Revisão Revisado por pares

A LARGE GLYCOPROTEIN LOST FROM THE SURFACES OF TRANSFORMED CELLS*

1978; Wiley; Volume: 312; Issue: 1 Linguagem: Inglês

10.1111/j.1749-6632.1978.tb16811.x

ISSN

1749-6632

Autores

Richard O. Hynes, Imran Ali, Antonia T. Destree, Vivien Mautner, Margaret Perkins, Donald R. Senger, Denisa D. Wagner, Karen Kaye Smith,

Tópico(s)

Advanced Fluorescence Microscopy Techniques

Resumo

Annals of the New York Academy of SciencesVolume 312, Issue 1 p. 317-342 A LARGE GLYCOPROTEIN LOST FROM THE SURFACES OF TRANSFORMED CELLS* R. O. Hynes, R. O. Hynes Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this authorI. U. Ali, I. U. Ali Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this authorA. T. Destree, A. T. Destree Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this authorV. Mautner, V. Mautner Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this authorM. E. Perkins, M. E. Perkins Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139 Recipient of a Damon Runyon-Walter Winchell Postdoctoral Fellowship.Search for more papers by this authorD. R. Senger, D. R. Senger Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139 Recipient of a National Institutes of Health Postdoctoral Fellowship.Search for more papers by this authorD. D. Wagner, D. D. Wagner Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this authorK. K. Smith, K. K. Smith The Rockefeller University New York, New York 10021 Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this author R. O. Hynes, R. O. Hynes Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this authorI. U. Ali, I. U. Ali Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this authorA. T. Destree, A. T. Destree Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this authorV. Mautner, V. Mautner Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this authorM. E. Perkins, M. E. Perkins Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139 Recipient of a Damon Runyon-Walter Winchell Postdoctoral Fellowship.Search for more papers by this authorD. R. Senger, D. R. Senger Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139 Recipient of a National Institutes of Health Postdoctoral Fellowship.Search for more papers by this authorD. D. Wagner, D. D. Wagner Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this authorK. K. Smith, K. K. Smith The Rockefeller University New York, New York 10021 Department of Biology and Center for Cancer Research Massachusetts Institute of Technology Cambridge, Massachusetts 02139Search for more papers by this author First published: June 1978 https://doi.org/10.1111/j.1749-6632.1978.tb16811.xCitations: 109 * Supported by Grants CA 14051 and CA 17007 from the National Institutes of Health and by Grant VC-258 from the American Cancer Society. AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 Hynes, R. O. 1973. Alteration of cell-surface proteins by viral transformation and by proteolysis. Proc. Nat. Acad. Sci. USA 70: 3170–3174. 2 Wickus, G. G., P. E. Branton & P. W. Robbins. 1974. Rous sarcoma virus transformation of the chick cell surface. In Control of Proliferation in Animal Cells. B. Clarkson & R. Baserga, Eds.: 541–546. Cold Spring Harbor Laboratory. Cold Spring Harbor , N.y. . 3 Hogg, N. M. 1974. A comparison of membrane proteins of normal and transformed cells by lactoperoxidase labelling. Proc. Nat. Acad. Sci. USA 71: 489–492. 4 Gahmberg, C. G., D. Kiehn & S. Hakomori. 1974. Changes in a surface-labelled galactoprotein and in glycolipid concentrations in cells transformed by a temperature-sensitive polyoma virus mutant. Nature (London) 248: 413–415. 5 Stone, K. R., R. E. Smith & W. K. Joklik. 1974. Changes in membrane polypeptides that occur when chick embryo fibroblasts and NRK cells are transformed with avian sarcoma viruses. Virology 58: 86–100. 6 Hynes, R. O. 1976. Cell surface proteins and malignant transformation. BBA Rev. Cancer 458: 73–107. 7 Hynes, R. O. 1974. Role of surface alterations in cell transformation: the importance of proteases and surface proteins. Cell 1: 147–156. 8 Hynes, R. O. & J. M. Bye. 1974. Density and cell cycle dependence of cell surface proteins in hamster fibroblasts. Cell 3: 113–120. 9 Graham, J. M., R. O. Hynes, E. A. Davidson & D. F. Bainton. 1975. The location of proteins labelled by the 125I-lactoperoxidase system in the NIL8 hamster fibroblast. Cell 4: 353–365. 9a Graham, J. M., R. O. Hynes, C. Rowlatt & J. K. Sandall. This monograph. 10 Ruoslahti, E. & A. Vaheri. 1974. Novel human serum protein from fibroblast plasma membrane. Nature (London) 248: 789–791. 11 Vaheri, A. & E. Ruoslahti. 1974. Disappearance of a major cell-type specific surface glycoprotein antigen (SF) after transformation of fibroblasts by Rous sarcoma virus. Int. J. Cancer 13: 579–586. 12 Wartiovaara, J., E. Linder, E. Ruoslahti & A. Vaheri. 1975. Distribution of fibroblast surface antigen. Association with fibrillar structures of normal cells and loss upon viral transformation. J. Exp. Med. 140: 1522–1533. 13 Hynes, R. O., A. T. Destree & V. M. Mautner. 1976. Spatial organization at the cell surface. In Membranes and Neoplasia: New Approaches and Strategies. V. T. Marchesi, Ed.: 189–201. Alan R. Liss, Inc. New York , N.y. . 14 Keski-Oja, J., A. Vaheri & E. Ruoslahti. 1976. Fibroblast surface antigen (SF): the external glycoprotein lost in proteolytic stimulation and malignant transformation. Int. J. Cancer 17: 261–269. 15 Ruoslahti, E. & A. Vaheri. 1975. Interaction of soluble fibroblast surface antigen with fibrinogen and fibrin. J. Exp. Med. 141: 497–501. 16 Mosesson, M. W. & R. A. Umfleet. 1970. The cold-insoluble globulin of human plasma. J. Biol. Chem. 245: 5728–5736. 17 Mosher, D. F. 1975. Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor. J. Biol. Chem. 250: 6614–6621. 18 Mosesson, M. W., A. B. Chen & R. M. Huseby. 1975. The cold-insoluble globulin of human plasma: studies of its essential structural features. Biochim. Biophys. Acta 386: 509–524. 19 Weston, J. A. & K. L. Hendricks. 1972. Reversible transformation by urea of contact-inhibited fibroblasts. Proc. Nat. Acad. Sci. USA 69: 3727–3731. 20 Yamada, K. M. & J. A. Weston. 1974. Isolation of a major cell surface glycoprotein from fibroblasts. Proc. Nat. Acad. Sci. USA 71: 3492–3496. 21 Yamada, K. M., S. S. Yamada & I. Pastan. 1976. Cell surface protein partially restores morphology, adhesiveness, and contact inhibition of movement to transformed fibroblasts. Proc. Nat. Acad. Sci. USA 73: 1217–1221. 22 Ali, I. U., V. M. Mautner, R. P. Lanza & R. O. Hynes. 1977. Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein. Cell 11: 115–126. 23 Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227: 680–685. 24 Hynes, R. O. & A. T. Destree. 1977. Extensive disulfide bonding at the mammalian cell surface. Proc. Nat. Acad. Sci. USA 74: 2855–2859. 25 Lazarides, E. 1976. Actin, α-actinin and tropomyosin interaction in the structural organization of actin filaments in non-muscle cells. J. Cell Biol. 68: 202–219. 26 Mautner, V. M. & R. O. Hynes. 1977. Surface distribution of LETS protein in relation to the cytoskeleton of normal and transformed fibroblasts. J. Cell Biol. 75: 743–758. 27 Hynes, R. O. & A. T. Destree. 1978. 10nm Filaments in normal and transformed cells. Cell 13: 151–163. 28 Burridge, K. 1976. Changes in cellular glycoproteins after transformation: identification of specific glycoproteins and antigens in sodium dodecyl sulfate gels. Proc. Nat. Acad. Sci. USA 73: 4457–4461. 29 Brinkley, B. R., G. M. Fuller & D. P. Highfield. 1975. Cytoplasmic microtubules in normal and transformed cells in culture: analysis by tubulin antibody immunofluorescence. Proc. Nat. Acad. Sci. USA 72: 4981–4985. 30 Sheetz, M., R. G. Painter & S. J. Singer. 1976. Relationships of the spectrin complex of human erythrocyte membranes to the actomyosins of muscle cells. Biochemistry 15: 4486–4492. 31 Albrecht-Buehler, G. 1977. The phagokinetic tracks of 3T3 cells. Cell 11: 395–404. 32 Engvall, E. & E. Ruoslahti. 1977. Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int. J. Cancer 20: 1–5. 33 Phillips, D. R. & P. P. Agin. 1977. Platelet plasma membrane glycoproteins. J. Biol. Chem. 252: 2121–2126. 34 Teng, N. N. H. & L. B. Chen. 1975. The role of surface proteins in cell proliferation as studied with thrombin and other proteases. Proc. Nat. Acad. Sci. USA 72: 413–417. 35 Blumberg, P. M. & P. W. Robbins. 1975. Effects of proteases on activation of resting chick embryo fibroblasts and on cell surface proteins. Cell 6: 137–147. 36 Hynes, R. O., J. A. Wyke, J. M. Bye, K. C. Humphryes & E. S. Pearlstein. 1975. Are proteins involved in altering cell surface proteins during viral transformation? In Proteases and Biological Control. E. Reich, E. Shaw & D. B. Rifkin, Eds.: 931–944. Cold Spring Harbor Laboratory. Cold Spring Harbor , N.Y. . 37 Unkeless, J. C., A. Tobia, L. Ossowski, J. P. Quigley, D. B. Rifkin & E. Reich. 1973. An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. I. Chick embryo fibroblast cultures transformed by avian RNA tumor viruses. J. Exp. Med. 137: 85–111. 38 Ossowski, L., J. P. Quigley, G. M. Kellerman & E. Reich. 1973. Fibrinolysis associated with oncogenic transformation. Requirement of plasminogen for correlated changes in cellular morphology, colony formation in agar, and cell migration. J. Exp. Med. 138: 1056–1064. 39 Robbins, P. W., G. G. Wickus, P. E. Branton, B. J. Gaffney, C. B. Hirschberg, P. Fuchs & P. M. Blumberg. 1974. The chick fibroblast cell surface following transformation by Rous sarcoma virus. Cold Spring Harbor Symp. Quant. Biol. 39: 1173–1180. 40 Hynes, R. O. & J. A. Wyke. 1975. Alterations in surface proteins in chicken cells transformed by temperature-sensitive mutants of Rous sarcoma virus. Virology 64: 492–504. 41 Hynes, R. O. & E. S. Pearlstein. 1976. Investigations of the possible role of proteases in altering surface proteins of virally transformed hamster fibroblasts. J. Supramol. Struct. 4: 1–14. 42 Mahdavi, V. & R. O. Hynes. 1978. Effects of cocultivation with transformed cells on surface proteins of normal cells. Biochim. Biophys. Acta. In press. 43 Pearlstein, E. S., R. O. Hynes, L. M. Franks & V. J. Hemmings. 1976. Surface proteins and fibrinolytic activity of cultured mammalian cells. Cancer Res. 36: 1475–1480. 44 Hynes, R. O., A. T. Destree, V. M. Mautner & I. U. Ali. 1977. Synthesis, secretion, and attachment of LETS glycoprotein in normal and transformed cells. J. Supramol. Struct. 7: 397–408. 45 Olden, K. & K. M. Yamada. 1977. Mechanism of the decrease in the major cell surface protein of chick embryo fibroblasts after transformation. Cell 11: 957–969. 46 Pollack, R., M. Osborn & K. Weber. 1975. Patterns of organization of actin and myosin in normal and transformed cultured cells. Proc. Nat. Acad. Sci. USA 72: 994–998. 47 Ash, J. F., P. K. Vogt & S. J. Singer. 1976. Reversion from transformed to normal phenotype by inhibition of protein synthesis in rat kidney cells infected with a temperature-sensitive mutant of Rous sarcoma virus. Proc. Nat. Acad. Sci. USA 73: 3603–3607. 48 Edelman, G. M. & I. Yahara. 1976. Temperature-sensitive changes in surface modulating assemblies of fibroblasts transformed by mutants of Rous sarcoma virus. Proc. Nat. Acad. Sci. USA 73: 2047–2051. 49 Pollack, R. & D. Rifkin. 1975. Actin-containing cables within anchoragedependent rat embryo cells are dissociated by plasmin and trypsin. Cell 6: 495–506. 49a Ali, I. U. 1977. Unpublished results. 50 Carter, S. B. 1967. Haptotaxis and the mechanism of cell motility. Nature (London) 213: 256–260. 51 Harris, A. 1973. Behavior of cultured cells on substrata of variable adhesiveness. Exp. Cell Res. 77: 285–297. 52 Gail, M. H. & C. W. Boone. 1972. Cell-substrate adhesivity. A determinant of cell motility. Exp. Cell Res. 70: 33–40. 52a Ali, I. U. & R. O. Hynes. 1978. Effects of LETS glycoprotein on cell motility. Cell. In press. 53 Hynes, R. O., I. U. Ali, V. M. Mautner & A. T. Destree. 1978. LETS glycoprotein: arrangement and function at the cell surface. In Molecular Basis of Cell-Cell Interactions: 139–153. Alan R. Liss, Inc. New York , N.y. . 54 Chen, L. B., P. H. Gallimore & J. K. McDougall. 1976. Correlation between tumor induction and cell surface LETS protein. Proc. Nat. Acad. Sci. USA 73: 3570–3574. 55 Chen, L. B., N. Maitland, P. H. Gallimore & J. K. McDougall. 1977. Detection of the large external transformation-sensitive protein on some epithelial cells. Exp. Cell Res. 106: 39–46. 56 Schlessinger, J., L. S. Barak, G. G. Hammes, K. M. Yamada, I. Pastan, W. W. Webb & E. L. Elson. 1977. Proc. Nat. Acad. Sci. USA 74: 2909–2913. 57 Albrecht-Buehler, G. & L. B. Chen. 1977. Nature (London) 266: 454–456. 57a Hynes, R. O. & K. K. Smith. 1977. Unpublished results. 58 Nicolson, G. L. 1976. Transmembrane control of the receptors on normal and tumor cells. II. Surface changes associated with transformation and malignancy. Biochim. Biophys. Acta 458: 1–72. 59 Edelman, G. M. 1976. Surface modulation in cell recognition and cell growth. Science 192: 218–226. 60 Berlin, R. D., J. M. Oliver, T. E. Ukena & H. H. Yin. 1974. Control of cell surface topography. Nature (London) 247: 45–46. 61 Ali, I. U. & R. O. Hynes. 1977. Effects of cytochalasin B and colchicine on attachment of a major surface protein of fibroblasts. Biochim. Biophys. Acta 471: 16–24. 61a Wagner, D. D. & R. O. Hynes. In preparation. 62 Chen, A. B., D. K. Amrani & M. W. Mosesson. 1977. Heterogeneity of the coldinsoluble globulin of human plasma (CIg), a circulating cell surface protein. Biochim. Biophys. Acta. 493: 310–324. 63 Jilek, F. & H. Hörmann. 1977. Cold-insoluble globulin. II. Plasminolysis of coldinsoluble globulin. Hoppe-Seyler's Z. Physiol. Chem. 358: 133–136. 64 Eisenman, R., V. M. Vogt & H. Diggelman. 1975. Synthesis of avian RNA tumor virus structural proteins. Cold Spring Harbor Symp. Quant. Biol. 39: 1067–1075. 65 Adams, S. L., M. E. Sobel, B. H. Howard, K. Olden, K. M. Yamada, B. Crombrugghe & I. Pastan. 1977. Levels of translatable mRNAs for cell surface protein, collagen precursors and two membrane proteins in Rous transformed chick embryo fibroblasts. Proc. Nat. Acad. Sci. USA 74: 3399–3403. 66 Chen, L. B., R. C. Gudor, T. T. Sun, A. B. Chen & M. W. Mosesson. 1977. Control of a cell surface major glycoprotein by epidermal growth factor. Science 197: 776–778. 67 Vaheri, A. & E. Ruoslahti. 1975. Fibroblast surface antigen produced but not retained by virus transformed human cells. J. Exp. Med. 142: 530–538. 68 Vahkri, A., E. Ruoslahti, B. Westermark & J. Ponten. 1976. A common cell-type specific surface antigen in cultured human glial cells and fibroblasts: loss in malignant cells. J. Exp. Med. 143: 64–72. 69 Abercrombie, M. 1970. Contact inhibition in tissue culture. In Vitro 6: 128–142. 70 Martz, E., H. M. Phillips & M. S. Steinberg. 1974. Contact inhibition of overlapping and differential cell adhesion: a sufficient model for the control of certain cell culture morphologies. J. Cell Sci. 16: 401–419. 71 Bell, P. B. 1977. Locomotory behavior, contact inhibition, and pattern formation of 3T3 and polyoma virus-transformed 3T3 cells in culture. J. Cell Biol. 74: 963–982. 72 Yamada, K. M., S. H. Ohanian & I. Pastan. 1976. Cell surface protein decreases microvilli and ruffles on transformed mouse and chick cells. Cell 9: 241–245. 73 Willingham, M. C., K. M. Yamada, S. S. Yamada, J. Pouyssegur & I. Pastan. 1977. Microfilament bundles and cell shape are related to adhesiveness to substratum and are dissociable from growth control in cultured fibroblasts. Cell 10: 375–380. 74 Goldman, R. D., C. Chang & J. F. Williams. 1974. Properties and behavior of hamster embryo cells transformed by human adenovirus 5. Cold Spring Harbor Symp. Quant. Biol. 39: 601–614. 75 Ukena, T. E. & M. J. Karnovsky. 1976. Patching, microvilli and the agglutination of normal and transformed cells. In Membranes and Neoplasia: New Approaches and Strategies. V. T. Marchesi, Ed.: 261–273. Alan R. Liss, Inc. New York , N.y. . 76 Tucker, R. W., K. K. Sanford & F. R. Frankel. 1977. Cell. In press. 77 Yamada, K. M., S. S. Yamada & I. Pastan. 1975. The major cell surface glycoprotein of chick embryo fibroblasts is an agglutinin. Proc. Nat. Acad. Sci. USA 72: 3158–3162. 78 Klebe, R. J. 1974. Isolation of a collagen-dependent cell attachment factor. Nature (London) 250: 248–251. 79 Grinnell, F. 1976. Cell spreading factor: occurrence and specificity of action. Exp. Cell Res. 102: 51–62. Citing Literature Volume312, Issue1Fibroblast Surface ProteinJune 1978Pages 317-342 ReferencesRelatedInformation

Referência(s)