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. 1977 Aug 1;74(2):649–654. doi: 10.1083/jcb.74.2.649

Quantitation of a transformation-sensitive, adhesive cell surface glycoprotein. Decrease of several untransformed permanent cell lines

PMCID: PMC2110070  PMID: 328519

Abstract

We have quantitated the transformation-sensitive, cell surface LETS glycoprotein on many untransformed cell types. By SDS-polyacrylamide gel electrophoresis, this trypsin-sensitive iodinatable glycoprotein comprises 1-3% of total cellular protein of the seven early passage cell types tested. In contrast, it constitutes less than 0.15% of the protein in four of six continuous cell lines. This decrease is reflected in alterations both in [14C]glucosamine labeling and in the immunofluorescent staining of early passage vs. these four permanent cell lines. These results help to clarify previous experiments in which CSP, a purified LETS protein, partially restored a fibroblastic phenotype to cells transformed by tumor viruses. These findings also indicate that a major decrease in this cell surface glycoprotein can occur in the establishment of a continuous cell line without resulting in cellular transformation.

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Selected References

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  1. Aaronson S. A., Todaro G. J. Basis for the acquisition of malignant potential by mouse cells cultivated in vitro. Science. 1968 Nov 29;162(3857):1024–1026. doi: 10.1126/science.162.3857.1024. [DOI] [PubMed] [Google Scholar]
  2. Aaronson S. A., Weaver C. A. Characterization of murine sarcoma virus (Kirsten) transformation of mouse and human cells. J Gen Virol. 1971 Nov;13(2):245–252. doi: 10.1099/0022-1317-13-2-245. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Davies P., Shizuta Y., Olden K., Gallo M., Pastan I. Phosphorylation of filamin and other proteins in cultured fibroblasts. Biochem Biophys Res Commun. 1977 Jan 10;74(1):300–307. doi: 10.1016/0006-291x(77)91408-5. [DOI] [PubMed] [Google Scholar]
  5. Diamond L. Two spontaneously transformed cell lines derived from the same hamster embryo culture. Int J Cancer. 1967 Mar 15;2(2):143–152. doi: 10.1002/ijc.2910020209. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. HAYFLICK L. THE LIMITED IN VITRO LIFETIME OF HUMAN DIPLOID CELL STRAINS. Exp Cell Res. 1965 Mar;37:614–636. doi: 10.1016/0014-4827(65)90211-9. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Huu Duc-Nguyen, Rosenblum E. N., Zeigel R. F. Persistent infection of a rat kidney cell line with Rauscher murine leukemia virus. J Bacteriol. 1966 Oct;92(4):1133–1140. doi: 10.1128/jb.92.4.1133-1140.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. 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]
  12. Hynes R. O., Destree A. T., Mautner V. Spatial organization at the cell surface. Prog Clin Biol Res. 1976;9:189–201. [PubMed] [Google Scholar]
  13. Jainchill J. L., Aaronson S. A., Todaro G. J. Murine sarcoma and leukemia viruses: assay using clonal lines of contact-inhibited mouse cells. J Virol. 1969 Nov;4(5):549–553. doi: 10.1128/jvi.4.5.549-553.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  15. 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]
  16. Pouysségur J. M., Pastan I. Mutants of Balb/c 3T3 fibroblasts defective in adhesiveness to substratum: evidence for alteration in cell surface proteins. Proc Natl Acad Sci U S A. 1976 Feb;73(2):544–548. doi: 10.1073/pnas.73.2.544. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. STOKER M., MACPHERSON I. SYRIAN HAMSTER FIBROBLAST CELL LINE BHK21 AND ITS DERIVATIVES. Nature. 1964 Sep 26;203:1355–1357. doi: 10.1038/2031355a0. [DOI] [PubMed] [Google Scholar]
  19. Stone K. R., Smith R. E., Joklik W. K. Changes in membrane polypeptides that occur when chick embryo fibroblasts and NRK cells are transformed with avian sarcoma viruses. Virology. 1974 Mar;58(1):86–100. doi: 10.1016/0042-6822(74)90143-3. [DOI] [PubMed] [Google Scholar]
  20. TODARO G. J., GREEN H. Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines. J Cell Biol. 1963 May;17:299–313. doi: 10.1083/jcb.17.2.299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Wang K., Ash J. F., Singer S. J. Filamin, a new high-molecular-weight protein found in smooth muscle and non-muscle cells. Proc Natl Acad Sci U S A. 1975 Nov;72(11):4483–4486. doi: 10.1073/pnas.72.11.4483. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. 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]
  23. Yamada K. M., Ohanian S. H., Pastan I. Cell surface protein decreases microvilli and ruffles on transformed mouse and chick cells. Cell. 1976 Oct;9(2):241–245. doi: 10.1016/0092-8674(76)90115-x. [DOI] [PubMed] [Google Scholar]
  24. Yamada K. M., Pastan I. The relationship between cell surface protein and glucose and alpha-aminoisobutyrate transport in transformed chick and mouse cells. J Cell Physiol. 1976 Dec;89(4):827–829. doi: 10.1002/jcp.1040890450. [DOI] [PubMed] [Google Scholar]
  25. Yamada K. M., Weston J. A. The synthesis, turnover, and artificial restoration of a major cell surface glycoprotein. Cell. 1975 May;5(1):75–81. doi: 10.1016/0092-8674(75)90094-x. [DOI] [PubMed] [Google Scholar]
  26. 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]
  27. 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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