Abstract
Cell surface labeling can cause rearrangements of randomly distributed membrane components. Removal of the label bound to the cell surface allows the membrane components to return to their original random distribution, demonstrating that label is necessary to maintain as well as to induce rearrangements. With scanning electron microscopy, the rearrangement of concanavalin A (con A) and ricin binding sites on LA-9 cells has been followed by means of hemocyanin, a visual label. The removal of con A from its binding sites at the cell surface with alpha- methyl mannoside, and the return of these sites to their original distribution are also followed in this manner. There are labeling differences with con A and ricin. Under some conditions, however, the same rearrangements are seen with both lectins. The disappearance of labeled sites from areas of ruffling activity is a major feature of the rearrangements seen. Both this ruffling activity and the rearrangement of label are sensitive to cytochalasin B, and ruffling activity, perhaps along with other cytochalasin-sensitive structure, may play a role in the rearrangements of labeled sites.
Full Text
The Full Text of this article is available as a PDF (3.9 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Abercrombie M., Heaysman J. E., Pegrum S. M. Locomotion of fibroblasts in culture. V. Surface marking with concanavalin A. Exp Cell Res. 1972 Aug;73(2):536–539. doi: 10.1016/0014-4827(72)90090-0. [DOI] [PubMed] [Google Scholar]
- Abercrombie M., Heaysman J. E., Pegrum S. M. The locomotion of fibroblasts in culture. 3. Movements of particles on the dorsal surface of the leading lamella. Exp Cell Res. 1970 Oct;62(2):389–398. doi: 10.1016/0014-4827(70)90570-7. [DOI] [PubMed] [Google Scholar]
- Abercrombie M., Heaysman J. E., Pegrum S. M. The locomotion of fibroblasts in culture. II. "RRuffling". Exp Cell Res. 1970 Jun;60(3):437–444. doi: 10.1016/0014-4827(70)90537-9. [DOI] [PubMed] [Google Scholar]
- Agrawal B. B., Goldstein I. J. Protein-carbohydrate interaction. VI. Isolation of concanavalin A by specific adsorption on cross-linked dextran gels. Biochim Biophys Acta. 1967 Oct 23;147(2):262–271. [PubMed] [Google Scholar]
- Bretton R., Wicker R., Bernhard W. Ultrastructural localization of concanavalin A receptors in normal and SV 40 -transformed hamster and rat cells. Int J Cancer. 1972 Sep 15;10(2):397–410. doi: 10.1002/ijc.2910100222. [DOI] [PubMed] [Google Scholar]
- Burnside B., Manasek F. J. Cytochalasin B: problems in interpretating its effect on cells. Dev Biol. 1972 Mar;27(3):443–444. doi: 10.1016/0012-1606(72)90184-4. [DOI] [PubMed] [Google Scholar]
- Carter S. B. The cytochalasins as research tools in cytology. Endeavour. 1972 May;31(113):77–82. [PubMed] [Google Scholar]
- DULBECCO R., VOGT M. Plaque formation and isolation of pure lines with poliomyelitis viruses. J Exp Med. 1954 Feb;99(2):167–182. doi: 10.1084/jem.99.2.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dahl D. R., Redburn D. A., Samson F. E., Jr Regional distribution of colchicine-binding (microtubular) protein in the rat brain. J Neurochem. 1970 Aug;17(8):1215–1219. doi: 10.1111/j.1471-4159.1970.tb03371.x. [DOI] [PubMed] [Google Scholar]
- De Petris S. Inhibition and reversal of capping by cytochalasin B, vinblastine and colchicine. Nature. 1974 Jul 5;250(461):54–56. doi: 10.1038/250054a0. [DOI] [PubMed] [Google Scholar]
- Drysdale R. G., Herrick P. R., Franks D. The specificity of the haemagglutinin of the Castor bean, Ricinus communis. Vox Sang. 1968;15(3):194–202. doi: 10.1111/j.1423-0410.1968.tb01749.x. [DOI] [PubMed] [Google Scholar]
- Edidin M. Two-dimensional diffusion in membranes. Symp Soc Exp Biol. 1974;(28):1–14. [PubMed] [Google Scholar]
- Edidin M., Weiss A. Antigen cap formation in cultured fibroblasts: a reflection of membrane fluidity and of cell motility. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2456–2459. doi: 10.1073/pnas.69.9.2456. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Everhart L. P., Jr, Rubin R. W. Cyclic changes in the cell surface. II. The effect of cytochalasin B on the surface morphology of synchronized Chinese hamster ovary cells. J Cell Biol. 1974 Feb;60(2):442–447. doi: 10.1083/jcb.60.2.442. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Feit H., Barondes S. H. Colchicine-binding activity in particulate fractions of mouse brain. J Neurochem. 1970 Sep;17(9):1355–1364. doi: 10.1111/j.1471-4159.1970.tb06870.x. [DOI] [PubMed] [Google Scholar]
- GOLDSTEIN I. J., HOLLERMAN C. E., MERRICK J. M. PROTEIN-CARBOHYDRATE INTERACTION. I. THE INTERACTION OF POLYSACCHARIDES WITH CONCANAVALIN A. Biochim Biophys Acta. 1965 Jan 4;97:68–76. doi: 10.1016/0304-4165(65)90270-9. [DOI] [PubMed] [Google Scholar]
- Goldman R. D. The effects of cytochalasin B on the microfilaments of baby hamster kidney (BHK-21) cells. J Cell Biol. 1972 Feb;52(2):246–254. doi: 10.1083/jcb.52.2.246. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Holtzer H., Sanger J. W. Cytochalasin-B: microfilaments, cell movement and what else? Dev Biol. 1972 Mar;27(3):444–446. [PubMed] [Google Scholar]
- Ingram V. M. A side view of moving fibroblasts. Nature. 1969 May 17;222(5194):641–644. doi: 10.1038/222641a0. [DOI] [PubMed] [Google Scholar]
- Karnovsky M. J., Unanue E. R. Mapping and migration of lymphocyte surface macromolecules. Fed Proc. 1973 Jan;32(1):55–59. [PubMed] [Google Scholar]
- Kourilsky F. M., Silvestre D., Neauport-Sautes C., Loosfelt Y., Dausset J. Antibody-induced redistribution of HL-A antigens at the cell surface. Eur J Immunol. 1972 Jun;2(3):249–257. doi: 10.1002/eji.1830020311. [DOI] [PubMed] [Google Scholar]
- Krishan A. Fine structure of cytochalasin-induced multinucleated cells. J Ultrastruct Res. 1971 Jul;36(1):191–204. doi: 10.1016/s0022-5320(71)80097-7. [DOI] [PubMed] [Google Scholar]
- LITTLEFIELD J. W. THREE DEGREES OF GUANYLIC ACID--INOSINIC ACID PYROPHOSPHORYLASE DEFICIENCY IN MOUSE FIBROBLASTS. Nature. 1964 Sep 12;203:1142–1144. doi: 10.1038/2031142a0. [DOI] [PubMed] [Google Scholar]
- 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]
- Lagnado J. R., Lyons C., Wickremasinghe G. The subcellular distribution of colchicine-binding protein ('microtubule protein') in rat brain. FEBS Lett. 1971 Jun 24;15(3):254–258. doi: 10.1016/0014-5793(71)80324-1. [DOI] [PubMed] [Google Scholar]
- Lieberman M., Manasek F. J., Sawanobori T., Johnson E. A. Cytochalasin B: its morphological and electrophysiological actions on synthetic strands of cardiac muscle. Dev Biol. 1973 Apr;31(2):380–403. doi: 10.1016/0012-1606(73)90273-x. [DOI] [PubMed] [Google Scholar]
- Loor F., Forni L., Pernis B. The dynamic state of the lymphocyte membrane. Factors affecting the distribution and turnover of surface immunoglobulins. Eur J Immunol. 1972 Jun;2(3):203–212. doi: 10.1002/eji.1830020304. [DOI] [PubMed] [Google Scholar]
- Mizel S. B., Wilson L. Nucleoside transport in mammalian cells. Inhibition by colchicine. Biochemistry. 1972 Jul 4;11(14):2573–2578. doi: 10.1021/bi00764a003. [DOI] [PubMed] [Google Scholar]
- Nemanic M. K., Carter D. P., Pitelka D. R., Wofsy L. Hapten-sandwich labeling. II. Immunospecific attachment of cell surface markers suitable for scanning electron microscopy. J Cell Biol. 1975 Feb;64(2):311–321. doi: 10.1083/jcb.64.2.311. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nicolson G. L., Blaustein J. The interaction of Ricinus communis agglutinin with normal and tumor cell surfaces. Biochim Biophys Acta. 1972 May 9;266(2):543–547. doi: 10.1016/0005-2736(72)90109-5. [DOI] [PubMed] [Google Scholar]
- Revel J. P. Contacts and junctions between cells. Symp Soc Exp Biol. 1974;(28):447–461. [PubMed] [Google Scholar]
- Rosenblith J. Z., Ukena T. E., Yin H. H., Berlin R. D., Karnovsky M. J. A comparative evaluation of the distribution of concanavalin A-binding sites on the surfaces of normal, virally-transformed, and protease-treated fibroblasts. Proc Natl Acad Sci U S A. 1973 Jun;70(6):1625–1629. doi: 10.1073/pnas.70.6.1625. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ryan G. B., Borysenko J. Z., Karnovsky M. J. Factors affecting the redistribution of surface-bound concanavalin A on human polymorphonuclear leukocytes. J Cell Biol. 1974 Aug;62(2):351–365. doi: 10.1083/jcb.62.2.351. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sanger J. W., Holtzer H. Cytochalasin B: effects on cell morphology, cell adhesion, and mucopolysaccharide synthesis (cultured cells-contractile microfilaments-glycoproteins-embryonic cells-sorting-out). Proc Natl Acad Sci U S A. 1972 Jan;69(1):253–257. doi: 10.1073/pnas.69.1.253. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Singer S. J., Nicolson G. L. The fluid mosaic model of the structure of cell membranes. Science. 1972 Feb 18;175(4023):720–731. doi: 10.1126/science.175.4023.720. [DOI] [PubMed] [Google Scholar]
- Smith S. B., Revel J. P. Mapping of concanavalin A binding sites on the surface of several cell types. Dev Biol. 1972 Mar;27(3):434–441. doi: 10.1016/0012-1606(72)90183-2. [DOI] [PubMed] [Google Scholar]
- Stackpole C. W., De Milio L. T., Hämmerling U., Jacobson J. B., Lardis M. P. Hybrid antibody-induced topographical redistribution of surface immunoglobulins, alloantigens, and concanavalin A receptors on mouse lymphoid cells. Proc Natl Acad Sci U S A. 1974 Mar;71(3):932–936. doi: 10.1073/pnas.71.3.932. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sundqvist K. G. Redistribution of surface antigens--a general property of animal cells? Nat New Biol. 1972 Oct 4;239(92):147–149. doi: 10.1038/newbio239147a0. [DOI] [PubMed] [Google Scholar]
- Sällström J. F., Alm G. V. Binding of concanavalin A to thymic and bursal chicken lymphoid cells. Exp Cell Res. 1972 Nov;75(1):63–72. doi: 10.1016/0014-4827(72)90520-4. [DOI] [PubMed] [Google Scholar]
- Taverna R. D., Langdon R. G. Reversible association of cytochalasin B with the human erythrocyte membrane. Inhibition of glucose transport and the stoichiometry of cytochalasin binding. Biochim Biophys Acta. 1973 Oct 11;323(2):207–219. doi: 10.1016/0005-2736(73)90145-4. [DOI] [PubMed] [Google Scholar]
- Triche T. J., Tillack T. W., Kornfeld S. Localization of the binding sites for the Ricinus communis, Agaricus bisporus and wheat germ lectins on human erythrocyte membranes. Biochim Biophys Acta. 1975 Jul 18;394(4):540–549. doi: 10.1016/0005-2736(75)90139-x. [DOI] [PubMed] [Google Scholar]
- Unanue E. R., Karnovsky M. J., Engers H. D. Ligand-induced movement of lymphocyte membrane macromolecules. 3. Relationship between the formation and fate of anti-Ig-surface Ig complexes and cell metabolism. J Exp Med. 1973 Mar 1;137(3):675–689. doi: 10.1084/jem.137.3.675. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Unanue E. R., Karnovsky M. J. Ligand-induced movement of lymphocyte membrane macromolecules. V. Capping, cell movement, and microtubular function in normal and lectin-treated lymphocytes. J Exp Med. 1974 Nov 1;140(5):1207–1220. doi: 10.1084/jem.140.5.1207. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weller N. K. Visualization of concanavalin A-binding sites with scanning electron microscopy. J Cell Biol. 1974 Nov;63(2 Pt 1):699–707. doi: 10.1083/jcb.63.2.699. [DOI] [PMC free article] [PubMed] [Google Scholar]
- de Petris S., Raff M. C. Distribution of immunoglobulin on the surface of mouse lymphoid cells as determined by immunoferritin electron microscopy. Antibody-induced, temperature-dependent redistribution and its implications for membrane structure. Eur J Immunol. 1972 Dec;2(6):523–535. doi: 10.1002/eji.1830020611. [DOI] [PubMed] [Google Scholar]
- de Petris S., Raff M. C. Normal distribution, patching and capping of lymphocyte surface immunoglobulin studied by electron microscopy. Nat New Biol. 1973 Feb 28;241(113):257–259. doi: 10.1038/newbio241257a0. [DOI] [PubMed] [Google Scholar]