Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1980 Oct 1;87(1):309–313. doi: 10.1083/jcb.87.1.309

Fibronectin in the developing sea urchin embryo

PMCID: PMC2110722  PMID: 6998990

Abstract

The presence of fibronectin in developing sea urchin embryos was studied uing immunofluorescence staining. The fluorescence pattern indicates that fibronectin is found on the cell surfaces and between cells in the blastula and gastrula stages, indicating that it plays a role in cell adhesion. Its presence on invaginating cells also suggests its involvement in morphogenesis during early development.

Full Text

The Full Text of this article is available as a PDF (544.4 KB).

Selected References

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

  1. Ali I. U., Mautner V., Lanza R., Hynes R. O. Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein. Cell. 1977 May;11(1):115–126. doi: 10.1016/0092-8674(77)90322-1. [DOI] [PubMed] [Google Scholar]
  2. Balian G., Click E. M., Crouch E., Davidson J. M., Bornstein P. Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin. J Biol Chem. 1979 Mar 10;254(5):1429–1432. [PubMed] [Google Scholar]
  3. Critchley D. R., England M. A., Wakely J., Hynes R. O. Distribution of fibronectin in the ectoderm of gastrulating chick embryos. Nature. 1979 Aug 9;280(5722):498–500. doi: 10.1038/280498a0. [DOI] [PubMed] [Google Scholar]
  4. DAN K. Cyto-embryology of echinoderms and amphibia. Int Rev Cytol. 1960;9:321–367. doi: 10.1016/s0074-7696(08)62751-5. [DOI] [PubMed] [Google Scholar]
  5. Gustafson T., Wolpert L. Cellular movement and contact in sea urchin morphogenesis. Biol Rev Camb Philos Soc. 1967 Aug;42(3):442–498. doi: 10.1111/j.1469-185x.1967.tb01482.x. [DOI] [PubMed] [Google Scholar]
  6. Hahn L. H., Yamada K. M. Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1160–1163. doi: 10.1073/pnas.76.3.1160. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. Hynes R. O. Cell surface proteins and malignant transformation. Biochim Biophys Acta. 1976 Apr 30;458(1):73–107. doi: 10.1016/0304-419x(76)90015-9. [DOI] [PubMed] [Google Scholar]
  9. Jockusch B. M., Kelley K. H., Meyer R. K., Burger M. M. An efficient method to produce specific anti-actin. Histochemistry. 1978 Apr 4;55(3):177–184. doi: 10.1007/BF00495757. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Mautner V., Hynes R. O. Surface distribution of LETS protein in relation to the cytoskeleton of normal and transformed cells. J Cell Biol. 1977 Dec;75(3):743–768. doi: 10.1083/jcb.75.3.743. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Perkins M. E., Ji T. H., Hynes R. O. Cross-linking of fibronectin to sulfated proteoglycans at the cell surface. Cell. 1979 Apr;16(4):941–952. doi: 10.1016/0092-8674(79)90109-0. [DOI] [PubMed] [Google Scholar]
  14. Peters K., Richards F. M. Chemical cross-linking: reagents and problems in studies of membrane structure. Annu Rev Biochem. 1977;46:523–551. doi: 10.1146/annurev.bi.46.070177.002515. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. Spiegel E., Spiegel M. The hyaline layer is a collagen-containing extracellular matrix in sea urchin embryos and reaggregating cells. Exp Cell Res. 1979 Oct 15;123(2):434–441. doi: 10.1016/0014-4827(79)90495-6. [DOI] [PubMed] [Google Scholar]
  17. Vaheri A., Alitalo K., Hedman K., Keski-Oja J., Kurkinen M., Wartiovaara J. Fibronectin and the pericellular matrix of normal and transformed adherent cells. Ann N Y Acad Sci. 1978 Jun 20;312:343–353. doi: 10.1111/j.1749-6632.1978.tb16812.x. [DOI] [PubMed] [Google Scholar]
  18. Vaheri A., Mosher D. F. High molecular weight, cell surface-associated glycoprotein (fibronectin) lost in malignant transformation. Biochim Biophys Acta. 1978 Sep 18;516(1):1–25. doi: 10.1016/0304-419x(78)90002-1. [DOI] [PubMed] [Google Scholar]
  19. Vuento M., Vaheri A. Purification of fibronectin from human plasma by affinity chromatography under non-denaturing conditions. Biochem J. 1979 Nov 1;183(2):331–337. doi: 10.1042/bj1830331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wartiovaara J., Leivo I., Virtanen I., Vaheri A., Graham C. F. Cell surface and extracellular matrix glycoprotein fibronectin: expression in embryogenesis and in teratocarcinoma differentiation. Ann N Y Acad Sci. 1978 Jun 20;312:132–141. doi: 10.1111/j.1749-6632.1978.tb16798.x. [DOI] [PubMed] [Google Scholar]
  21. Yamada K. M., Olden K. Fibronectins--adhesive glycoproteins of cell surface and blood. Nature. 1978 Sep 21;275(5677):179–184. doi: 10.1038/275179a0. [DOI] [PubMed] [Google Scholar]
  22. Yamada K. M., Weston J. A. Isolation of a major cell surface glycoprotein from fibroblasts. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3492–3496. doi: 10.1073/pnas.71.9.3492. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Yamada K. M., Yamada S. S., Pastan I. Cell surface protein partially restores morphology, adhesiveness, and contact inhibition of movement to transformed fibroblasts. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1217–1221. doi: 10.1073/pnas.73.4.1217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Zetter B. R., Martin G. R. Expression of a high molecular weight cell surface glycoprotein (LETS protein) by preimplantation mouse embryos and teratocarcinoma stem cells. Proc Natl Acad Sci U S A. 1978 May;75(5):2324–2328. doi: 10.1073/pnas.75.5.2324. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES