Abstract
The distribution of a major glycoprotein (fibronectin) of human fibroblast cultures was studied in immunoelectron microscopy with peroxidase- or ferritin-labeled antibodies. External fibronectin was visualized in pericellular structures, in some areas on the growth substratum, and to a lesser degree in close association with the upper and lower surface membranes of the cell. The pericellular fibronectin- containing structures consisted of amorphous or vaguely fibrillar material forming strands or patches, 50-500 nm in diameter; the structures appeared to mediate distant cell-to-cell and cell-to- substrate contacts. When in close association with the plasma membrane, fibronectin markers were seen as discrete patches. The exact relationship between this form of fibronectin and the plasma membrane, however, remained open. Filamentous material was commonly seen in the cortical cytoplasm under patches of membrane-associated fibronectin. The distribution that we observed is consistent with the proposed roles of fibronectin in cell interactions with neighboring structures and with its presence in vivo as an extracellular glycoprotein in connective tissue matrix and basal laminae.
Full Text
The Full Text of this article is available as a PDF (4.0 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Ames G. F. Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. Membrane, soluble, and periplasmic fractions. J Biol Chem. 1974 Jan 25;249(2):634–644. [PubMed] [Google Scholar]
- Bornstein P., Ash J. F. Cell surface-associated structural proteins in connective tissue cells. Proc Natl Acad Sci U S A. 1977 Jun;74(6):2480–2484. doi: 10.1073/pnas.74.6.2480. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bornstein P. The biosynthesis of collagen. Annu Rev Biochem. 1974;43(0):567–603. doi: 10.1146/annurev.bi.43.070174.003031. [DOI] [PubMed] [Google Scholar]
- Chen L. B., Gallimore P. H., McDougall J. K. Correlation between tumor induction and the large external transformation sensitive protein on the cell surface. Proc Natl Acad Sci U S A. 1976 Oct;73(10):3570–3574. doi: 10.1073/pnas.73.10.3570. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gahmberg C. G., Hakomori S. Surface carbohydrates of hamster fibroblasts. II. Interaction of hamster NIL cell surfaces with Ricinus communis lectin and concanavalin A as revealed by surface galactosyl label. J Biol Chem. 1975 Apr 10;250(7):2447–2451. [PubMed] [Google Scholar]
- Gahmberg C. G., Kiehn D., Hakomori S. Changes in a surface-labelled galactoprotein and in glycolipid concentrations in cells transformed by a temperature-sensitive polyoma virus mutant. Nature. 1974 Mar 29;248(447):413–415. doi: 10.1038/248413a0. [DOI] [PubMed] [Google Scholar]
- Graham J. M., Hynes R. O., Davidson E. A., Bainton D. F. The location of proteins labeled by the 125I-lactoperoxidase system in the NIL 8 hamster fibroblast. Cell. 1975 Apr;4(4):353–365. doi: 10.1016/0092-8674(75)90156-7. [DOI] [PubMed] [Google Scholar]
- 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]
- 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]
- Hynes R. O., Destree A. Extensive disulfide bonding at the mammalian cell surface. Proc Natl Acad Sci U S A. 1977 Jul;74(7):2855–2859. doi: 10.1073/pnas.74.7.2855. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jilek F., Hörmann H. Cold-insoluble globulin, II. Plasminolysis of cold-insoluble globulin. Hoppe Seylers Z Physiol Chem. 1977 Jan;358(1):133–136. [PubMed] [Google Scholar]
- 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]
- Kishida Y., Olsen B. R., Berg R. A., Prockop D. J. Two improved methods for preparing ferritin-protein conjugates for electron microscopy. J Cell Biol. 1975 Feb;64(2):331–339. doi: 10.1083/jcb.64.2.331. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laskey R. A., Mills A. D. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem. 1975 Aug 15;56(2):335–341. doi: 10.1111/j.1432-1033.1975.tb02238.x. [DOI] [PubMed] [Google Scholar]
- Rice R. H., Means G. E. Radioactive labeling of proteins in vitro. J Biol Chem. 1971 Feb 10;246(3):831–832. [PubMed] [Google Scholar]
- Robbins P. W., Wickus G. G., Branton P. E., Gaffney B. J., Hirschberg C. B., Fuchs P., Blumberg P. The chick fibroblast cell surface after transformation by Rous sarcoma virus. Cold Spring Harb Symp Quant Biol. 1975;39(Pt 2):1173–1180. doi: 10.1101/sqb.1974.039.01.135. [DOI] [PubMed] [Google Scholar]
- 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]
- Russell W. C., Newman C., Williamson D. H. A simple cytochemical technique for demonstration of DNA in cells infected with mycoplasmas and viruses. Nature. 1975 Feb 6;253(5491):461–462. doi: 10.1038/253461a0. [DOI] [PubMed] [Google Scholar]
- 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]
- 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]