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. 1977 Aug 1;74(2):453–467. doi: 10.1083/jcb.74.2.453

Changes in the distribution of a major fibroblast protein, fibronectin, during mitosis and interphase

S Stenman, J Wartiovaara, A Vaheri
PMCID: PMC2110083  PMID: 328516

Abstract

The distribution of a major fibroblast protein, fibronectin, was studied by immunofluorescence and immunoscanning electron microscopy in cultures of human and chicken fibroblasts during different phases of the cell cycle. The main findings were: (a) In interphase cells, the intensity of surface-associated fibronectin fluorescence correlated with that of intracellular fibronectin fluorescence. (b) The intensity of the fluorescence of both surface-associated and intracellular fibronectins was not changed in cells that were synthesizing DNA. (c) Mitotic cells had reduced amounts of surface-associated but not of intracellular fibronectin. The surface fibronectin that remained on meta-, ana-, or telophase cells had a distinct punctate distribution and was also localized to strands attaching the cells to the substratum. Fibronectin strands first reappeared on the surface of flattening cytoplasmic parts of telophase cells. (d) Fibronectin was also detected in extracellular fibrillar material on the growth substratum, particularly around dividing cells. Thus, surface-associated fibrillar fibronectin was present during G(1), S, and G(2) but in cells undergoing mitosis the distribution was altered and the amount appeared to be reduced. The observations on the distribution of surface-associated fibronectin suggest that rather than being involved in growth control this fibronectin plays a structural role in interactions of cells with the environment.

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Selected References

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

  1. Gahmberg C. G., Hakomori S. I. Altered growth behavior of malignant cells associated with changes in externally labeled glycoprotein and glycolipid. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3329–3333. doi: 10.1073/pnas.70.12.3329. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Gahmberg C. G., Hakomori S. Organization of glycolipids and glycoproteins in surface membranes: dependency on cell cycle and on transformation. Biochem Biophys Res Commun. 1974 Jul 10;59(1):283–291. doi: 10.1016/s0006-291x(74)80204-4. [DOI] [PubMed] [Google Scholar]
  3. Hogg N. M. A comparison of membrane proteins of normal and transformed cells by lactoperoxidase labeling. Proc Natl Acad Sci U S A. 1974 Feb;71(2):489–492. doi: 10.1073/pnas.71.2.489. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hunt R. C., Gold E., Brown J. C. Cell cycle dependent exposure of a high molecular weight protein on the surface of mouse L cells. Biochim Biophys Acta. 1975 Dec 16;413(3):453–458. doi: 10.1016/0005-2736(75)90128-5. [DOI] [PubMed] [Google Scholar]
  5. Hynes R. O. Alteration of cell-surface proteins by viral transformation and by proteolysis. Proc Natl Acad Sci U S A. 1973 Nov;70(11):3170–3174. doi: 10.1073/pnas.70.11.3170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hynes R. O., Bye J. M. Density and cell cycle dependence of cell surface proteins in hamster fibroblasts. Cell. 1974 Oct;3(2):113–120. doi: 10.1016/0092-8674(74)90114-7. [DOI] [PubMed] [Google Scholar]
  7. Keski-Oja J., Mosher D. F., Vaheri A. Cross-linking of a major fibroblast surface-associated glycoprotein (fibronectin) catalyzed by blood coagulation factor XIII. Cell. 1976 Sep;9(1):29–35. doi: 10.1016/0092-8674(76)90049-0. [DOI] [PubMed] [Google Scholar]
  8. Keski-Oja J., Mosher D. F., Vaheri A. Dimeric character of fibronectin, a major cell surface-associated glycoprotein. Biochem Biophys Res Commun. 1977 Jan 24;74(2):699–706. doi: 10.1016/0006-291x(77)90359-x. [DOI] [PubMed] [Google Scholar]
  9. Keski-Oja J., Vaheri A., Ruoslahti E. Fibroblast surface antigen (SF): the external glycoprotein lost in proteolytic stimulation and maligant transfromation. Int J Cancer. 1976 Feb 15;17(2):261–269. doi: 10.1002/ijc.2910170215. [DOI] [PubMed] [Google Scholar]
  10. Kuusela P., Ruoslahti E., Engvall E., Vaheri A. Immunological interspecies cross-reactions of fibroblast surface antigen (fibronectin). Immunochemistry. 1976 Aug;13(8):639–642. doi: 10.1016/0019-2791(76)90203-2. [DOI] [PubMed] [Google Scholar]
  11. Lambert W. C., Studzinski G. P. Thymidine as a synchronizing agent. II. Partial recovery of HeLa cells from unbalanced growth. J Cell Physiol. 1969 Jun;73(3):261–266. doi: 10.1002/jcp.1040730310. [DOI] [PubMed] [Google Scholar]
  12. Linder E., Vaheri A., Ruoslahti E., Wartiovaara J. Distribution of fibroblast surface antigen in the developing chick embryo. J Exp Med. 1975 Jul 1;142(1):41–49. doi: 10.1084/jem.142.1.41. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Linthicum D. S., Sell S., Wagner R. M., Trefts P. Scanning immunoelectron microscopy of mouse B and T lymphocytes. Nature. 1974 Nov 8;252(5479):173–175. doi: 10.1038/252173a0. [DOI] [PubMed] [Google Scholar]
  14. Mosesson M. W., Chen A. B., Huseby R. M. The cold-insoluble globulin of human plasma: studies of its essential structural features. Biochim Biophys Acta. 1975 Apr 29;386(2):509–524. doi: 10.1016/0005-2795(75)90294-9. [DOI] [PubMed] [Google Scholar]
  15. Mosher D. F. Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor. J Biol Chem. 1975 Aug 25;250(16):6614–6621. [PubMed] [Google Scholar]
  16. Pearlstein E. Plasma membrane glycoprotein which mediates adhesion of fibroblasts to collagen. Nature. 1976 Aug 5;262(5568):497–500. doi: 10.1038/262497a0. [DOI] [PubMed] [Google Scholar]
  17. Pollack R., Osborn M., Weber K. Patterns of organization of actin and myosin in normal and transformed cultured cells. Proc Natl Acad Sci U S A. 1975 Mar;72(3):994–998. doi: 10.1073/pnas.72.3.994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Ruoslahti E., Vaheri A. Interaction of soluble fibroblast surface antigen with fribrinogen and fibrin. J Exp Med. 1975 Feb 1;141(2):497–501. doi: 10.1084/jem.141.2.497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ruoslahti E., Vaheri A., Kuusela P., Linder E. Fibroblast surface antigen: a new serum protein. Biochim Biophys Acta. 1973 Oct 18;322(2):352–358. doi: 10.1016/0005-2795(73)90310-3. [DOI] [PubMed] [Google Scholar]
  20. Sanger J. W. Changing patterns of actin localization during cell division. Proc Natl Acad Sci U S A. 1975 May;72(5):1913–1916. doi: 10.1073/pnas.72.5.1913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Studzinski G. P., Lambert W. C. Thymidine as a synchronizing agent. I. Nucleic acid and protein formation in synchronous HeLa cultures treated with excess thymidine. J Cell Physiol. 1969 Apr;73(2):109–117. doi: 10.1002/jcp.1040730204. [DOI] [PubMed] [Google Scholar]
  22. Teng N. N., Bo Chen L. The role of surface proteins in cell proliferation as studied with thrombin and other proteases. Proc Natl Acad Sci U S A. 1975 Feb;72(2):413–417. doi: 10.1073/pnas.72.2.413. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Vaheri A., Ruoslahti E. Disappearance of a major cell-type specific surface glycoprotein antigen (SF) after transformation of fibroblasts by Rous sarcoma virus. Int J Cancer. 1974 May 15;13(5):579–586. doi: 10.1002/ijc.2910130502. [DOI] [PubMed] [Google Scholar]
  24. Vaheri A., Ruoslahti E. Fibroblast surface antigen produced but not retained by virus-transformed human cells. J Exp Med. 1975 Aug 1;142(2):530–535. doi: 10.1084/jem.142.2.530. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Vaheri A., Ruoslahti E., Hovi T., Nordling S. Stimulation of density-inhibited cell cultures by insulin. J Cell Physiol. 1973 Jun;81(3):355–364. doi: 10.1002/jcp.1040810308. [DOI] [PubMed] [Google Scholar]
  26. Vaheri A., Ruoslahti E., Linder E., Wartiovaara J., Keski-Oja J., Kuusela P., Saksela O. Fibroblast surface antigen (SF): molecular properties, distribution in vitro and in vivo, and altered expression in transformed cells. J Supramol Struct. 1976;4(1):63–70. doi: 10.1002/jss.400040107. [DOI] [PubMed] [Google Scholar]
  27. Vaheri A., Ruoslahti E., Westermark B., Ponten J. A common cell-type specific surface antigen in cultured human glial cells and fibroblasts: loss in malignant cells. J Exp Med. 1976 Jan 1;143(1):64–72. doi: 10.1084/jem.143.1.64. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Wartiovaara J., Linder E., Ruoslahti E., Vaheri A. Distribution of fibroblast surface antigen: association with fibrillar structures of normal cells and loss upon viral transformation. J Exp Med. 1974 Dec 1;140(6):1522–1533. doi: 10.1084/jem.140.6.1522. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Wartiovaara J., Stenman S., Vaheri A. Changes in expression of fibroblast surface antigen (SFA) during cytodifferentiation and heterokaryon formation. Differentiation. 1976 Jun 4;5(2-3):85–89. doi: 10.1111/j.1432-0436.1976.tb00896.x. [DOI] [PubMed] [Google Scholar]
  30. Yamada K. M., Yamada S. S., Pastan I. The major cell surface glycoprotein of chick embryo fibroblasts is an agglutinin. Proc Natl Acad Sci U S A. 1975 Aug;72(8):3158–3162. doi: 10.1073/pnas.72.8.3158. [DOI] [PMC free article] [PubMed] [Google Scholar]

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