.00661.x. [DOI] [PubMed] [Google Scholar]
  67. Teixidó J., Hemler M. E., Greenberger J. S., Anklesaria P. Role of beta 1 and beta 2 integrins in the adhesion of human CD34hi stem cells to bone marrow stroma. J Clin Invest. 1992 Aug;90(2):358–367. doi: 10.1172/JCI115870. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Timpl R. Structure and biological activity of basement membrane proteins. Eur J Biochem. 1989 Apr 1;180(3):487–502. doi: 10.1111/j.1432-1033.1989.tb14673.x. [DOI] [PubMed] [Google Scholar]
  69. Tsai S., Patel V., Beaumont E., Lodish H. F., Nathan D. G., Sieff C. A. Differential binding of erythroid and myeloid progenitors to fibroblasts and fibronectin. Blood. 1987 Jun;69(6):1587–1594. [PubMed] [Google Scholar]
  70. Verfaillie C. M., McCarthy J. B., McGlave P. B. Differentiation of primitive human multipotent hematopoietic progenitors into single lineage clonogenic progenitors is accompanied by alterations in their interaction with fibronectin. J Exp Med. 1991 Sep 1;174(3):693–703. doi: 10.1084/jem.174.3.693. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Verfaillie C. M., McCarthy J. B., McGlave P. B. Mechanisms underlying abnormal trafficking of malignant progenitors in chronic myelogenous leukemia. Decreased adhesion to stroma and fibronectin but increased adhesion to the basement membrane components laminin and collagen type IV. J Clin Invest. 1992 Oct;90(4):1232–1241. doi: 10.1172/JCI115985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Weinstein R., Riordan M. A., Wenc K., Kreczko S., Zhou M., Dainiak N. Dual role of fibronectin in hematopoietic differentiation. Blood. 1989 Jan;73(1):111–116. [PubMed] [Google Scholar]
  73. Weller A., Beck S., Ekblom P. Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis. J Cell Biol. 1991 Jan;112(2):355–362. doi: 10.1083/jcb.112.2.355. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Whitlock C. A., Witte O. N. Long-term culture of B lymphocytes and their precursors from murine bone marrow. Proc Natl Acad Sci U S A. 1982 Jun;79(11):3608–3612. doi: 10.1073/pnas.79.11.3608. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Williams D. A., Rios M., Stephens C., Patel V. P. Fibronectin and VLA-4 in haematopoietic stem cell-microenvironment interactions. Nature. 1991 Aug 1;352(6334):438–441. doi: 10.1038/352438a0. [DOI] [PubMed] [Google Scholar]
  76. Yang-Yen H. F., Chambard J. C., Sun Y. L., Smeal T., Schmidt T. J., Drouin J., Karin M. Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction. Cell. 1990 Sep 21;62(6):1205–1215. doi: 10.1016/0092-8674(90)90396-v. [DOI] [PubMed] [Google Scholar]
  77. Zuckerman K. S., Rhodes R. K., Goodrum D. D., Patel V. R., Sparks B., Wells J., Wicha M. S., Mayo L. A. Inhibition of collagen deposition in the extracellular matrix prevents the establishment of a stroma supportive of hematopoiesis in long-term murine bone marrow cultures. J Clin Invest. 1985 Mar;75(3):970–975. doi: 10.1172/JCI111798. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES