Cell surface protein partially restores morphology, adhesiveness, and contact inhibition of movement to transformed fibroblasts
- PMID: 177979
- PMCID: PMC430233
- DOI: 10.1073/pnas.73.4.1217
Cell surface protein partially restores morphology, adhesiveness, and contact inhibition of movement to transformed fibroblasts
Abstract
We have isolated the major cell surface glycoprotein of chick embryo fibroblasts, CSP, and added it to a variety of transformed cells in vitro. The transformed cells become more elongated, often more flattened, and show increased adhesion to the substratum. Several transformed cell lines also align in striking parallel arrays. This alignment is characterized by a decrease in the amount of nuclear overlapping, probably indicating restoration of contact inhibition of movement. The morphological changes are antagonized by antibody to CSP. These effects of CSP are not associated with an elevation of cellular 3':5'-cyclic AMP. Moreover, the morphological reversion is not accompanied by an alteration in growth properties. Our results are consistent with a role for CSP in cell adhesion and morphology but not in growth control.
Similar articles
-
Transformation-sensitive cell surface protein: isolation, characterization, and role in cellular morphology and adhesion.Ann N Y Acad Sci. 1978 Jun 20;312:256-77. doi: 10.1111/j.1749-6632.1978.tb16807.x. Ann N Y Acad Sci. 1978. PMID: 291364
-
Microfilament bundles and cell shape are related to adhesiveness to substratum and are dissociable from growth control in cultured fibroblasts.Cell. 1977 Mar;10(3):375-80. doi: 10.1016/0092-8674(77)90024-1. Cell. 1977. PMID: 557370
-
Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein.Cell. 1977 May;11(1):115-26. doi: 10.1016/0092-8674(77)90322-1. Cell. 1977. PMID: 326414
-
Cellular transformation and the 'morphologic phenotype' of transformed cells.Nature. 1978 Aug 17;274(5672):645-50. doi: 10.1038/274645a0. Nature. 1978. PMID: 209337 Review.
-
LETS glycoprotein: arrangement and function at the cell surface.Birth Defects Orig Artic Ser. 1978;14(2):139-53. Birth Defects Orig Artic Ser. 1978. PMID: 346077 Review.
Cited by
-
Lactoperoxidase-catalysed iodination of surface proteins on human melanoma cells.Br J Cancer. 1978 Jul;38(1):114-21. doi: 10.1038/bjc.1978.170. Br J Cancer. 1978. PMID: 687508 Free PMC article.
-
Requirements for sulfate transport and the diastrophic dysplasia sulfate transporter in fibronectin matrix assembly.J Cell Biol. 2007 Dec 3;179(5):999-1009. doi: 10.1083/jcb.200707150. J Cell Biol. 2007. PMID: 18056413 Free PMC article.
-
Sequence rearrangement and duplication of double stranded fibronectin cDNA probably occurring during cDNA synthesis by AMV reverse transcriptase and Escherichia coli DNA polymerase I.Nucleic Acids Res. 1980 Jul 11;8(13):3055-64. doi: 10.1093/nar/8.13.3055. Nucleic Acids Res. 1980. PMID: 6159581 Free PMC article.
-
Distribution of the LETS protein (fibronectin) in rat cerebellum. An in vitro and in vivo developmental study.Cell Tissue Res. 1981;214(3):491-500. doi: 10.1007/BF00233490. Cell Tissue Res. 1981. PMID: 7214462
-
Fibronectin is chemotactic for CT 26 colon carcinoma cells: sub-lines selected for increased chemotaxis to fibronectin display decreased tumorigenicity and lung colonization.Clin Exp Metastasis. 1998 Nov;16(8):683-91. doi: 10.1023/a:1006572526520. Clin Exp Metastasis. 1998. PMID: 10211981
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources